<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Monge, N.</style></author><author><style face="normal" font="default" size="100%">Pinto, LFV</style></author><author><style face="normal" font="default" size="100%">Ferreira, E</style></author><author><style face="normal" font="default" size="100%">Almeida, PL</style></author><author><style face="normal" font="default" size="100%">Figueirinhas, J. L.</style></author><author><style face="normal" font="default" size="100%">Carvalho, AL</style></author><author><style face="normal" font="default" size="100%">Sebastião, PJ</style></author><author><style face="normal" font="default" size="100%">Godinho, M. H.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Hierarchical Twist: Chirality Across Scales in Cellulose Cholesterics</style></title><secondary-title><style face="normal" font="default" size="100%">Advanced Optical MaterialsAdvanced Optical Materials</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">chiral nematic liquid crystals</style></keyword><keyword><style  face="normal" font="default" size="100%">hierarchical twisted supramolecular structures</style></keyword><keyword><style  face="normal" font="default" size="100%">mechanoresponsive materials</style></keyword><keyword><style  face="normal" font="default" size="100%">thermotropic cellulose derivatives</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2026</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2026</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://doi.org/10.1002/adom.202502728</style></url></web-urls></urls><publisher><style face="normal" font="default" size="100%">John Wiley &amp; Sons, Ltd</style></publisher><volume><style face="normal" font="default" size="100%">14</style></volume><pages><style face="normal" font="default" size="100%">e02728</style></pages><isbn><style face="normal" font="default" size="100%">2195-1071</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Abstract One of the unresolved aspects of cellulose-based liquid crystalline phases is their chirality. Although cellulose is intrinsically chiral, both left-handed (LH) and right-handed (RH) chiral nematic phases are reported in cellulose derivatives under different conditions. The origin of these discrepancies?and whether LH and RH twisted structures coexist within a single material?has remained unclear. Here, the first direct evidence of hierarchical LH and RH twisted structures coexisting in a solvent-free, thermotropic cellulose derivative at room temperature is provided. Free-standing cholesteric films exhibit distinct LH and RH twisted domains, whose pitches respond oppositely to uniaxial mechanical strain: the LH pitch increases, while the RH pitch decreases with increasing strain. This contrasting response results from the coexistence of intertwined LH and RH twisted structures, whose optical axes are oriented differently relative to the strain direction. Notably, after stretching beyond their elastic limit, the films spontaneously recover their original shape within minutes. During this recovery, circular dichroism (CD) measurements reveal an increase in RH pitch and a decrease in LH pitch, evidencing reversible, strain-responsive behavior. Multiscale structural characterization confirms the hierarchical chiral organization and its mechanoresponsive nature, providing new insights into the origin of chirality in cellulose-based liquid crystalline materials.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Simões, Rita S.M.</style></author><author><style face="normal" font="default" size="100%">Teodoro, João S.</style></author><author><style face="normal" font="default" size="100%">Alves, Victor D.</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Bule, Pedro</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Noncatalytic surface electrostatic networks tune thermolability in uracil-DNA glycosylase</style></title></titles><keywords><keyword><style  face="normal" font="default" size="100%">carryover contamination</style></keyword><keyword><style  face="normal" font="default" size="100%">electrostatics</style></keyword><keyword><style  face="normal" font="default" size="100%">enzyme inactivation</style></keyword><keyword><style  face="normal" font="default" size="100%">enzyme mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">enzyme structure</style></keyword><keyword><style  face="normal" font="default" size="100%">psychrophilic enzymes</style></keyword><keyword><style  face="normal" font="default" size="100%">site-directed mutagenesis</style></keyword><keyword><style  face="normal" font="default" size="100%">thermolability</style></keyword><keyword><style  face="normal" font="default" size="100%">thermostability</style></keyword><keyword><style  face="normal" font="default" size="100%">uracil-DNA glycosylase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2026</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2026</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.sciencedirect.com/science/article/pii/S0021925826020843</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">302</style></volume><pages><style face="normal" font="default" size="100%">113212</style></pages><isbn><style face="normal" font="default" size="100%">0021-9258</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Uracil-DNA glycosylases (UDGs) are widely used to prevent carryover contamination in nucleic acid amplification–based diagnostics; however, existing thermolabile UDGs exhibit limited thermal inactivation windows for emerging applications. Here, we combine evolutionary mining, structural analysis, and structure-guided saturation mutagenesis to define non-catalytic determinants that tune UDG thermolability without compromising catalytic function. From 8482 bacterial UDG sequences, we assembled a 24-member diversity panel and identified UDG_7 as a naturally thermolabile scaffold coupling robust low-temperature activity with sharp inactivation near 45 °C. The crystal structure of UDG_7 reveals a canonical family-I α/β fold with a fully conserved active site, closely resembling both mesophilic human and Escherichia coli UDGs and thermolabile cod UDG. These structural insights guided the design of a single-site variant library targeting 48 non-catalytic positions involved in packing and electrostatic networks. Pooled thermal shift assays distinguished a rigid structural core from 16 surface thermolability hotspots. A high-throughput functional screening of 480 single mutants yielded 114 clones with a desirable “on–off–off” profile and, after sequence consolidation, identified 54 unique variants that retained activity at 25 °C but lost activity at 30 to 37.5 °C. Biochemical characterization revealed nine single substitutions, Q51I, T112Y, V144M, D167F, R201F, R201Y, D219M, R221P, and R221D, that markedly lower the melting temperature while preserving near-native activity. Together, these results indicate that UDG_7 thermolability is encoded by a distributed, surface-biased electrostatic network that can be selectively disrupted without perturbing the conserved catalytic core, shifting the functional inactivation boundary downward and supporting robust carryover control under low-temperature amplification constraints.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">7</style></issue><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Marlene Duarte</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Ferreira, Magda C.</style></author><author><style face="normal" font="default" size="100%">Caires, Beatriz</style></author><author><style face="normal" font="default" size="100%">Romão, Maria João</style></author><author><style face="normal" font="default" size="100%">Prates, José A. M.</style></author><author><style face="normal" font="default" size="100%">Najmudin, Shabir</style></author><author><style face="normal" font="default" size="100%">Bayer, Edward A.</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos MGA.</style></author><author><style face="normal" font="default" size="100%">Bule, Pedro</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Tripartite binding mode of cohesin-dockerin complexes from Ruminococcus flavefaciens involving naturally truncated dockerins</style></title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Carbohydrates</style></keyword><keyword><style  face="normal" font="default" size="100%">cellulosome</style></keyword><keyword><style  face="normal" font="default" size="100%">cohesin</style></keyword><keyword><style  face="normal" font="default" size="100%">dockerin</style></keyword><keyword><style  face="normal" font="default" size="100%">protein assembly</style></keyword><keyword><style  face="normal" font="default" size="100%">protein complex</style></keyword><keyword><style  face="normal" font="default" size="100%">protein structure</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2025</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2025</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.sciencedirect.com/science/article/pii/S0021925825021751</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">301</style></volume><pages><style face="normal" font="default" size="100%">110325</style></pages><isbn><style face="normal" font="default" size="100%">0021-9258</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Polysaccharides in plant cell walls serve as a rich carbon and energy source, yet their structural complexity presents a barrier to efficient degradation. To address this, anaerobic microorganisms like R. flavefaciens have developed sophisticated multi-enzyme complexes known as cellulosomes, which enable the efficient breakdown of these recalcitrant polysaccharides. These complexes are assembled through high-affinity interactions between cohesin (Coh) modules in scaffoldin proteins and dockerin (Doc) modules in cellulosomal enzymes. R. flavefaciens FD-1 harbors one of the most intricate cellulosomes described to date, comprising over 200 Doc-containing proteins encoded in its genome. Despite substantial research on this cellulosome, the role of a group of truncated but functional dockerins, known as group-2 Docs, remains unclear. In this study, we present a detailed structural and binding analysis of a Coh-Doc complex involving the cohesin from the cell-anchoring scaffoldin ScaE and a group-2 Doc that bears only one of the two Ca+2-coordinating loops that characterise the canonical Docs. Our findings reveal a novel tripartite binding mechanism, in which the cohesin can simultaneously bind two distinct dockerin units in three alternative conformations. This discovery provides new insights into the modular versatility of the R. flavefaciens cellulosome and sheds light on the mechanisms that enhance its efficiency in polysaccharide degradation.