Zobrazeno 1 - 10
of 46
pro vyhledávání: '"I. Petitpas"'
Publikováno v:
Molecular Microbiology. 91:1164-1178
Bacteriophage SPP1 is a nanomachine built to infect the bacterium Bacillus subtilis. The phage particle is composed of an icosahedric capsid, which contains the viral DNA, and a long non-contractile tail. Capsids and tails are produced in infected ce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80b8c38181875e962681cc6ba3b20b64
https://doi.org/10.1111/mmi.12526
https://doi.org/10.1111/mmi.12526
Autor:
Bernard Gilquin, Benjamin Chagot, Paulo Tavares, Matthieu Gallopin, I. Petitpas, Isabelle Auzat, Sophie Zinn-Justin
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 80:319-326
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::57577511eed5c67f97922dc0d5d15905
https://doi.org/10.1002/prot.23191
https://doi.org/10.1002/prot.23191
Autor:
J. Ghuman, A.A. Bhattacharya, Masaki Otagiri, Stephen Curry, I. Petitpas, Patricia A. Zunszain
Publikováno v:
Journal of Molecular Biology. 353:38-52
Human serum albumin (HSA) is an abundant plasma protein that binds a remarkably wide range of drugs, thereby restricting their free, active concentrations. The problem of overcoming the binding affinity of lead compounds for HSA represents a major ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1195d3ca874a53227fec9cb73e9b323c
https://doi.org/10.1016/j.jmb.2005.07.075
https://doi.org/10.1016/j.jmb.2005.07.075
Publikováno v:
Journal of Biological Chemistry. 276:22804-22809
Human serum albumin (HSA) is an abundant transport protein found in plasma that binds a wide variety of drugs in two primary binding sites (I and II) and can have a significant impact on their pharmacokinetics. We have determined the crystal structur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c77bd0e449de1399657a92552621adb3
https://doi.org/10.1074/jbc.m100575200
https://doi.org/10.1074/jbc.m100575200
Autor:
Pierre Pothier, B. V. Venkataram Prasad, Jean Cohen, I. Petitpas, Evelyne Kohli, Jean Lepault, Magali Mathieu, Jorge Navaza, Félix A. Rey
Publikováno v:
The EMBO Journal. 20:1485-1497
The structural protein VP6 of rotavirus, an important pathogen responsible for severe gastroenteritis in children, forms the middle layer in the triple-layered viral capsid. Here we present the crystal structure of VP6 determined to 2 A resolution an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e37b008add010ce6055ca0b6031da373
https://doi.org/10.1093/emboj/20.7.1485
https://doi.org/10.1093/emboj/20.7.1485
Autor:
I. Petitpas
Publikováno v:
Médecine et Maladies Infectieuses. 29:573-580
Resume Objectifs Les rotavirus sont la principale cause de gastroenterites severes chez les jeunes enfants a travers le monde. Ils sont constitues d'une capside icosaedrique renfermant 11 segments d'ARN bicatenaire. Cette capside comporte trois couch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cc045b04f70081ba7816545bd4066152
https://doi.org/10.1016/s0399-077x(00)80086-4
https://doi.org/10.1016/s0399-077x(00)80086-4
Autor:
Félix A. Rey, Evelyne Kohli, Annie Charpilienne, Patrice Vachette, Jean Cohen, I. Petitpas, Pierre Pothier, Magali Mathieu, Jean Lepault
Publikováno v:
Journal of Virology. 72:7615-7619
As a first step to gain insight into the structure of the rotavirus virion at atomic resolution, we report here the expression, purification, and crystallization of recombinant rotavirus protein VP6. This protein has the property of polymerizing in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2be6e388126df3aa0e82a068a09b75d
https://doi.org/10.1128/jvi.72.9.7615-7619.1998
https://doi.org/10.1128/jvi.72.9.7615-7619.1998
Autor:
Félix A. Rey, Aure Saulnier, Annette Martin, Patrick England, Carlos M. Kikuti, Bruno Baron, Bruno Robert, I. Petitpas, Mats A. A. Persson, Laurence Damier-Piolle, Rajiv G. Tawar, Daniel X. Johansson, Thomas Krey, Jacques d'Alayer
Publikováno v:
PLoS Pathogens, Vol 6, Iss 2, p e1000762 (2010)
PLoS Pathogens
PLoS Pathogens, Public Library of Science, 2010, 6 (2), pp.e1000762. ⟨10.1371/journal.ppat.1000762⟩
PLoS Pathogens, 2010, 6 (2), pp.e1000762. ⟨10.1371/journal.ppat.1000762⟩
PLoS Pathogens
PLoS Pathogens, Public Library of Science, 2010, 6 (2), pp.e1000762. ⟨10.1371/journal.ppat.1000762⟩
PLoS Pathogens, 2010, 6 (2), pp.e1000762. ⟨10.1371/journal.ppat.1000762⟩
Hepatitis C virus (HCV), a major cause of chronic liver disease in humans, is the focus of intense research efforts worldwide. Yet structural data on the viral envelope glycoproteins E1 and E2 are scarce, in spite of their essential role in the viral
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f65baf646a5f2d203413ee015c250fd2
http://europepmc.org/articles/PMC2824758?pdf=render
http://europepmc.org/articles/PMC2824758?pdf=render
Autor:
Nadhipuram V. Bhagavan, I. Petitpas, Jeffrey R. Simard, James A. Hamilton, Patricia A. Zunszain, Stephen Curry, Chung-Eun Ha, Jinsheng Yang
Human serum albumin (HSA) is a versatile transport protein for endogenous compounds and drugs. To evaluate physiologically relevant interactions between ligands for the protein, it is necessary to determine the locations and relative affinities of di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbade2aaed24b9aa9daa6cef91ba22c3
https://europepmc.org/articles/PMC1312385/
https://europepmc.org/articles/PMC1312385/
Autor:
Charles E. Petersen, Nadhipuram V. Bhagavan, I. Petitpas, J. Ghuman, Chung-Eun Ha, Patricia A. Zunszain, A.A. Bhattacharya, Stephen Curry
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 100(11)
Human serum albumin (HSA) is the major protein component of blood plasma and serves as a transporter for thyroxine and other hydrophobic compounds such as fatty acids and bilirubin. We report here a structural characterization of HSA–thyroxine inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2aa62e3b733c435852ba075247fe34b6
https://pubmed.ncbi.nlm.nih.gov/12743361
https://pubmed.ncbi.nlm.nih.gov/12743361