Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Adrien Nicolaï"'
Autor:
Nicolas Petiot, Mathieu Schwartz, Patrice Delarue, Patrick Senet, Fabrice Neiers, Adrien Nicolaï
Publikováno v:
Biomolecules, Vol 14, Iss 7, p 759 (2024)
Glutathione transferase (GST) is a superfamily of ubiquitous enzymes, multigenic in numerous organisms and which generally present homodimeric structures. GSTs are involved in numerous biological functions such as chemical detoxification as well as c
Externí odkaz:
https://doaj.org/article/07c52687a9334bf18936c65551a5d312
Autor:
Andreina Urquiola Hernández, Patrice Delarue, Christophe Guyeux, Adrien Nicolaï, Patrick Senet
Publikováno v:
Frontiers in Nanotechnology, Vol 5 (2023)
Proteins are essential biological molecules to use as biomarkers for early disease diagnosis. Therefore, their detection is crucial. In recent years, protein sequencing has become one of the most promising techniques. In particular, solid-state nanop
Externí odkaz:
https://doaj.org/article/4eb18696c37a43c9a56162ca430ecd06
Autor:
Steve Tyler, Christophe Laforge, Adrien Guzzo, Adrien Nicolaï, Gia G. Maisuradze, Patrick Senet
Publikováno v:
Molecules, Vol 28, Iss 18, p 6659 (2023)
The folded structures of proteins can be accurately predicted by deep learning algorithms from their amino-acid sequences. By contrast, in spite of decades of research studies, the prediction of folding pathways and the unfolded and misfolded states
Externí odkaz:
https://doaj.org/article/1e0a764c1a2c48d6be7cb56a2de89458
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
α-Synuclein is a 140 amino-acid intrinsically disordered protein mainly found in the brain. Toxic α-synuclein aggregates are the molecular hallmarks of Parkinson’s disease. In vitro studies showed that α-synuclein aggregates in oligomeric struct
Externí odkaz:
https://doaj.org/article/c3eb8fd9f12c465f8453ba015b6785a7
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
α-Synuclein is an intrinsically disordered protein occurring in different conformations and prone to aggregate in β-sheet structures, which are the hallmark of the Parkinson disease. Missense mutations are associated with familial forms of this neu
Externí odkaz:
https://doaj.org/article/112f16c14a3c47bbb2e9336e93c00391
Autor:
Adrien Nicolaï, Nicolas Petiot, Paul Grassein, Patrice Delarue, Fabrice Neiers, Patrick Senet
Publikováno v:
Applied Sciences, Vol 12, Iss 16, p 8196 (2022)
Glutathione transferases (GSTs) are a superfamily of enzymes which have in common the ability to catalyze the nucleophilic addition of the thiol group of reduced glutathione (GSH) onto electrophilic and hydrophobic substrates. This conjugation reacti
Externí odkaz:
https://doaj.org/article/052ba3f141164e8b97640b6b954a3321
Autor:
Stéphane Fraichard, Daniel Gonzalez, Paul Grassein, Patrice Delarue, Patrick Senet, Adrien Nicolaï, Evelyne Chavanne, Elodie Mucher, Yves Artur, Jean-François Ferveur, Jean-Marie Heydel, Loïc Briand, Fabrice Neiers
Publikováno v:
Data in Brief, Vol 20, Iss , Pp 254-257 (2018)
The data presented in this article are related to the research article entitled “Characterization of a Drosophila glutathione transferase involved in isothiocyanate detoxification.” (Gonzalez et al., 2018) [1]. This article includes the expressio
Externí odkaz:
https://doaj.org/article/487ae45e49264bd289e2d48f0cdd3d7b
Publikováno v:
ACS Omega, Vol 1, Iss 6, Pp 1067-1074 (2016)
Externí odkaz:
https://doaj.org/article/ea51de1e12f148e99f52fa87918e4629
Publikováno v:
PLoS Computational Biology, Vol 9, Iss 12, p e1003379 (2013)
ATP regulates the function of many proteins in the cell by transducing its binding and hydrolysis energies into protein conformational changes by mechanisms which are challenging to identify at the atomic scale. Based on molecular dynamics (MD) simul
Externí odkaz:
https://doaj.org/article/130146fe93ad4fb19c49dd1f266cae5b
Autor:
Adrien, Guzzo, Patrice, Delarue, Ana, Rojas, Adrien, Nicolaï, Gia G, Maisuradze, Patrick, Senet
Publikováno v:
Frontiers in molecular biosciences. 9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c17fc930344397d808f8dc869f96186e
https://pubmed.ncbi.nlm.nih.gov/35836937
https://pubmed.ncbi.nlm.nih.gov/35836937