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pro vyhledávání: '"Brevern, Alexandre"'
AlphaFold2 (AF2) has emerged in recent years as a groundbreaking innovation that has revolutionized several scientific fields, in particular structural biology, drug design and the elucidation of disease mechanisms. Many scientists now use AF2 on a d
Externí odkaz:
http://arxiv.org/abs/2403.12668
Autor:
de Brevern, Alexandre G.1,2 (AUTHOR) alexandre.debrevern@univ-paris-diderot.fr
Publikováno v:
International Journal of Molecular Sciences. Oct2024, Vol. 25 Issue 19, p10793. 13p.
Publikováno v:
International Journal of Molecular Sciences, MDPI, 2020, 21 (15), pp.5402
The synthesis of complex oligosaccharides is desired for their potential as prebiotics, and their role in the pharmaceutical and food industry. Levansucrase (LS, EC 2.4.1.10), a fructosyl-transferase, can catalyze the synthesis of these compounds. LS
Externí odkaz:
http://arxiv.org/abs/2008.04531
Akademický článek
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Autor:
Nekrasov, Alexei, Alekseeva, Ludmila, Pogosyan, Rudolf A., Dolgikh, Dmitry, Kirpichnikov, M. P., de Brevern, Alexandre, Anashkina, Anastasia
Publikováno v:
Biochimie, Elsevier, 2019, 160, pp.88-92
The aim of this work was to find a minimal set of structurally stable pentapeptides, which allows forming a polypeptide chain of a required 3D structure. To search for factors that ensure structural stability of the pentapeptide, we generated peptide
Externí odkaz:
http://arxiv.org/abs/1908.05126
Publikováno v:
Amino Acids, Springer Verlag, 2019, 51 (7), pp.1065-1079
Post-Translational Modifications (PTMs) are known to play a critical role in the regulation of the protein functions. Their impact on protein structures, and their link to disorder regions have already been spotted on the past decade. Nonetheless, th
Externí odkaz:
http://arxiv.org/abs/1908.05122
Autor:
Narwani, Tarun, Etchebest, Catherine, Craveur, Pierrick, Léonard, Sylvain, Rebehmed, Joseph, Srinivasan, Narayanaswamy, Bornot, Aurélie, Gelly, Jean-Christophe, de Brevern, Alexandre
Publikováno v:
Biochimie, Elsevier, 2019, 165, pp.150-155
Flexibility is an intrinsic essential feature of protein structures, directly linked to their functions. To this day, most of the prediction methods use the crystallographic data (namely B-factors) as the only indicator of protein's inner flexibility
Externí odkaz:
http://arxiv.org/abs/1908.05120
Autor:
de Brevern, Alexandre G.1,2 alexandre.debrevern@univ-paris-diderot.fr
Publikováno v:
BioMedInformatics. Mar2024, Vol. 4 Issue 1, p1-7. 7p.
Publikováno v:
PLoS Computational Biology, Public Library of Science, 2018, 14 (2), pp.e1006008
The majority of the proteins encoded in the genomes of eukaryotes contain more than one domain. Reasons for high prevalence of multi-domain proteins in various organisms have been attributed to higher stability and functional and folding advantages o
Externí odkaz:
http://arxiv.org/abs/1808.03642
Autor:
Martins, Carla, Gardebien, Fabrice, Nadaradjane, Aravindan Arun, Diharce, Julien, de Brevern, Alexandre G.
Publikováno v:
Molecules; Oct2024, Vol. 29 Issue 20, p4863, 13p