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">7</style></issue><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Caseiro, Catarina</style></author><author><style face="normal" font="default" size="100%">McGregor, Nicholas G.S.</style></author><author><style face="normal" font="default" size="100%">Alves, Victor Diogo</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Romão, Maria João</style></author><author><style face="normal" font="default" size="100%">Davies, Gideon J.</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Bule, Pedro</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Family GH157 enzyme exhibits broad linkage tolerance and a dual endo/exo- β -glucanase activity on β-glucans</style></title></titles><keywords><keyword><style  face="normal" font="default" size="100%">CAZYme</style></keyword><keyword><style  face="normal" font="default" size="100%">Endo-1,3(4)-β-glucanase</style></keyword><keyword><style  face="normal" font="default" size="100%">GH157</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycoside hydrolase</style></keyword><keyword><style  face="normal" font="default" size="100%">β-Glucans</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2024</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2024</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.sciencedirect.com/science/article/pii/S0141813024082114</style></url></web-urls></urls><pages><style face="normal" font="default" size="100%">137402</style></pages><isbn><style face="normal" font="default" size="100%">0141-8130</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The structural and chemical diversity of β-glucans is reflected on the variety of essential biological roles tackled by these polysaccharides. This natural heterogeneity requires an elaborate assortment of enzymatic mechanisms to assemble, degrade or modify, as well as to extract their full biotechnological potential. Recent metagenomic efforts have provided an unprecedented growth in potential new biocatalysts, most of which remain unconfirmed or uncharacterized. Here we report the first biochemical and structural characterization of two bacterial β-glucanases from the recently created glycoside hydrolase family 157 (LaGH157 and BcGH157) and investigate their molecular basis for substrate hydrolysis. Structural analysis by X-ray crystallography revealed that GH157 enzymes belong to clan GH-A, possessing a (β/α)8-barrel fold catalytic domain, two β-sandwich accessory domains and two conserved catalytic glutamates residues, with relative positions compatible with a retaining mechanism of hydrolysis. Specificity screening and enzyme kinetics suggest that the enzymes prefer mixed-linkage glucans over β-1,3-glucans. Activity screening showed that both enzymes exhibit pH optimum at 6.5 and temperature optimum for LaGH157 and BcGH157 at 25 °C and 48 °C, respectively. Product analysis with HPAEC-PAD and LC-MS revealed that both enzymes are endo-1,3(4)-β-glucanases, capable of cleaving β-1,3 and β-1,4-linked glucoses, when preceded by a β-1,3 linkage. Moreover, BcGH157 needs a minimum of 4 subsites occupied for hydrolysis to occur, while LaGH157 only requires 3 subsites. Additionally, LaGH157 possesses exohydrolytic activity on β-1,3 and branching β-1,6 linkages. This unusual bifunctional endo-1,3(4)/exo-1,3–1,6 activity constitutes an expansion on our understanding of β-glucan deconstruction, with the potential to inspire future applications.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Silva, José Malanho</style></author><author><style face="normal" font="default" size="100%">Cerofolini, Linda</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Ravera, Enrico</style></author><author><style face="normal" font="default" size="100%">Fragai, Marco</style></author><author><style face="normal" font="default" size="100%">Parigi, Giacomo</style></author><author><style face="normal" font="default" size="100%">Macedo, Anjos L</style></author><author><style face="normal" font="default" size="100%">Geraldes, Carlos F.G.C.</style></author><author><style face="normal" font="default" size="100%">Luchinat, Claudio</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Elucidating the concentration-dependent effects of thiocyanate binding to carbonic anhydrase</style></title></titles><keywords><keyword><style  face="normal" font="default" size="100%">EPR</style></keyword><keyword><style  face="normal" font="default" size="100%">Human carbonic anhydrase II</style></keyword><keyword><style  face="normal" font="default" size="100%">NMR</style></keyword><keyword><style  face="normal" font="default" size="100%">Paramagnetism</style></keyword><keyword><style  face="normal" font="default" size="100%">Sodium thiocyanate</style></keyword><keyword><style  face="normal" font="default" size="100%">Structural biology</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2023</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.sciencedirect.com/science/article/pii/S0162013423001046</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">244</style></volume><pages><style face="normal" font="default" size="100%">112222</style></pages><isbn><style face="normal" font="default" size="100%">0162-0134</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Many proteins naturally carry metal centers, with a large share of them being in the active sites of several enzymes. Paramagnetic effects are a powerful source of structural information and, therefore, if the native metal is paramagnetic, or it can be functionally substituted with a paramagnetic one, paramagnetic effects can be used to study the metal sites, as well as the overall structure of the protein. One notable example is cobalt(II) substitution for zinc(II) in carbonic anhydrase. In this manuscript we investigate the effects of sodium thiocyanate on the chemical environment of the metal ion of the human carbonic anhydrase II. The electron paramagnetic resonance (EPR) titration of the cobalt(II) protein with thiocyanate shows that the EPR spectrum changes from A-type to C-type on passing from 1:1 to 1:1000-fold ligand excess. This indicates the occurrence of a change in the electronic structure, which may reflect a sizable change in the metal coordination environment in turn caused by a modification of the frozen solvent glass. However, paramagnetic nuclear magnetic resonance (NMR) data indicate that the metal coordination cage remains unperturbed even in 1:1000-fold ligand excess. This result proves that the C-type EPR spectrum observed at large ligand concentration should be ascribed to the low temperature at which EPR measurements are performed, which impacts on the structure of the protein when it is destabilized by a high concentration of a chaotropic agent.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Marlene Duarte</style></author><author><style face="normal" font="default" size="100%">Alves, Victor D.</style></author><author><style face="normal" font="default" size="100%">Correia, Márcia</style></author><author><style face="normal" font="default" size="100%">Caseiro, Catarina</style></author><author><style face="normal" font="default" size="100%">Ferreira, Luís M A</style></author><author><style face="normal" font="default" size="100%">Romão, Maria João</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Najmudin, Shabir</style></author><author><style face="normal" font="default" size="100%">Bayer, Edward A.</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Bule, Pedro</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assemblies</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Biological Macromolecules</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biomass degradation</style></keyword><keyword><style  face="normal" font="default" size="100%">Carbohydrates</style></keyword><keyword><style  face="normal" font="default" size="100%">cellulosome</style></keyword><keyword><style  face="normal" font="default" size="100%">cohesin</style></keyword><keyword><style  face="normal" font="default" size="100%">dockerin</style></keyword><keyword><style  face="normal" font="default" size="100%">protein complex</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.sciencedirect.com/science/article/pii/S0141813022023480</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">224</style></volume><pages><style face="normal" font="default" size="100%">55-67</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The cellulosome is an elaborate multi-enzyme structure secreted by many anaerobic microorganisms for the efficient degradation of lignocellulosic substrates. It is composed of multiple catalytic and non-catalytic components that are assembled through high-affinity protein-protein interactions between the enzyme-borne dockerin (Doc) modules and the repeated cohesin (Coh) modules present in primary scaffoldins. In some cellulosomes, primary scaffoldins can interact with adaptor and cell-anchoring scaffoldins to create structures of increasing complexity. The cellulosomal system of the ruminal bacterium, Ruminococcus flavefaciens, is one of the most intricate described to date. An unprecedent number of different Doc specificities results in an elaborate architecture, assembled exclusively through single-binding-mode type-III Coh-Doc interactions. However, a set of type-III Docs exhibits certain features associated with the classic dual-binding mode Coh-Doc interaction. Here, the structure of the adaptor scaffoldin-borne ScaH Doc in complex with the Coh from anchoring scaffoldin ScaE is described. This complex, unlike previously described type-III interactions in R. flavefaciens, was found to interact in a dual-binding mode. The key residues determining Coh recognition were also identified. This information was used to perform structure-informed protein engineering to change the electrostatic profile of the binding surface and to improve the affinity between the two modules. The results show that the nature of the residues in the ligand-binding surface plays a major role in Coh recognition and that Coh-Doc affinity can be manipulated through rational design, a key feature for the creation of designer cellulosomes or other affinity-based technologies using tailored Coh-Doc interactions.