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Software transactional memory (STM) algorithms associate metadata with the memory locations accessed during a transaction's lifetime. This metadata may be stored in an external table by resorting to a mapping function that associates the address of a memory cell with the table entry containing the corresponding metadata (out-place or external strategy). Alternatively, the metadata may be stored adjacent to the associated memory cell by wrapping the cell and metadata together (in-place strategy). The implementation techniques to support these two approaches are very different and each STM framework is usually biased towards one of them, only allowing the efficient implementation of STM algorithms which suit one of the approaches and inhibiting a fair comparison with STM algorithms suiting the other. In this paper, we introduce a technique to implement in-place metadata that does not wrap memory cells, thus overcoming the bias and allowing STM algorithms to directly access the transactional metadata. The proposed technique is available as an extension to Deuce and enables the efficient implementation of a wide range of STM algorithms and their fair (unbiased) comparison in a common STM framework. We illustrate the benefits of our approach by analyzing its impact in two popular transactional memory algorithms with several transactional workloads, TL2 and multiversioning, each befitting out-place and in-place, respectively.

Acetylcholinesterase (AChE) inhibition is one of the most currently available therapies for the management of Alzheimer’s disease (AD) symptoms. In this context, NMR spectroscopy binding studies were accomplished to explain the inhibition of AChE activity by Salvia sclareoides extracts. HPLC-MS analyses of the acetone, butanol and water extracts eluted with methanol and acidified water showed that rosmarinic acid is present in all the studied samples and is a major constituent of butanol and water extracts. Moreover, luteolin 4′-O-glucoside, luteolin 3′,7-di-O-glucoside and luteolin 7-O-(6′′-O-acetylglucoside) were identified by MS2 and MS3 data acquired during the LC-MSn runs. Quantification of rosmarinic acid by HPLC with diode-array detection (DAD) showed that the butanol extract is the richest one in this component (134 μg mg−1 extract). Saturation transfer difference (STD) NMR spectroscopy binding experiments of S. sclareoides crude extracts in the presence of AChE in buffer solution determined rosmarinic acid as the only explicit binder for AChE. Furthermore, the binding epitope and the AChE-bound conformation of rosmarinic acid were further elucidated by STD and transferred NOE effect (trNOESY) experiments. As a control, NMR spectroscopy binding experiments were also carried out with pure rosmarinic acid, thus confirming the specific interaction and inhibition of this compound against AChE. The binding site of AChE for rosmarinic acid was also investigated by STD-based competition binding experiments using Donepezil, a drug currently used to treat AD, as a reference. These competition experiments demonstrated that rosmarinic acid does not compete with Donepezil for the same binding site. A 3D model of the molecular complex has been proposed. Therefore, the combination of the NMR spectroscopy based data with molecular modelling has permitted us to detect a new binding site in AChE, which could be used for future drug development.

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We introduce a class of finite semigroups obtained by considering Rees
quotients of numerical semigroups.
Several natural questions concerning this class, as well as particular
subclasses obtained by considering some special ideals, are answered while
others remain open. We exhibit nice presentations for these semigroups and
prove that the Rees quotients by ideals of N, the positive integers under
addition, constitute a set of generators for the pseudovariety of commutative
and nilpotent semigroups.

Non-catalytic cellulosomal carbohydrate-binding modules (CBMs) are responsible for increasing the catalytic efficiency of cellulosic enzymes by selectively putting the substrate (a wide range of poly- and oligosaccharides) and enzyme into close contact. In the present work we carried out an atomistic rationalization of the molecular determinants of ligand specificity of a family 11 CBM from thermophilic C. thermocellum (CtCBM11), based on a NMR and molecular modeling approach. We have determined the NMR solution structure of CtCBM11 at 25 and 50 ºC and derived information on the residues of the protein involved in ligand recognition and on the influence of the length of the saccharide chain on binding. We obtained models of the CtCBM11/cellohexaose and CtCBM11/cellotetraose complexes by docking in accordance with the NMR experimental data. Specific ligand/protein CH-π and Van der Waals interactions were found to be determinant for the stability of the complexes and for defining specificity. Using the order parameters derived from backbone dynamics analysis in the presence and absence of ligand and at 25 and 50 ºC, we determined that the protein’s backbone conformational entropy is slightly positive. This data in combination with the negative binding entropy calculated from ITC studies supports a selection mechanism where a rigid protein selects a defined oligosaccharide conformation.

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