Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Jeremy Esque"'
Autor:
Alexandra S. Tauzin, Mariana Rangel Pereira, Liisa D. Van Vliet, Pierre-Yves Colin, Elisabeth Laville, Jeremy Esque, Sandrine Laguerre, Bernard Henrissat, Nicolas Terrapon, Vincent Lombard, Marion Leclerc, Joël Doré, Florian Hollfelder, Gabrielle Potocki-Veronese
Publikováno v:
Microbiome, Vol 8, Iss 1, Pp 1-20 (2020)
Abstract Background Despite the importance of the mucosal interface between microbiota and the host in gut homeostasis, little is known about the mechanisms of bacterial gut colonization, involving foraging for glycans produced by epithelial cells. T
Externí odkaz:
https://doaj.org/article/0da607aad04942898d172b17871996c9
Autor:
Elisabeth Laville, Josette Perrier, Nada Bejar, Marc Maresca, Jeremy Esque, Alexandra S. Tauzin, Emna Bouhajja, Marion Leclerc, Elodie Drula, Bernard Henrissat, Stephane Berdah, Eric Di Pasquale, Patrick Robe, Gabrielle Potocki-Veronese
Publikováno v:
Frontiers in Microbiology, Vol 10 (2019)
The human Intestinal mucus is formed by glycoproteins, the O- and N-linked glycans which constitute a crucial source of carbon for commensal gut bacteria, especially when deprived of dietary glycans of plant origin. In recent years, a dozen carbohydr
Externí odkaz:
https://doaj.org/article/ad4a9dcce15f4ef1b98584e3b8b87cff
Autor:
Xiaoqian Li, Guy Lippens, Jean-Luc Parrou, Gianluca Cioci, Jérémy Esque, Zhi Wang, Elisabeth Laville, Gabrielle Potocki-Veronese, Aurore Labourel
Publikováno v:
mSphere, Vol 9, Iss 8 (2024)
ABSTRACT In ruminants, the rumen is a specialized stomach that is adapted to the breakdown of plant-derived complex polysaccharides through the coordinated activities of a diverse microbial community. Bacteroidota is a major phylum in this bovine rum
Externí odkaz:
https://doaj.org/article/7bacb263be0349b686dd0b967040f6ff
Autor:
Elisabeth Laville, Josette Perrier, Nada Bejar, Marc Maresca, Jeremy Esque, Alexandra S. Tauzin, Emna Bouhajja, Marion Leclerc, Elodie Drula, Bernard Henrissat, Stephane Berdah, Eric Di Pasquale, Patrick Robe, Gabrielle Potocki-Veronese
Publikováno v:
Frontiers in Microbiology
Frontiers in Microbiology, Frontiers Media, 2019, 10, 12 p. ⟨10.3389/fmicb.2019.01286⟩
Frontiers in Microbiology, 2019, 10, 12 p. ⟨10.3389/fmicb.2019.01286⟩
Frontiers in Microbiology, Vol 10 (2019)
Frontiers in Microbiology (10), 12 p.. (2019)
Frontiers in Microbiology, Frontiers Media, 2019, 10, 12 p. ⟨10.3389/fmicb.2019.01286⟩
Frontiers in Microbiology, 2019, 10, 12 p. ⟨10.3389/fmicb.2019.01286⟩
Frontiers in Microbiology, Vol 10 (2019)
Frontiers in Microbiology (10), 12 p.. (2019)
The human Intestinal mucus is formed by glycoproteins, the O- and N-linked glycans which constitute a crucial source of carbon for commensal gut bacteria, especially when deprived of dietary glycans of plant origin. In recent years, a dozen carbohydr
Autor:
Stéphane Téletchéa, Jérémy Esque, Aurélie Urbain, Catherine Etchebest, Alexandre G. de Brevern
Publikováno v:
BioMedInformatics, Vol 3, Iss 2, Pp 306-326 (2023)
Transmembrane proteins (TMPs) are a class of essential proteins for biological and therapeutic purposes. Despite an increasing number of structures, the gap with the number of available sequences remains impressive. The choice of a dedicated function
Externí odkaz:
https://doaj.org/article/0229553b59f842e4a4f6396501008586
Autor:
Jeremy Esque, Marco Cecchini
Publikováno v:
The Journal of Physical Chemistry B. 119:5194-5207
The calculation of the free energy of conformation is key to understanding the function of biomolecules and has attracted significant interest in recent years. Here, we present an improvement of the confinement method that was designed for use in the
Autor:
Xixian Chen, Rehka T, Jérémy Esque, Congqiang Zhang, Sudha Shukal, Chin Chin Lim, Leonard Ong, Derek Smith, Isabelle André
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)
Retrosynthetic pathway design using promiscuous enzymes can provide a solution to the biosynthetic production of natural products. Here, the authors design a pathway for the production of cis-α-irone with a promiscuous methyltransferase using struct
Externí odkaz:
https://doaj.org/article/913a9e6923b0454cb3e5d54b2cd70510
Publikováno v:
Journal of Chemical Information and Modeling
Journal of Chemical Information and Modeling, American Chemical Society, 2011, 51 (2), pp.493-507. ⟨10.1021/ci100195t⟩
Journal of Chemical Information and Modeling, American Chemical Society, 2011, 51 (2), pp.493-507. ⟨10.1021/ci100195t⟩
International audience; The 3D structure of a protein is the main physical support of a protein's biological function; 3D protein folds are primarily maintained through interactions between amino acids. Inter-residue contacts are essential for the st
Autor:
Pierrick, Craveur, Agnel P, Joseph, Jeremy, Esque, Tarun J, Narwani, Floriane, Noël, Nicolas, Shinada, Matthieu, Goguet, Sylvain, Leonard, Pierre, Poulain, Olivier, Bertrand, Guilhem, Faure, Joseph, Rebehmed, Amine, Ghozlane, Lakshmipuram S, Swapna, Ramachandra M, Bhaskara, Jonathan, Barnoud, Stéphane, Téletchéa, Vincent, Jallu, Jiri, Cerny, Bohdan, Schneider, Catherine, Etchebest, Narayanaswamy, Srinivasan, Jean-Christophe, Gelly, Alexandre G, de Brevern
Publikováno v:
Frontiers in Molecular Biosciences
Protein structures are valuable tools to understand protein function. Nonetheless, proteins are often considered as rigid macromolecules while their structures exhibit specific flexibility, which is essential to complete their functions. Analyses of
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2013, 41 (Web Server issue), pp.W373-8. ⟨10.1093/nar/gkt509⟩
Nucleic Acids Research, 2013, 41 (Web Server issue), pp.W373-8. ⟨10.1093/nar/gkt509⟩
Nucleic Acids Research, Oxford University Press, 2013, 41 (Web Server issue), pp.W373-8. ⟨10.1093/nar/gkt509⟩
Nucleic Acids Research, 2013, 41 (Web Server issue), pp.W373-8. ⟨10.1093/nar/gkt509⟩
International audience; Protein structures are an ensemble of atoms determined experimentally mostly by X-ray crystallography or Nuclear Magnetic Resonance. Studying 3D protein structures is a key point for better understanding protein function at a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f10cdbcdd7f767231f25e70533857c89
https://www.hal.inserm.fr/inserm-00926547/document
https://www.hal.inserm.fr/inserm-00926547/document