<?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%">Lima, Carlos  D. L.</style></author><author><style face="normal" font="default" size="100%">Helena Coelho</style></author><author><style face="normal" font="default" size="100%">Gimeno, Ana</style></author><author><style face="normal" font="default" size="100%">Trovão, Filipa</style></author><author><style face="normal" font="default" size="100%">Diniz, Ana</style></author><author><style face="normal" font="default" size="100%">Dias, Jorge  S.</style></author><author><style face="normal" font="default" size="100%">Jesús Jiménez-Barbero</style></author><author><style face="normal" font="default" size="100%">Corzana, Francisco</style></author><author><style face="normal" font="default" size="100%">Carvalho, Ana Luísa</style></author><author><style face="normal" font="default" size="100%">Cabrita, Eurico J.</style></author><author><style face="normal" font="default" size="100%">Marcelo, Filipa</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural insights into the molecular recognition mechanism of the cancer and pathogenic epitope, LacdiNAc by immune-related lectins</style></title><secondary-title><style face="normal" font="default" size="100%">Chemistry – A European JournalChemistry – A European Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">glycan-protein interactions</style></keyword><keyword><style  face="normal" font="default" size="100%">hGal-3</style></keyword><keyword><style  face="normal" font="default" size="100%">hMGL</style></keyword><keyword><style  face="normal" font="default" size="100%">LacdiNAc</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular recognition</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2021</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2021</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://doi.org/10.1002/chem.202100800</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%">n/a</style></volume><isbn><style face="normal" font="default" size="100%">0947-6539</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Interactions of glycan-specific epitopes to human lectin receptors represent novel immune checkpoints for investigating cancer and infection diseases. By employing a multidisciplinary approach that combines isothermal titration calorimetry, NMR spectroscopy, molecular dynamics simulations, and X-ray crystallography, we disclosed the molecular determinants that govern the recognition of the tumour and pathogenic glycobiomarker LacdiNAc (GalNAc?1-4GlcNAc, LDN), including their comparison with the ubiquitous LacNAc epitope (Gal?1-4GlcNAc, LN), by two human immune-related lectins, galectin-3 (hGal-3) and the macrophage galactose C-type lectin (hMGL). A different mechanism of binding and interactions is observed for the hGal-3/LDN and hMGL/LDN complexes, which explains the remarkable difference in the binding specificity of LDN and LN by these two lectins. The new structural clues reported herein are fundamental for the chemical design of mimetics targeting hGal-3/hMGL recognition process.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">n/a</style></issue><notes><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;https://doi.org/10.1002/chem.202100800&quot;&gt;https://doi.org/10.1002/chem.202100800&lt;/a&gt;&lt;/p&gt;
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