Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Valérie Simonet"'
Autor:
Christophe Fremaux, Jean-Marc Berjeaud, Laurence Simon, Karine Dalet, Jacques Frère, Yves Cenatiempo, Valérie Simonet, Willy Aucher
Publikováno v:
FEMS Microbiology Letters. 232:15-22
Leuconostoc mesenteroides Y105 and L. mesenteroides FR52 produce both mesentericin Y105 and B105, in equal amounts. The mesentericin operons of L. mesenteroides FR52 and Y105 which are involved in mesentericin Y105 and B105 production, were both sequ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b776322bf757d97c468666772dd3224
https://doi.org/10.1016/s0378-1097(04)00011-4
https://doi.org/10.1016/s0378-1097(04)00011-4
Publikováno v:
Biochemical Journal. 376:245-252
The L3 loop is an important feature of the OmpF porin structure, contributing to both channel size and electrostatic properties. Colicins A and N, spermine, and antibiotics that use OmpF to penetrate the cell, were used to investigate the structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::092d75050bc15a39a850cd64196ddeca
https://doi.org/10.1042/bj20030814
https://doi.org/10.1042/bj20030814
Autor:
Jérôme BREDIN, Nathalie SAINT, Monique MALLÉA, Emmanuelle DÉ, Gérard MOLLE, Jean-Marie PAGÈS, Valérie SIMONET
Publikováno v:
Biochemical Journal. 363:521-528
The Escherichia coli OmpF pore is governed by an internal constriction consisting of the negatively charged loop 3 folded into the lumen and the positively charged barrel wall located on the opposite side across the pore, ‘anti-loop 3'. To investig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8f10979cf4031d53309164ff8a5f05a5
https://doi.org/10.1042/bj3630521
https://doi.org/10.1042/bj3630521
Publikováno v:
Antimicrobial Agents and Chemotherapy. 44:311-315
The Escherichia coli OmpF porin is a nonspecific channel involved in the membrane translocation of small hydrophilic molecules and especially in the passage of β-lactam antibiotics. In order to understand the dynamic of charged-compound uptake throu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c00b69e69d8aafcb68e6fd4f1871722
https://doi.org/10.1128/aac.44.2.311-315.2000
https://doi.org/10.1128/aac.44.2.311-315.2000
Publikováno v:
ResearcherID
With the recent resolution of the crystal structures of several bacterial porins, it is worthwhile to define the generality of their organization throughout the Enterobacteriaceae. The distribution of specific epitopes was analysed among various Gram
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10972ddbcbb8a9fe4061a686e5099ab4
https://doi.org/10.1111/j.1574-6968.1996.tb08030.x
https://doi.org/10.1111/j.1574-6968.1996.tb08030.x
Autor:
Valérie Simonet, Monique Malléa, Ekkehard Collatz, Laurent Gutmann, Eun-Hee Lee, Jean-Marie Pagès, Régis Gervier
Publikováno v:
FEMS Microbiology Letters. 129:273-279
Bacteriocin susceptibilities indicate that during cloacin DF13 uptake the F porin of Enterobacter cloacae plays a similar role to that reported for the OmpF porin of Escherichia coli during colicin A entry. The translocatory activities of these two p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f78dba629ece2b82dc1f5d6af989875
https://doi.org/10.1016/0378-1097(95)00171-z
https://doi.org/10.1016/0378-1097(95)00171-z
Autor:
Régis Gervier, Jean-Marie Pagès, Valérie Simonet, Ekkehard Collatz, Monique Malléa, Laurent Gutmann, Eun-Hee Lee
Publikováno v:
FEMS Microbiology Letters. 129:273-279
Bacteriocin susceptibilities indicate that during cloacin DF13 uptake the F porin of Enterobacter cloacae plays a similar role to that reported for the OmpF porin of Escherichia coli during colicin A entry. The translocatory activities of these two p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0dc34a29366737f355879786ae5e4884
https://doi.org/10.1111/j.1574-6968.1995.tb07592.x
https://doi.org/10.1111/j.1574-6968.1995.tb07592.x
Autor:
Jérôme, Bredin, Nathalie, Saint, Monique, Malléa, Emmanuelle, Dé, Gérard, Molle, Jean-Marie, Pagès, Valérie, Simonet
Publikováno v:
The Biochemical journal. 363(Pt 3)
The Escherichia coli OmpF pore is governed by an internal constriction consisting of the negatively charged loop 3 folded into the lumen and the positively charged barrel wall located on the opposite side across the pore, 'anti-loop 3'. To investigat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b3c841c128c56065f5e96219452558ef
https://pubmed.ncbi.nlm.nih.gov/11964152
https://pubmed.ncbi.nlm.nih.gov/11964152
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/
