Zobrazeno 1 - 10
of 181
pro vyhledávání: '"M. Knossow"'
Publikováno v:
INRAE Productions Animales, Vol 17, Iss HS (2004)
Le polymorphisme génétique de la protéine prion ovine associé à des degrés divers de résistance ou de sensibilité à la tremblante ouvre une voie féconde pour comprendre le lien entre les propriétés structurales de la protéine et le méca
Externí odkaz:
https://doaj.org/article/1876606db0274f1fa5b8b0080c7c3310
Publikováno v:
Structure. 7:1385-1393
Background: Small organic molecules coupled to a carrier protein elicit an antibody response on immunisation. The diversity of this response has been found to be very narrow in several cases. Some antibodies also catalyse chemical reactions. Such cat
Publikováno v:
Topics in current chemistry. 286
Microtubules (MTs) are dynamic structures of the eukaryotic cytoskeleton that, during cell division, form the mitotic spindle. Perturbing them leads to mitotic arrest and ultimately to cell death. Consistently, MTs and their building block, αβ tubu
Publikováno v:
Journal of Virology. 65:4853-4859
In an attempt to understand the implication of the rabies virus glycoprotein (G) in the first steps of the viral cycle, we studied the pH dependence of virus-induced fusion and hemagglutination, as well as modifications of the structure and propertie
Publikováno v:
Pathologie-biologie. 51(1)
Stathmin family proteins interact with tubulin and negatively regulate its assembly in microtubules. One stathmin molecule forms a complex with two alphabeta tubulin heterodimers in an interaction that is weakened upon stathmin phosphorylation. The X
Publikováno v:
Current topics in microbiology and immunology. 260
Autor:
B. Gigant, B. Barrere, M. Knossow, C. Barbey-Martin, D. Fleury, J.J. Skehel, Thierry Bizebard
Publikováno v:
Current Topics in Microbiology and Immunology ISBN: 9783642074868
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::289f7b0a502f76b5c789c90758e3f146
https://doi.org/10.1007/978-3-662-05783-4_4
https://doi.org/10.1007/978-3-662-05783-4_4
Publikováno v:
Proteins. 40(4)
The structure of a complex between the hemagglutinin of influenza virus and the Fab of a neutralizing antibody was determined by X-ray crystallography at 2.8 A resolution. This antibody and another which has only 56% sequence identity bind to the sam
Publikováno v:
Nature structural biology. 6(6)
The structure of a complex of influenza hemagglutinin (HA) with a neutralizing antibody shows that the antibody binds to HA at a distance from the virus receptor binding site. Comparison of the properties of this antibody and its Fab with those of an
Fusion of rabies virus with membranes occurs at acidic pH and is mediated by the viral spike glycoprotein (G). In this paper, we provide the basis for a description of structural transitions associated with exposure to low pH and of their role in mem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24a027bd5341e18c996aba033a8c196f
https://europepmc.org/articles/PMC237506/
https://europepmc.org/articles/PMC237506/