Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Alexej Prilipov"'
Publikováno v:
Journal of Bacteriology. 180:3388-3392
The genomic DNA of the B E strain of Escherichia coli has been scrutinized to detect porin genes that have not been identified so far. Southern blot analysis yielded two DNA segments which proved highly homologous to, yet distinct from, the ompC , om
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1402ed4d89b2a63fc1a2f92c41820a8a
https://doi.org/10.1128/jb.180.13.3388-3392.1998
https://doi.org/10.1128/jb.180.13.3388-3392.1998
Publikováno v:
FEMS Microbiology Letters. 163:65-72
Combination of an origin repair mutagenesis system with a new mutS host strain increased the efficiency of mutagenesis from 46% to 75% mutant clones. Overexpression with the T7 expression system afforded large quantities of proteins from mutant strai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7145e71b99e80a113b0fc8c2af529f7a
https://doi.org/10.1111/j.1574-6968.1998.tb13027.x
https://doi.org/10.1111/j.1574-6968.1998.tb13027.x
Autor:
Gabriele Rummel, Tilman Schirmer, Kuo-Long Lou, Jurg P. Rosenbusch, Nathalie Saint, Alexej Prilipov, Spencer A. Benson
Publikováno v:
Journal of Biological Chemistry. 271:20669-20675
OmpF porin is a nonspecific pore protein from the outer membrane of Escherichia coli. Previously, a set of mutants was selected that allow the passage of long maltodextrins that do not translocate through the wild-type pore. Here, we describe the cry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::473ae74e077b9f582b1e2617e4493fe7
https://doi.org/10.1074/jbc.271.34.20669
https://doi.org/10.1074/jbc.271.34.20669
Autor:
Kuo-Long Lou, Prashant S. Phale, Tilman Schirmer, Ariane Hardmeyer, Alexej Prilipov, Jurg P. Rosenbusch
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 94(13)
In the homotrimeric OmpF porin from Escherichia coli , each channel is constricted by a loop protruding into the β-barrel of the monomer about halfway through the membrane. The water-filled channels exist in open or closed states, depending on the t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1634a89d3523864d1d0f027a02e91d01
https://pubmed.ncbi.nlm.nih.gov/9192635
https://pubmed.ncbi.nlm.nih.gov/9192635
Autor:
Ria van Boxtel, Jurg P. Rosenbusch, Prashant S. Phale, Alexej Prilipov, Elaine F Eppens, Jan Tommassen, Patrick Van Gelder, Nathalie Saint
Publikováno v:
Journal of molecular biology. 269(4)
The porins PhoE and OmpF form anion and cation-selective pores, respectively, in the outer membrane of Escherichia coli. Each monomer of these trimeric proteins consists of a 16-stranded beta-barrel, which contains a constriction at half the height o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba15ff7122b7fb76261ea6931defaff6
https://pubmed.ncbi.nlm.nih.gov/9217251
https://pubmed.ncbi.nlm.nih.gov/9217251
Autor:
Kuo-Long Lou, Nathalie Saint, Jurg P. Rosenbusch, Tilman Schirmer, Ariane Hardmeyer, Alexej Prilipov
Publikováno v:
Biochemical and biophysical research communications. 223(1)
The sole histidine residue in OmpF porin was replaced by threonine using site-directed mutagenesis. This exchange affected neither channel properties nor channel structure, as determined by X-ray analysis to 3.2 A. Conductance and critical voltage (V
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4355b30e0e465895433f354335f2f12e
https://pubmed.ncbi.nlm.nih.gov/8660355
https://pubmed.ncbi.nlm.nih.gov/8660355