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Correia Viviana G.</style></author><author><style face="normal" font="default" size="100%">Trovão Filipa</style></author><author><style face="normal" font="default" size="100%">Pinheiro Benedita A.</style></author><author><style face="normal" font="default" size="100%">Brás Joana L. A.</style></author><author><style face="normal" font="default" size="100%">Silva Lisete M.</style></author><author><style face="normal" font="default" size="100%">Nunes Cláudia</style></author><author><style face="normal" font="default" size="100%">Coimbra Manuel A.</style></author><author><style face="normal" font="default" size="100%">Liu Yan</style></author><author><style face="normal" font="default" size="100%">Feizi Ten</style></author><author><style face="normal" font="default" size="100%">Fontes Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Mulloy Barbara</style></author><author><style face="normal" font="default" size="100%">Chai Wengang</style></author><author><style face="normal" font="default" size="100%">Carvalho Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Palma Angelina S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Mapping Molecular Recognition of β1,3-1,4-Glucans by a Surface Glycan-Binding Protein from the Human Gut Symbiont Bacteroides ovatus</style></title><secondary-title><style face="normal" font="default" size="100%">Microbiology SpectrumMicrobiology Spectrum</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2021</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://doi.org/10.1128/Spectrum.01826-21</style></url></web-urls></urls><publisher><style face="normal" font="default" size="100%">American Society for Microbiology</style></publisher><pages><style face="normal" font="default" size="100%">e01826-21</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;n/a&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">&lt;p&gt;doi: 10.1128/Spectrum.01826-21&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Marlene Duarte</style></author><author><style face="normal" font="default" size="100%">Viegas, Aldino</style></author><author><style face="normal" font="default" size="100%">Alves, Victor D.</style></author><author><style face="normal" font="default" size="100%">Prates, José A. M.</style></author><author><style face="normal" font="default" size="100%">Ferreira, Luís M A</style></author><author><style face="normal" font="default" size="100%">Najmudin, Shabir</style></author><author><style face="normal" font="default" size="100%">Cabrita, Eurico J.</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Bule, Pedro</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">A dual cohesin–dockerin complex binding mode in Bacteroides cellulosolvens contributes to the size and complexity of its cellulosome</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Biological Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">cellulase</style></keyword><keyword><style  face="normal" font="default" size="100%">cellulose</style></keyword><keyword><style  face="normal" font="default" size="100%">cellulosome</style></keyword><keyword><style  face="normal" font="default" size="100%">cohesin</style></keyword><keyword><style  face="normal" font="default" size="100%">crystal structure</style></keyword><keyword><style  face="normal" font="default" size="100%">dockerin</style></keyword><keyword><style  face="normal" font="default" size="100%">dual-binding</style></keyword><keyword><style  face="normal" font="default" size="100%">protein complex</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2021</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.sciencedirect.com/science/article/pii/S0021925821003306</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">296</style></volume><pages><style face="normal" font="default" size="100%">100552</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The Cellulosome is an intricate macromolecular protein complex that centralizes the cellulolytic efforts of many anaerobic microorganisms through the promotion of enzyme synergy and protein stability. The assembly of numerous carbohydrate processing enzymes into a macromolecular multiprotein structure results from the interaction of enzyme-borne dockerin modules with repeated cohesin modules present in noncatalytic scaffold proteins, termed scaffoldins. Cohesin–dockerin (Coh-Doc) modules are typically classified into different types, depending on structural conformation and cellulosome role. Thus, type I Coh-Doc complexes are usually responsible for enzyme integration into the cellulosome, while type II Coh-Doc complexes tether the cellulosome to the bacterial wall. In contrast to other known cellulosomes, cohesin types from Bacteroides cellulosolvens, a cellulosome-producing bacterium capable of utilizing cellulose and cellobiose as carbon sources, are reversed for all scaffoldins, i.e., the type II cohesins are located on the enzyme-integrating primary scaffoldin, whereas the type I cohesins are located on the anchoring scaffoldins. It has been previously shown that type I B. cellulosolvens interactions possess a dual-binding mode that adds flexibility to scaffoldin assembly. Herein, we report the structural mechanism of enzyme recruitment into B. cellulosolvens cellulosome and the identification of the molecular determinants of its type II cohesin–dockerin interactions. The results indicate that, unlike other type II complexes, these possess a dual-binding mode of interaction, akin to type I complexes. Therefore, the plasticity of dual-binding mode interactions seems to play a pivotal role in the assembly of B. cellulosolvens cellulosome, which is consistent with its unmatched complexity and size.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Goodfellow, Brian J.</style></author><author><style face="normal" font="default" size="100%">Freire, Filipe</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Aveiro, Susana S.</style></author><author><style face="normal" font="default" size="100%">Charbonnier, Peggy</style></author><author><style face="normal" font="default" size="100%">Moulis, Jean-Marc</style></author><author><style face="normal" font="default" size="100%">Delgado, Leonildo</style></author><author><style face="normal" font="default" size="100%">Ferreira, Gloria C</style></author><author><style face="normal" font="default" size="100%">Rodrigues, João E</style></author><author><style face="normal" font="default" size="100%">Poussin-Courmontagne, Pierre</style></author><author><style face="normal" font="default" size="100%">Birck, Catherine</style></author><author><style face="normal" font="default" size="100%">McEwen, Alastair</style></author><author><style face="normal" font="default" size="100%">Macedo, Anjos L</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">{The SOUL family of heme-binding proteins: Structure and function 15 years later}</style></title><secondary-title><style face="normal" font="default" size="100%">Coordination Chemistry Reviews</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Function</style></keyword><keyword><style  face="normal" font="default" size="100%">HEBP1</style></keyword><keyword><style  face="normal" font="default" size="100%">HEBP2</style></keyword><keyword><style  face="normal" font="default" size="100%">NMR spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">SOUL protein</style></keyword><keyword><style  face="normal" font="default" size="100%">Structure</style></keyword><keyword><style  face="normal" font="default" size="100%">X-ray crystallography</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2021</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.sciencedirect.com/science/article/pii/S001085452100463X</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">448</style></volume><pages><style face="normal" font="default" size="100%">214189</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The SOUL, or heme-binding protein HBP/SOUL, family represents a group of evolutionary conserved putative heme-binding proteins that contains a number of members in animal, plant andbacterial species. The structures of the murine form of HEBP1, or p22HBP, and the human form of HEBP2, or SOUL, have been determined in 2006 and 2011 respectively. In this work we discuss the structures of HEBP1 and HEBP2 in light of new X-ray data for heme bound murine HEBP1. The interaction between tetrapyrroles and HEBP1, initially proven to be hydrophobic in nature, was thought to also involve electrostatic interactions between heme propionate groups and positively charged amino acid side chains. However, the new X-ray structure, and results from murine HEBP1 variants and human HEBP1, confirm the hydrophobic nature of the heme-HEBP1 interaction, resulting in Kd values in the low nanomolar range, and rules out any electrostatic stabilization. Results from NMR relaxation time measurements for human HEBP1 describe a rigid globular protein with no change in motional regime upon heme binding. X-ray structures deposited in the PDB for human HEBP2 are very similar to each other and to the new heme-bound murine HEBP1 X-ray structure (backbone rmsd ca. 1 {\AA}). Results from a HSQC spectrum centred on the histidine side chain N$δ$-proton region for HEBP2 confirm that HEBP2 does not bind heme via H42 as no chemical shift differences were observed upon heme addition for backbone NH and N$δ$ protons. A survey of the functions attributed to HEBP1 and HEBP2 over the last 20 years span a wide range of cellular pathways. Interestingly, many of them are specific to higher eukaryotes, particularly mammals and a potential link between heme release under oxidative stress and human HEBP1 is also examined using recent data. However, at the present moment, trying to relate function to the involvement of heme or tetrapyrrole binding, specifically, makes little sense with our current biological knowledge and can only be applied to HEBP1, as HEBP2 does not interact with heme. We suggest that it may not be justified to call this very small family of proteins, heme-binding proteins. The family may be more correctly called “the SOUL family of proteins related to cellular fate” as, even though only HEBP1 binds heme tightly, both proteins may be involved in cell survival and/or proliferation.