Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Denis Jeanteur"'
Publikováno v:
Journal of Molecular Biology. 235:898-907
The ion-channel forming C-terminal fragment of colicin A binds to negatively charged lipid vesicles and provides an example of the insertion of a soluble protein into a lipid bilayer. The soluble structure is known and consists of a ten-helix bundle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a0b1d3f134d5f3238584ec60e23d3c41
https://doi.org/10.1006/jmbi.1994.1047
https://doi.org/10.1006/jmbi.1994.1047
Autor:
Kosuke Morikawa, Katsuo Katayanagi, Denis Jeanteur, Tatsuki Kashiwagi, Shigenori Kanaya, Mitsuru Haruki
Publikováno v:
Protein engineering. 9(10)
Three mutants of Escherichia coli ribonuclease HI, in which an invariant acidic residue Asp134 was replaced, were crystallized, and their three-dimensional structures were determined by X-ray crystallography. The D134A mutant is completely inactive,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a83a68eb4f30204e5b302541cb69d1cf
https://pubmed.ncbi.nlm.nih.gov/8931125
https://pubmed.ncbi.nlm.nih.gov/8931125
Publikováno v:
Molecular microbiology. 16(5)
Pseudomonas aeruginosa OprD is a 420-amino-acid protein that facilitates the uptake of basic amino acids, imipenem and gluconate across the outer membrane. OprD was the first specific porin that could be aligned with members of the non-specific porin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51f55ed06254a70df6118fabf5bdb025
https://pubmed.ncbi.nlm.nih.gov/7476190
https://pubmed.ncbi.nlm.nih.gov/7476190
Autor:
Valérie Simonet, Jean-Marie Pagès, Gabriele Rummel, Christine Widmer, Didier Fourel, Jurg P. Rosenbusch, Franc Pattus, Tilman Schirmer, Denis Jeanteur
A strain of Escherichia coli, selected on the basis of its resistance to colicin N, reveals distinct structural and functional alterations in unspecific OmpF porin. A single mutation [Gly-119-->Asp (G119D)] was identified in the internal loop L3 that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::911649e21bf78b7b46b38aae6aa3f903
https://europepmc.org/articles/PMC45084/
https://europepmc.org/articles/PMC45084/
Publisher Summary This chapter discusses the diversity and common features of the porin superfamily. The name porin was first used by Taiji Nakae in 1976 to describe a class of oligomeric proteins from the outer membrane of Gram-negative bacteria whi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c5ec4ece68dd7e5db7d97b28e1f92a4c
https://doi.org/10.1016/s0167-7306(08)60420-2
https://doi.org/10.1016/s0167-7306(08)60420-2
Autor:
Juan Manuel González-Mañas, H. U. Wilmsen, Franc Pattus, Dominique Massotte, Jeremy H. Lakey, Denis Jeanteur, F. G. van der Goot, S. Scianimanico, N. Didat
Publikováno v:
The Jerusalem Symposia on Quantum Chemistry and Biochemistry ISBN: 9789401052054
Colicin A from Citrobacter freundii and aerolysin from Aeromonas hydrophila are representatives of two classes of pore-forming toxins. Colicin A, an alpha-helical protein, contains a hydrophobic hairpin which is buried inside the structure in solutio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb8e8a4224b551e98dd452a2d78e3cd4
https://doi.org/10.1007/978-94-011-2718-9_31
https://doi.org/10.1007/978-94-011-2718-9_31