Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Francois Bontems"'
Autor:
Francois Bontems
Publikováno v:
Natures Sciences Sociétés. 30:317-324
Autor:
Marie S. Prevost, Nathalie Barilone, Gabrielle Dejean de la Bâtie, Stéphanie Pons, Gabriel Ayme, Patrick England, Marc Gielen, François Bontems, Gérard Pehau-Arnaudet, Uwe Maskos, Pierre Lafaye, Pierre-Jean Corringer
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)
Abstract The human α7 nicotinic receptor is a pentameric channel mediating cellular and neuronal communication. It has attracted considerable interest in designing ligands for the treatment of neurological and psychiatric disorders. To develop a nov
Externí odkaz:
https://doaj.org/article/d6e9fbacc04e466aa0ecb78f49b2c30d
Autor:
Benedict Akinyamoju, Ezinne Amanda Nnebocha, Sam Epete, Esuru Rita Okoroafor, Francois Bontems, Chiedu Andrew Enwemadu, Marco Ciaroni, Kamaljeet Singh
Publikováno v:
All Days.
Drilling in progressively deeper water environments requires that even more attention be given to well integrity because of the serious implications to health, safety and environment. Conventional cement evaluation tools have been available for many
Autor:
Marc Guérineau, Luiza Bessa, Séverine Moriau, Ewen Lescop, François Bontems, Nathalie Mathy, Eric Guittet, Julien Bischerour, Mireille Bétermier, Nelly Morellet
Publikováno v:
Mobile DNA, Vol 12, Iss 1, Pp 1-22 (2021)
Abstract Background Transposons are mobile genetic elements that colonize genomes and drive their plasticity in all organisms. DNA transposon-encoded transposases bind to the ends of their cognate transposons and catalyze their movement. In some case
Externí odkaz:
https://doaj.org/article/efda5350ace14a0aa672aa28e0ea173d
Publikováno v:
Peptides ISBN: 9789401050050
Peptides
Peptides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::96b4b8ad5df8f4d3b30b2cdafbdc8aa1
https://doi.org/10.1007/978-94-011-2264-1_67
https://doi.org/10.1007/978-94-011-2264-1_67
Publikováno v:
Science (New York, N.Y.). 254(5037)
Conflicting three-dimensional structures of charybdotoxin (Chtx), a blocker of K+ channels, have been previously reported. A high-resolution model depicting the tertiary structure of Chtx has been obtained by DIANA and X-PLOR calculations from new pr
Autor:
Christophe Cardone, Claire-Marie Caseau, Benjamin Bardiaux, Aurélien Thureaux, Marie Galloux, Monika Bajorek, Jean-François Eléouët, Marc Litaudon, François Bontems, Christina Sizun
Publikováno v:
Biomolecules, Vol 11, Iss 8, p 1225 (2021)
The phosphoprotein P of Mononegavirales (MNV) is an essential co-factor of the viral RNA polymerase L. Its prime function is to recruit L to the ribonucleocapsid composed of the viral genome encapsidated by the nucleoprotein N. MNV phosphoproteins of
Externí odkaz:
https://doaj.org/article/a64137b10a9842f4b354c6bf8f13e94c
Autor:
Marie-Lise Blondot, Virginie Dubosclard, Jenna Fix, Safa Lassoued, Magali Aumont-Nicaise, François Bontems, Jean-François Eléouët, Christina Sizun
Publikováno v:
PLoS Pathogens, Vol 8, Iss 5, p e1002734 (2012)
Respiratory syncytial virus (RSV) protein M2-1 functions as an essential transcriptional cofactor of the viral RNA-dependent RNA polymerase (RdRp) complex by increasing polymerase processivity. M2-1 is a modular RNA binding protein that also interact
Externí odkaz:
https://doaj.org/article/9ce5ff1c455d4da78dc075aead552d90
Autor:
Dorothea Bankwitz, Steven K. H. Foung, Ieva Vasiliauskaite, Arvind H. Patel, Thomas Krey, Joseph Marcotrigiano, Sarah Cole, Patrick England, Félix A. Rey, Ania M. Owsianka, Thomas Pietschmann, Abdul Ghafoor Khan
Publikováno v:
mBio
mBio, Vol 8, Iss 3 (2017)
mBio, 2017, 8 (3), pp.e00382-17. ⟨10.1128/mBio.00382⟩
mBio, Vol 8, Iss 3, p e00382-17 (2017)
mBio, Vol 8, Iss 3 (2017)
mBio, 2017, 8 (3), pp.e00382-17. ⟨10.1128/mBio.00382⟩
mBio, Vol 8, Iss 3, p e00382-17 (2017)
The hepatitis C virus (HCV) glycoprotein E2 is the major target of neutralizing antibodies and is therefore highly relevant for vaccine design. Its structure features a central immunoglobulin (Ig)-like β-sandwich that contributes to the binding site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46115abb57c9817644e9aa1c663e240b
https://eprints.gla.ac.uk/140242/1/140242.pdf
https://eprints.gla.ac.uk/140242/1/140242.pdf
Autor:
Saïda, Fakhri
Publikováno v:
Sciences du Vivant [q-bio]. Ecole Polytechnique X, 2003. Français
The restriction endoribonuclease RegB from the bacteriophage T4 is involved in the transition between the early and the middle phase of the lytic cycle of the virus. RegB cleaves with an almost absolute specificity the GGAG sequence needed for the ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::3215c2ba85023e0d7b7b1f3f5c2c49c9
https://pastel.archives-ouvertes.fr/pastel-00000707/document
https://pastel.archives-ouvertes.fr/pastel-00000707/document