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Gomes, Ana Sara</style></author><author><style face="normal" font="default" size="100%">Ramos, Helena</style></author><author><style face="normal" font="default" size="100%">Gomes, Sara</style></author><author><style face="normal" font="default" size="100%">Loureiro, Joana B.</style></author><author><style face="normal" font="default" size="100%">Soares, Joana</style></author><author><style face="normal" font="default" size="100%">Barcherini, Valentina</style></author><author><style face="normal" font="default" size="100%">Monti, Paola</style></author><author><style face="normal" font="default" size="100%">Fronza, Gilberto</style></author><author><style face="normal" font="default" size="100%">Oliveira, Carla</style></author><author><style face="normal" font="default" size="100%">Domingues, Lucília</style></author><author><style face="normal" font="default" size="100%">Bastos, Margarida</style></author><author><style face="normal" font="default" size="100%">Dourado, Daniel F.A.R.</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Romão, Maria João</style></author><author><style face="normal" font="default" size="100%">Pinheiro, Benedita</style></author><author><style face="normal" font="default" size="100%">Marcelo, Filipa</style></author><author><style face="normal" font="default" size="100%">Carvalho, Alexandra</style></author><author><style face="normal" font="default" size="100%">Santos, Maria M.M.</style></author><author><style face="normal" font="default" size="100%">Saraiva, Lucília</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">SLMP53-1 interacts with wild-type and mutant p53 DNA-binding domain and reactivates multiple hotspot mutations</style></title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cancer</style></keyword><keyword><style  face="normal" font="default" size="100%">Chemotherapy</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutant</style></keyword><keyword><style  face="normal" font="default" size="100%">p53</style></keyword><keyword><style  face="normal" font="default" size="100%">Reactivator</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2020</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.sciencedirect.com/science/article/pii/S0304416519302260</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">1864</style></volume><pages><style face="normal" font="default" size="100%">129440</style></pages><isbn><style face="normal" font="default" size="100%">0304-4165</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;BackgroundHalf of human cancers harbour TP53 mutations that render p53 inactive as a tumor suppressor. As such, reactivation of mutant (mut)p53 through restoration of wild-type (wt)-like function represents one of the most promising therapeutic strategies in cancer treatment. Recently, we have reported the (S)-tryptophanol-derived oxazoloisoindolinone SLMP53-1 as a new reactivator of wt and mutp53 R280K with in vitro and in vivo p53-dependent antitumor activity. The present work aimed a mechanistic elucidation of mutp53 reactivation by SLMP53-1.&lt;br /&gt;
Methods and results&lt;br /&gt;
By cellular thermal shift assay (CETSA), it is shown that SLMP53-1 induces wt and mutp53 R280K thermal stabilization, which is indicative of intermolecular interactions with these proteins. Accordingly, in silico studies of wt and mutp53 R280K DNA-binding domain with SLMP53-1 unveiled that the compound binds at the interface of the p53 homodimer with the DNA minor groove. Additionally, using yeast and p53-null tumor cells ectopically expressing distinct highly prevalent mutp53, the ability of SLMP53-1 to reactivate multiple mutp53 is evidenced.&lt;br /&gt;
Conclusions&lt;br /&gt;
SLMP53-1 is a p53-activating agent with the ability to directly target wt and a set of hotspot mutp53.&lt;br /&gt;
General Significance&lt;br /&gt;
This work reinforces the encouraging application of SLMP53-1 in the personalized treatment of cancer patients harboring distinct p53 status.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ribeiro, Diana O.</style></author><author><style face="normal" font="default" size="100%">Viegas, Aldino</style></author><author><style face="normal" font="default" size="100%">Pires, Virgínia M R</style></author><author><style face="normal" font="default" size="100%">Medeiros-Silva, João</style></author><author><style face="normal" font="default" size="100%">Bule, Pedro</style></author><author><style face="normal" font="default" size="100%">Chai, Wengang</style></author><author><style face="normal" font="default" size="100%">Marcelo, Filipa</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Cabrita, Eurico J.</style></author><author><style face="normal" font="default" size="100%">Palma, Angelina S.</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Molecular basis for the preferential recognition of β1,3-1,4-glucans by the family 11 carbohydrate-binding module from Clostridium thermocellum</style></title><secondary-title><style face="normal" font="default" size="100%">The FEBS Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">3-1</style></keyword><keyword><style  face="normal" font="default" size="100%">4-mixed-linked glucans</style></keyword><keyword><style  face="normal" font="default" size="100%">carbohydrate specificity</style></keyword><keyword><style  face="normal" font="default" size="100%">carbohydrate-binding module</style></keyword><keyword><style  face="normal" font="default" size="100%">cellulosome</style></keyword><keyword><style  face="normal" font="default" size="100%">Clostridium thermocellum</style></keyword><keyword><style  face="normal" font="default" size="100%">β1</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://febs.onlinelibrary.wiley.com/doi/abs/10.1111/febs.15162</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">13</style></number><volume><style face="normal" font="default" size="100%">287</style></volume><pages><style face="normal" font="default" size="100%">2723-2743</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Understanding the specific molecular interactions between proteins and β1,3-1,4-mixed-linked d-glucans is fundamental to harvest the full biological and biotechnological potential of these carbohydrates and of proteins that specifically recognize them. The family 11 carbohydrate-binding module from Clostridium thermocellum (CtCBM11) is known for its binding preference for β1,3-1,4-mixed-linked over β1,4-linked glucans. Despite the growing industrial interest of this protein for the biotransformation of lignocellulosic biomass, the molecular determinants of its ligand specificity are not well defined. In this report, a combined approach of methodologies was used to unravel, at a molecular level, the ligand recognition of CtCBM11. The analysis of the interaction by carbohydrate microarrays and NMR and the crystal structures of CtCBM11 bound to β1,3-1,4-linked glucose oligosaccharides showed that both the chain length and the position of the β1,3-linkage are important for recognition, and identified the tetrasaccharide Glcβ1,4Glcβ1,4Glcβ1,3Glc sequence as a minimum epitope required for binding. The structural data, along with site-directed mutagenesis and ITC studies, demonstrated the specificity of CtCBM11 for the twisted conformation of β1,3-1,4-mixed-linked glucans. This is mediated by a conformation–selection mechanism of the ligand in the binding cleft through CH-π stacking and a hydrogen bonding network, which is dependent not only on ligand chain length, but also on the presence of a β1,3-linkage at the reducing end and at specific positions along the β1,4-linked glucan chain. The understanding of the detailed mechanism by which CtCBM11 can distinguish between linear and mixed-linked β-glucans strengthens its exploitation for the design of new biomolecules with improved capabilities and applications in health and agriculture. Database Structural data are available in the Protein Data Bank under the accession codes 6R3M and 6R31.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Peixoto, Daniela</style></author><author><style face="normal" font="default" size="100%">Malta, Gabriela</style></author><author><style face="normal" font="default" size="100%">Cruz, Hugo</style></author><author><style face="normal" font="default" size="100%">Barroso, Sónia</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Ferreira, Luísa M.</style></author><author><style face="normal" font="default" size="100%">Paula S. Branco</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">N-Heterocyclic Olefin Catalysis for the Ring Opening of Cyclic Amidine Compounds: A Pathway to the Synthesis of ε-Caprolactam- and γ-Lactam-Derived Amines</style></title><secondary-title><style face="normal" font="default" size="100%">The Journal of Organic ChemistryThe Journal of Organic Chemistry</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2019</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://doi.org/10.1021/acs.joc.8b02823</style></url></web-urls></urls><publisher><style face="normal" font="default" size="100%">American Chemical Society</style></publisher><isbn><style face="normal" font="default" size="100%">0022-3263</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">n/a</style></abstract><notes><style face="normal" font="default" size="100%">&lt;p&gt;doi: 10.1021/acs.joc.8b02823&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Bule, Pedro</style></author><author><style face="normal" font="default" size="100%">Pires, Virgínia M R</style></author><author><style face="normal" font="default" size="100%">Alves, Victor D.</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Prates, José A. M.