Zobrazeno 1 - 10
of 94
pro vyhledávání: '"Patrick Senet"'
Autor:
Tiffany Bellanger, David da Silva Barreira, Frank Wien, Patrice Delarue, Patrick Senet, Aurélie Rieu, Fabrice Neiers, Paloma Fernández Varela, Sophie Combet, Stéphanie Weidmann
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-13 (2023)
Abstract To cope with environmental stresses, bacteria have developed different strategies, including the production of small heat shock proteins (sHSP). All sHSPs are described for their role as molecular chaperones. Some of them, like the Lo18 prot
Externí odkaz:
https://doaj.org/article/76e3f6d5ea39476c850a874449bc79f8
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:
Mathieu Schwartz, Nicolas Petiot, Jeanne Chaloyard, Véronique Senty-Segault, Frédéric Lirussi, Patrick Senet, Adrien Nicolai, Jean-Marie Heydel, Francis Canon, Sanjiv Sonkaria, Varsha Khare, Claude Didierjean, Fabrice Neiers
Publikováno v:
Biomolecules, Vol 14, Iss 7, p 758 (2024)
This study presents a comprehensive analysis of the dimerization interfaces of fly GSTs through sequence alignment. Our investigation revealed GSTE1 as a particularly intriguing target, providing valuable insights into the variations within Delta and
Externí odkaz:
https://doaj.org/article/54e82adfb4474af494580a88b3c19d1b
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
Autor:
Patrick Senet
Publikováno v:
ACS Omega, Vol 5, Iss 39, Pp 25349-25357 (2020)
Externí odkaz:
https://doaj.org/article/6bcfdfa5d26443c5b69629247bee67ba
Autor:
Mathieu Schwartz, Valentin Boichot, Stéphane Fraichard, Mariam Muradova, Patrick Senet, Adrien Nicolai, Frederic Lirussi, Mathilde Bas, Francis Canon, Jean-Marie Heydel, Fabrice Neiers
Publikováno v:
Biomolecules, Vol 13, Iss 2, p 322 (2023)
Glutathione transferases (GSTs) are ubiquitous key enzymes with different activities as transferases or isomerases. As key detoxifying enzymes, GSTs are expressed in the chemosensory organs. They fulfill an essential protective role because the chemo
Externí odkaz:
https://doaj.org/article/2e8af21a8912460d8451ea47cc162677
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