</style></author><author><style face="normal" font="default" size="100%">Ferreira, Luís M A</style></author><author><style face="normal" font="default" size="100%">Smith, Steven P.</style></author><author><style face="normal" font="default" size="100%">Gilbert, Harry J.</style></author><author><style face="normal" font="default" size="100%">Noach, Ilit</style></author><author><style face="normal" font="default" size="100%">Bayer, Edward A.</style></author><author><style face="normal" font="default" size="100%">Najmudin, Shabir</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction</style></title><secondary-title><style face="normal" font="default" size="100%">Scientific Reports</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2018</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://doi.org/10.1038/s41598-018-25171-8</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">8</style></volume><pages><style face="normal" font="default" size="100%">6987</style></pages><isbn><style face="normal" font="default" size="100%">2045-2322</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Cellulosomes are highly sophisticated molecular nanomachines that participate in the deconstruction of complex polysaccharides, notably cellulose and hemicellulose. Cellulosomal assembly is orchestrated by the interaction of enzyme-borne dockerin (Doc) modules to tandem cohesin (Coh) modules of a non-catalytic primary scaffoldin. In some cases, as exemplified by the cellulosome of the major cellulolytic ruminal bacterium Ruminococcus flavefaciens, primary scaffoldins bind to adaptor scaffoldins that further interact with the cell surface via anchoring scaffoldins, thereby increasing cellulosome complexity. Here we elucidate the structure of the unique Doc of R. flavefaciens FD-1 primary scaffoldin ScaA, bound to Coh 5 of the adaptor scaffoldin ScaB. The RfCohScaB5-DocScaA complex has an elliptical architecture similar to previously described complexes from a variety of ecological niches. ScaA Doc presents a single-binding mode, analogous to that described for the other two Coh-Doc specificities required for cellulosome assembly in R. flavefaciens. The exclusive reliance on a single-mode of Coh recognition contrasts with the majority of cellulosomes from other bacterial species described to date, where Docs contain two similar Coh-binding interfaces promoting a dual-binding mode. The discrete Coh-Doc interactions observed in ruminal cellulosomes suggest an adaptation to the exquisite properties of the rumen environment.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><notes><style face="normal" font="default" size="100%">&lt;p&gt;n/a&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Paula S. Branco</style></author><author><style face="normal" font="default" size="100%">Peixoto, Daniela</style></author><author><style face="normal" font="default" size="100%">Figueiredo, Margarida</style></author><author><style face="normal" font="default" size="100%">Malta, Gabriela</style></author><author><style face="normal" font="default" size="100%">Roma-Rodrigues, Catarina</style></author><author><style face="normal" font="default" size="100%">Batista, Pedro Viana</style></author><author><style face="normal" font="default" size="100%">Fernandes, Alexandra R.</style></author><author><style face="normal" font="default" size="100%">Barroso, Sónia</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luisa</style></author><author><style face="normal" font="default" size="100%">Afonso, Carlos A. M.</style></author><author><style face="normal" font="default" size="100%">Ferreira, Luísa Maria</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Synthesis, cytotoxicity evaluation in human cell lines and in vitro DNA interaction of a hetero arylidene-9(10H)-anthrone</style></title><secondary-title><style face="normal" font="default" size="100%">European Journal of Organic Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">anthracenecarboxaldehyde</style></keyword><keyword><style  face="normal" font="default" size="100%">arylidene anthrone</style></keyword><keyword><style  face="normal" font="default" size="100%">Decarbonylation</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA intercalation</style></keyword><keyword><style  face="normal" font="default" size="100%">Imidazolium salt</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1002/ejoc.201701500</style></url></web-urls></urls><pages><style face="normal" font="default" size="100%">n/a–n/a</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;A new and never yet reported hetero arylidene-9(10H)-anthrone structure (4) was unexpectedly isolated on reaction of 1,2-dimethyl-3-ethylimidazolium iodide (2) and 9-anthracenecarboxaldehyde (3) under basic conditions. Its structure was unequivocally attributed by X-ray crystallography. No cytotoxicity in human healthy fibroblasts and in two different cancer cell lines was observed indicating its applicability in biological systems. Compound 4 interacts with CT-DNA by intercalation between the adjacent base pairs of DNA with a high binding affinity (Kb = 2.0(± 0.20) x 105 M-1) which is 10x higher than that described for doxorubicin (Kb = 3.2 (±0.23) × 104 M-1). Furthermore, compound 4 quenches the fluorescence emission of GelRed-CT-DNA system with a quenching constant (KSV) of 3.3(±0.3) x 103 M-1 calculated by the Stern-Volmer equation.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">&lt;p&gt;n/a&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Gomes, Ana Sara</style></author><author><style face="normal" font="default" size="100%">Trovão, Filipa</style></author><author><style face="normal" font="default" size="100%">Andrade Pinheiro, Benedita</style></author><author><style face="normal" font="default" size="100%">Freire, Filipe</style></author><author><style face="normal" font="default" size="100%">Gomes, Sara</style></author><author><style face="normal" font="default" size="100%">Oliveira, Carla</style></author><author><style face="normal" font="default" size="100%">Domingues, Lucília</style></author><author><style face="normal" font="default" size="100%">Romão, Maria João</style></author><author><style face="normal" font="default" size="100%">Saraiva, Lucília</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The Crystal Structure of the R280K Mutant of Human p53 Explains the Loss of DNA Binding</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Molecular Sciences</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.mdpi.com/1422-0067/19/4/1184</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">4}, ARTICLE NUMBER = {1184</style></number><volume><style face="normal" font="default" size="100%">19</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The p53 tumor suppressor is widely found to be mutated in human cancer. This protein is regarded as a molecular hub regulating different cell responses, namely cell death. Compelling data have demonstrated that the impairment of p53 activity correlates with tumor development and maintenance. For these reasons, the reactivation of p53 function is regarded as a promising strategy to halt cancer. In the present work, the recombinant mutant p53R280K DNA binding domain (DBD) was produced for the first time, and its crystal structure was determined in the absence of DNA to a resolution of 2.0 Å. The solved structure contains four molecules in the asymmetric unit, four zinc(II) ions, and 336 water molecules. The structure was compared with the wild-type p53 DBD structure, isolated and in complex with DNA. These comparisons contributed to a deeper understanding of the mutant p53R280K structure, as well as the loss of DNA binding related to halted transcriptional activity. The structural information derived may also contribute to the rational design of mutant p53 reactivating molecules with potential application in cancer treatment.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kumar, Krishan</style></author><author><style face="normal" font="default" size="100%">Correia, Márcia</style></author><author><style face="normal" font="default" size="100%">Pires, Virgínia R.</style></author><author><style face="normal" font="default" size="100%">Dhillon, Arun</style></author><author><style face="normal" font="default" size="100%">Sharma, Kedar</style></author><author><style face="normal" font="default" size="100%">Rajulapati, Vikky</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Goyal, Arun</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Novel insights into the degradation of β-1,3-glucans by the cellulosome of Clostridium thermocellum revealed by structure and function studies of a family 81 glycoside hydrolase</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Biological Macromolecules</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">X-ray crystallography</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.sciencedirect.com/science/article/pii/S0141813018322384</style></url></web-urls></urls><pages><style face="normal" font="default" size="100%">-</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Abstract The family 81 glycoside hydrolase (GH81) from Clostridium thermocellum is a β-1,3-glucanase belonging to cellulosomal complex. The gene encoding \{GH81\} from Clostridium thermocellum (CtLam81A) was cloned and expressed displaying a molecular mass of  82 kDa. CtLam81A showed maximum activity against laminarin (100 U/mg), followed by curdlan (65 U/mg), at pH 7.0 and 75 °C. CtLam81A displayed Km, 2.1 ± 0.12 mg/ml and Vmax, 109 ± 1.8 U/mg, against laminarin under optimized conditions. CtLam81A activity was significantly enhanced by Ca2+ or Mg2+ ions. Melting curve analysis of CtLam81A showed an increase in melting temperature from 91 °C to 96 °C by Ca2+ or Mg2+ ions and decreased to 82 °C by EDTA, indicating that Ca2+ and Mg2+ ions may be involved in catalysis and in maintaining structural integrity. \{TLC\} and MALDI-TOF analysis of β-1,3-glucan hydrolysed products released initially, showed β-1,3-glucan-oligosaccharides degree of polymerization (DP) from \{DP2\} to DP7, confirming an endo-mode of action. The catalytically inactive mutant CtLam81A-E515A generated by site-directed mutagenesis was co-crystallized and tetragonal crystals diffracting up to 1.4 Å resolution were obtained. CtLam81A-E515A contained 15 α-helices and 38 β-strands forming a four-domain structure viz. a β-sandwich domain I at N-terminal, an α/β-domain II, an (α/α)6 barrel domain III, and a small 5-stranded β-sandwich domain IV.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kryshtafovych, Andriy</style></author><author><style face="normal" font="default" size="100%">Albrecht, Reinhard</style></author><author><style face="normal" font="default" size="100%">Baslé, Arnaud</style></author><author><style face="normal" font="default" size="100%">Bule, Pedro</style></author><author><style face="normal" font="default" size="100%">Caputo, Alessandro T.</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luisa</style></author><author><style face="normal" font="default" size="100%">Chao, Kinlin L.</style></author><author><style face="normal" font="default" size="100%">Diskin, Ron</style></author><author><style face="normal" font="default" size="100%">Fidelis, Krzysztof</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Fredslund, Folmer</style></author><author><style face="normal" font="default" size="100%">Gilbert, Harry J.</style></author><author><style face="normal" font="default" size="100%">Goulding, Celia W.</style></author><author><style face="normal" font="default" size="100%">Hartmann, Marcus D.</style></author><author><style face="normal" font="default" size="100%">Hayes, Christopher S.</style></author><author><style face="normal" font="default" size="100%">Herzberg, Osnat</style></author><author><style face="normal" font="default" size="100%">Hill, Johan C.</style></author><author><style face="normal" font="default" size="100%">Joachimiak, Andrzej</style></author><author><style face="normal" font="default" size="100%">Kohring, Gert-Wieland</style></author><author><style face="normal" font="default" size="100%">Koning, Roman I.</style></author><author><style face="normal" font="default" size="100%">{Lo Leggio}, Leila</style></author><author><style face="normal" font="default" size="100%">Mangiagalli, Marco</style></author><author><style face="normal" font="default" size="100%">Michalska, Karolina</style></author><author><style face="normal" font="default" size="100%">Moult, John</style></author><author><style face="normal" font="default" size="100%">Najmudin, Shabir</style></author><author><style face="normal" font="default" size="100%">Nardini, Marco</style></author><author><style face="normal" font="default" size="100%">Nardone, Valentina</style></author><author><style face="normal" font="default" size="100%">Ndeh, Didier</style></author><author><style face="normal" font="default" size="100%">Nguyen, Thanh H.</style></author><author><style face="normal" font="default" size="100%">Pintacuda, Guido</style></author><author><style face="normal" font="default" size="100%">Postel, Sandra</style></author><author><style face="normal" font="default" size="100%">van Raaij, Mark J.</style></author><author><style face="normal" font="default" size="100%">Roversi, Pietro</style></author><author><style face="normal" font="default" size="100%">Shimon, Amir</style></author><author><style face="normal" font="default" size="100%">Singh, Abhimanyu K.</style></author><author><style face="normal" font="default" size="100%">Sundberg, Eric J.</style></author><author><style face="normal" font="default" size="100%">Tars, Kaspars</style></author><author><style face="normal" font="default" size="100%">Zitzmann, Nicole</style></author><author><style face="normal" font="default" size="100%">Schwede, Torsten</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Target highlights from the first post-PSI CASP experiment (CASP12, May-August 2016)</style></title><secondary-title><style face="normal" font="default" size="100%">Proteins: Structure, Function, and Bioinformatics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">CASP</style></keyword><keyword><style  face="normal" font="default" size="100%">NMR</style></keyword><keyword><style  face="normal" font="default" size="100%">protein structure prediction</style></keyword><keyword><style  face="normal" font="default" size="100%">X-ray crystallography</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">oct</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/28960539 http://doi.wiley.com/10.1002/prot.25392</style></url></web-urls></urls><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The functional and biological significance of the selected CASP12 targets are described by the authors of the structures. The crystallographers discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submitted to the CASP12 experiment. This article is protected by copyright. All rights reserved.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">&lt;p&gt;n/a&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Pires, Virgínia M R</style></author><author><style face="normal" font="default" size="100%">Pereira, Pedro M M</style></author><author><style face="normal" font="default" size="100%">Brás, Joana L. A.</style></author><author><style face="normal" font="default" size="100%">Correia, Márcia</style></author><author><style face="normal" font="default" size="100%">Cardoso, Vânia</style></author><author><style face="normal" font="default" size="100%">Bule, Pedro</style></author><author><style face="normal" font="default" size="100%">Alves, Victor D.</style></author><author><style face="normal" font="default" size="100%">Najmudin, Shabir</style></author><author><style face="normal" font="default" size="100%">Venditto, Immacolata</style></author><author><style face="normal" font="default" size="100%">Ferreira, Luís M A</style></author><author><style face="normal" font="default" size="100%">Romão, Maria João</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Prazeres, Duarte Miguel</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Stability and ligand promiscuity of type A carbohydrate-binding modules are illustrated by the structure of Spirochaeta thermophila StCBM64C</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Biological Chemistry</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">mar</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://europepmc.org/abstract/med/28179427</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">12</style></number><volume><style face="normal" font="default" size="100%">292</style></volume><pages><style face="normal" font="default" size="100%">4847–4860</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Deconstruction of cellulose, the most abundant plant cell wall polysaccharide, requires the cooperative activity of a large repertoire of microbial enzymes. Modular cellulases contain non-catalytic type A Carbohydrate-Binding Modules (CBMs) that specifically bind to the crystalline regions of cellulose, thus promoting enzyme efficacy through proximity and targeting effects. Although type A CBMs play a critical role in cellulose recycling, their mechanism of action remains poorly understood. Here we produced a library of recombinant CBMs representative of the known diversity of type A modules. The binding properties of 40 CBMs, in fusion with an N-terminal green fluorescence protein (GFP) domain, revealed that type A CBMs possess the ability to recognize different crystalline forms of cellulose and chitin over a wide range of temperatures, pHs and ionic strengths. A Spirochaeta thermophila CBM64, in particular, displayed plasticity in its capacity to bind both crystalline and soluble carbohydrates under a wide range of extreme conditions. The structure of S. thermophila StCBM64C revealed an untwisted, flat, carbohydrate-binding interface comprising the side chains of four tryptophan residues in a coplanar linear arrangement. Significantly, two highly conserved asparagine side chains, each one located between two tryptophan residues, are critical to insoluble and soluble glucan recognition but not to bind xyloglucan. Thus, CBM64 compact structure and its extended and versatile ligand interacting platform illustrates how type A CBMs target their appended plant cell wall degrading enzymes to a diversity of recalcitrant carbohydrates under a wide range of environmental conditions.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">&lt;p&gt;n/a&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Bule, Pedro</style></author><author><style face="normal" font="default" size="100%">Alves, Victor D.</style></author><author><style face="normal" font="default" size="100%">Israeli-Ruimy, Vered</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana L.</style></author><author><style face="normal" font="default" size="100%">Ferreira, Luís M A</style></author><author><style face="normal" font="default" size="100%">Smith, Steven P.</style></author><author><style face="normal" font="default" size="100%">Gilbert, Harry J.</style></author><author><style face="normal" font="default" size="100%">Najmudin, Shabir</style></author><author><style face="normal" font="default" size="100%">Bayer, Edward A.</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes</style></title><secondary-title><style face="normal" font="default" size="100%">Scientific Reports</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2017</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1038/s41598-017-00919-w</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">7</style></volume><pages><style face="normal" font="default" size="100%">759</style></pages><isbn><style face="normal" font="default" size="100%">2045-2322</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Cellulosomes are sophisticated multi-enzymatic nanomachines produced by anaerobes to effectively deconstruct plant structural carbohydrates. Cellulosome assembly involves the binding of enzyme-borne dockerins (Doc) to repeated cohesin (Coh) modules located in a non-catalytic scaffoldin. Docs appended to cellulosomal enzymes generally present two similar Coh-binding interfaces supporting a dual-binding mode, which may confer increased positional adjustment of the different complex components. Ruminococcus flavefaciens’ cellulosome is assembled from a repertoire of 223 Doc-containing proteins classified into 6 groups. Recent studies revealed that Docs of groups 3 and 6 are recruited to the cellulosome via a single-binding mode mechanism with an adaptor scaffoldin. To investigate the extent to which the single-binding mode contributes to the assembly of R. flavefaciens cellulosome, the structures of two group 1 Docs bound to Cohs of primary (ScaA) and adaptor (ScaB) scaffoldins were solved. The data revealed that group 1 Docs display a conserved mechanism of Coh recognition involving a single-binding mode. Therefore, in contrast to all cellulosomes described to date, the assembly of R. flavefaciens cellulosome involves single but not dual-binding mode Docs. Thus, this work reveals a novel mechanism of cellulosome assembly and challenges the ubiquitous implication of the dual-binding mode in the acquisition of cellulosome flexibility.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><notes><style face="normal" font="default" size="100%">&lt;p&gt;n/a&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Brás, Joana L. A.</style></author><author><style face="normal" font="default" size="100%">Pinheiro, Benedita A.</style></author><author><style face="normal" font="default" size="100%">Cameron, Kate</style></author><author><style face="normal" font="default" size="100%">Cuskin, Fiona</style></author><author><style face="normal" font="default" size="100%">Viegas, Aldino</style></author><author><style face="normal" font="default" size="100%">Najmudin, Shabir</style></author><author><style face="normal" font="default" size="100%">Bule, Pedro</style></author><author><style face="normal" font="default" size="100%">Pires, Virginia M. R.</style></author><author><style face="normal" font="default" size="100%">Romão, Maria João</style></author><author><style face="normal" font="default" size="100%">Bayer, Edward A.</style></author><author><style face="normal" font="default" size="100%">Spencer, Holly L.</style></author><author><style face="normal" font="default" size="100%">Smith, Steven</style></author><author><style face="normal" font="default" size="100%">Gilbert, Harry J.</style></author><author><style face="normal" font="default" size="100%">Alves, Victor D.</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Diverse specificity of cellulosome attachment to the bacterial cell surface</style></title><secondary-title><style face="normal" font="default" size="100%">Scientific Reports</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">dec</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.nature.com/articles/srep38292</style></url></web-urls></urls><publisher><style face="normal" font="default" size="100%">The Author(s)</style></publisher><volume><style face="normal" font="default" size="100%">6</style></volume><pages><style face="normal" font="default" size="100%">38292</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;During the course of evolution, the cellulosome, one of Nature's most intricate multi-enzyme complexes, has been continuously fine-tuned to efficiently deconstruct recalcitrant carbohydrates. To facilitate the uptake of released sugars, anaerobic bacteria use highly ordered protein-protein interactions to recruit these nanomachines to the cell surface. Dockerin modules located within a non-catalytic macromolecular scaffold, whose primary role is to assemble cellulosomal enzymatic subunits, bind cohesin modules of cell envelope proteins, thereby anchoring the cellulosome onto the bacterial cell. Here we have elucidated the unique molecular mechanisms used by anaerobic bacteria for cellulosome cellular attachment. The structure and biochemical analysis of five cohesin-dockerin complexes revealed that cell surface dockerins contain two cohesin-binding interfaces, which can present different or identical specificities. In contrast to the current static model, we propose that dockerins utilize multivalent modes of cohesin recognition to recruit cellulosomes to the cell surface, a mechanism that maximises substrate access while facilitating complex assembly.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">&lt;p&gt;n/a&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Palma, A. S.</style></author><author><style face="normal" font="default" size="100%">Liu, Y.</style></author><author><style face="normal" font="default" size="100%">Zhang, H.</style></author><author><style face="normal" font="default" size="100%">Zhang, Y</style></author><author><style face="normal" font="default" size="100%">McCleary, B. V.</style></author><author><style face="normal" font="default" size="100%">Yu, G.</style></author><author><style face="normal" font="default" size="100%">Huang, Q.</style></author><author><style face="normal" font="default" size="100%">Guidolin, L. S.</style></author><author><style face="normal" font="default" size="100%">Ciocchini, A. E.</style></author><author><style face="normal" font="default" size="100%">Torosantucci, A.</style></author><author><style face="normal" font="default" size="100%">Wang, D.</style></author><author><style face="normal" font="default" size="100%">Carvalho, AL</style></author><author><style face="normal" font="default" size="100%">Fontes, C. M.</style></author><author><style face="normal" font="default" size="100%">Mulloy, B.</style></author><author><style face="normal" font="default" size="100%">Childs, R. A.</style></author><author><style face="normal" font="default" size="100%">Feizi, T.</style></author><author><style face="normal" font="default" size="100%">Chai, W.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Cell Proteomics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2015</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/25670804</style></url></web-urls></urls><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Glucans are polymers of D-glucose with differing linkages in linear or branched sequences. They are constituents of microbial and plant cell-walls and involved in important bio-recognition processes including immunomodulation, anti-cancer activities, pathogen virulence and plant cell-wall biodegradation. Translational possibilities for these activities in medicine and biotechnology are considerable. High-throughput micro-methods are needed to screen proteins for recognition of specific glucan sequences as a lead to structure-function studies and their exploitation. We describe construction of a glucome microarray, the first sequence-defined glycome-scale microarray, using a designer approach from targeted ligand-bearing glucans in conjunction with a novel high-sensitivity mass spectrometric sequencing method, as a screening tool to assign glucan recognition motifs. The glucome microarray comprises 153 oligosaccharide probes with high purity, representing major sequences in glucans. The negative-ion electrospray tandem mass spectrometry with collision-induced dissociation was used for complete linkage analysis of gluco-oligosaccharides in linear homo and hetero and branched sequences. The system is validated using antibodies and carbohydrate-binding modules known to target α- or β-glucans in different biological contexts, extending knowledge on their specificities, and applied to reveal new information on glucan recognition by two signalling molecules of the immune system against pathogens: Dectin-1 and DC-SIGN. The sequencing of the glucan oligosaccharides by the MS method and their interrogation on the microarrays provides detailed information on linkage, sequence and chain length requirements of glucan-recognizing proteins, and are a sensitive means of revealing unsuspected sequences in the polysaccharides.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type><notes><style face="normal" font="default" size="100%">&lt;p&gt;n/a&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ribeiro, Diana</style></author><author><style face="normal" font="default" size="100%">Kulakova, Alina</style></author><author><style face="normal" font="default" size="100%">Quaresma, Pedro</style></author><author><style face="normal" font="default" size="100%">Pereira, Eulalia</style></author><author><style face="normal" font="default" size="100%">Bonifacio, Cecilia</style></author><author><style face="normal" font="default" size="100%">Romao, Maria Joao</style></author><author><style face="normal" font="default" size="100%">Franco, Ricardo</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luisa</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Use of Gold Nanoparticles as Additives in Protein Crystallization</style></title><secondary-title><style face="normal" font="default" size="100%">Crystal Growth &amp; Design</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2014</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">&lt;Go to ISI&gt;://WOS:000329337000029</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">1</style></number><volume><style face="normal" font="default" size="100%">14</style></volume><pages><style face="normal" font="default" size="100%">222-227</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">n/a</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type><notes><style face="normal" font="default" size="100%">&lt;p&gt;Times Cited: 1 Carvalho, Ana Luisa/G-5638-2011; Romao, Maria/A-4115-2013; Pereira, Eulalia/C-6282-2013 Carvalho, Ana Luisa/0000-0002-3824-0240; Romao, Maria/0000-0002-3004-0543; Pereira, Eulalia/0000-0003-2086-5696 1&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Viegas, Aldino</style></author><author><style face="normal" font="default" size="100%">Sardinha, Joao</style></author><author><style face="normal" font="default" size="100%">Freire, Filipe</style></author><author><style face="normal" font="default" size="100%">Duarte, Daniel F</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana L.</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Romao, Maria J.</style></author><author><style face="normal" font="default" size="100%">Macedo, Anjos L</style></author><author><style face="normal" font="default" size="100%">Cabrita, Eurico J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Solution structure, dynamics and binding studies of a family 11 carbohydrate-binding module from Clostridium thermocellum (CtCBM11)</style></title><secondary-title><style face="normal" font="default" size="100%">The Biochemical journal</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2013</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">&lt;Go to ISI&gt;://MEDLINE:23356867</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">2</style></number><volume><style face="normal" font="default" size="100%">451</style></volume><pages><style face="normal" font="default" size="100%">289-300</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type><notes><style face="normal" font="default" size="100%">&lt;p&gt;23356867&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>5</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Bras, Joana L. A.</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luisa</style></author><author><style face="normal" font="default" size="100%">Viegas, Aldino</style></author><author><style face="normal" font="default" size="100%">Najmudin, Shabir</style></author><author><style face="normal" font="default" size="100%">Alves, Victor D.</style></author><author><style face="normal" font="default" size="100%">Prates, Jose A. M.</style></author><author><style face="normal" font="default" size="100%">Ferreira, Luis M. A.</style></author><author><style face="normal" font="default" size="100%">Romao, Maria J.</style></author><author><style face="normal" font="default" size="100%">Gilbert, Harry J.</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Escherichia coli expression, purification, crystallization, and structure determination of bacterial cohesin-dockerin complexes</style></title><secondary-title><style face="normal" font="default" size="100%">Methods in enzymology</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2012</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">&lt;Go to ISI&gt;://MEDLINE:22608738</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">510</style></volume><pages><style face="normal" font="default" size="100%">395-415</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Cellulosomes are highly efficient nanomachines that play a fundamental role during the anaerobic deconstruction of complex plant cell wall carbohydrates. The assembly of these complex nanomachines results from the very tight binding of repetitive cohesin modules, located in a noncatalytic molecular scaffold, and dockerin domains located at the C-terminus of the enzyme components of the cellulosome. The number of enzymes found in a cellulosome varies but may reach more than 100 catalytic subunits if cellulosomes are further organized in polycellulosomes, through a second type of cohesin-dockerin interaction. Structural studies have revealed how the cohesin-dockerin interaction mediates cellulosome assembly and cell-surface attachment, while retaining the flexibility required to potentiate catalytic synergy within the complex. Methods that might be applied for the production, purification, and structure determination of cohesin-dockerin complexes are described here. Copyright 2012 Elsevier Inc. All rights reserved.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type><notes><style face="normal" font="default" size="100%">&lt;p&gt;22608738&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Pinheiro, B. A.</style></author><author><style face="normal" font="default" size="100%">Bras, J. L. A.</style></author><author><style face="normal" font="default" size="100%">Najmudin, S.</style></author><author><style face="normal" font="default" size="100%">Carvalho, AL</style></author><author><style face="normal" font="default" size="100%">Ferreira, LMA</style></author><author><style face="normal" font="default" size="100%">Prates, JAM</style></author><author><style face="normal" font="default" size="100%">Fontes, CMGA</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Flexibility and specificity of the cohesin-dockerin interaction: implications for cellulosome assembly and functionality</style></title><secondary-title><style face="normal" font="default" size="100%">Biocatalysis and Biotransformation</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2012</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">&lt;Go to ISI&gt;://WOS:000304750500005</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">30</style></volume><pages><style face="normal" font="default" size="100%">309-315</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Cellulosomes are highly elaborate multi-enzyme complexes of Carbohydrate Active enZYmes (CAZYmes) secreted by cellulolytic microorganisms, which very effectively degrade the most abundant polymers on Earth, cellulose and hemicelluloses. Cellulosome assembly requires that a non-catalytic dockerin module found in cellulosomal enzymes binds to one of the various cohesin domains located in a large molecular scaffold called Scaffoldin. A diversity of cohesin -dockerin binding specificities have been described, the combination of which may result in complex plant cell wall degrading systems, maximising the synergy between enzymes in order to improve catalytic efficiency. Structural studies have allowed the spatial flexibility inherent to the cellulosomal system to be determined. Recent progress achieved from the study of the fundamental cohesin and dockerin units involved in cellulosome assembly will be reviewed.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type><notes><style face="normal" font="default" size="100%">&lt;p&gt;ISI Document Delivery No.: 951WJ Times Cited: 0 Cited Reference Count: 45 Pinheiro, Benedita Andrade Armada Bras, Joana Luis Najmudin, Shabir Carvalho, Ana Luisa Ferreira, Luis M. A. Prates, Jose A. M. Godinho Andrade Fontes, Carlos Mendes INFORMA HEALTHCARE LONDON&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Bras, Joana L. A.</style></author><author><style face="normal" font="default" size="100%">Alves, Victor D.</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luisa</style></author><author><style face="normal" font="default" size="100%">Najmudin, Shabir</style></author><author><style face="normal" font="default" size="100%">Prates, Jose A. M.</style></author><author><style face="normal" font="default" size="100%">Ferreira, Luis M. A.</style></author><author><style face="normal" font="default" size="100%">Bolam, David N.</style></author><author><style face="normal" font="default" size="100%">Romao, Maria Joao</style></author><author><style face="normal" font="default" size="100%">Gilbert, Harry J.</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Novel Clostridium thermocellum Type I Cohesin-Dockerin Complexes Reveal a Single Binding Mode</style></title><secondary-title><style face="normal" font="default" size="100%">The Journal of biological chemistry</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2012</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">&lt;Go to ISI&gt;://MEDLINE:23118225</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">53</style></number><volume><style face="normal" font="default" size="100%">287</style></volume><pages><style face="normal" font="default" size="100%">44394-405</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type><notes><style face="normal" font="default" size="100%">&lt;p&gt;23118225&lt;/p&gt;
</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Garcia-Alvarez, Begona</style></author><author><style face="normal" font="default" size="100%">Melero, Roberto</style></author><author><style face="normal" font="default" size="100%">Dias, Fernando M. V.</style></author><author><style face="normal" font="default" size="100%">Prates, Jose A. M.</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Smith, Steven P.</style></author><author><style face="normal" font="default" size="100%">Romao, Maria Joao</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luisa</style></author><author><style face="normal" font="default" size="100%">Llorca, Oscar</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Molecular Architecture and Structural Transitions of a Clostridium thermocellum Mini-Cellulosome</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Molecular Biology</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2011</style></year></dates><number><style face="normal" font="default" size="100%">4</style></number><volume><style face="normal" font="default" size="100%">407</style></volume><pages><style face="normal" font="default" size="100%">571-580</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">n/a</style></abstract><notes><style face="normal" font="default" size="100%">n/a</style></notes></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Bras, Joana L. A.</style></author><author><style face="normal" font="default" size="100%">Cartmell, Alan</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Lusia M.</style></author><author><style face="normal" font="default" size="100%">Verze, Genny</style></author><author><style face="normal" font="default" size="100%">Bayer, Edward A.</style></author><author><style face="normal" font="default" size="100%">Vazana, Yael</style></author><author><style face="normal" font="default" size="100%">Correia, Marcia A. S.</style></author><author><style face="normal" font="default" size="100%">Prates, Jose A. M.</style></author><author><style face="normal" font="default" size="100%">Ratnaparkhe, Supriya</style></author><author><style face="normal" font="default" size="100%">Boraston, Alisdair B.</style></author><author><style face="normal" font="default" size="100%">Romao, Maria J.</style></author><author><style face="normal" font="default" size="100%">Fontes, Carlos M. G. A.</style></author><author><style face="normal" font="default" size="100%">Gilbert, Harry J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural insights into a unique cellulase fold and mechanism of cellulose hydrolysis (vol 108, pg 5237, 2011)</style></title><secondary-title><style face="normal" font="default" size="100%">Proceedings of the National Academy of Sciences of the United States of America</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2011</style></year></dates><number><style face="normal" font="default" size="100%">20</style></number><volume><style face="normal" font="default" size="100%">108</style></volume><pages><style face="normal" font="default" size="100%">8525-8525</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">n/a</style></abstract><notes><style face="normal" font="default" size="100%">&lt;p&gt;Times Cited: 0&lt;/p&gt;
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