OMPF Antibody

1. Trimeric porins, such as ompF, have specific lipopolysaccharide binding sites that are essential for porin biogenesis. PMID: 27493217
2. Klebsiella pneumoniae OmpK35 and OmpK36 produced larger more permeable channels than their Escherichia coli homologs OmpF and OmpC. PMID: 27645385
3. Two different centered monoclinic crystals of the E. coli outer-membrane protein OmpF originate from the same building block PMID: 26620074
4. The site of lipopolysaccharide binding means that ColN will preferably bind at the interface and thus position itself close to the surface of its translocon component, OmpF. PMID: 24589252
5. they studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. PMID: 23812713
6. Presence of ordered aliphatic chains close to a positively charged area on the porin surface suggests a position for a lipopolysaccharide binding site on the surface of the major E. coli porins. PMID: 22484237
7. Data report the structure of the OmpF-OBS1 complex that shows the colicin bound within the porin lumen spanning the membrane bilayer. PMID: 21098297
8. This D37V mutant expressed reduced cation selectivity, in agreement with the view that D37 in wild-type OmpF is fully ionized, i.e., deprotonated. PMID: 20521145
9. HPA3P, an analogue of the antimicrobial peptide HP(2-20) isolated from the N-terminal region of the Helicobacter pylori ribosomal protein interacts with OmpF in a voltage- and concentration-dependent manner. PMID: 20180000
10. These data suggest that OmpF plays a key role in the transportation of positively charged polypyridyl chlororuthenium complexes into E. coli. PMID: 20176402
11. Separate pathways of anions and cations across the constriction zone of the OmpF pore. PMID: 19932117
12. study shows that quite different factors account for the selectivity of large channels. The elucidation of these factors is essential for understanding large channel selectivity and its regulation in vivo. PMID: 19134471
13. deletions of single extracellular loops affect pH sensitivity but not voltage dependence; study has provided some clues on the molecular determinants that underlie two major forms of modulation of OmpF porin activity by transmembrane voltage and acidic pH PMID: 15469993
14. for the classical porins OmpF and OmpC, our results show that the Cpx envelope stress response system plays a role in regulating their expression PMID: 16077119
15. OmpR allows distinct stepwise regulation of ompF and ompC transcription, which minimizes their overlapping expression upon changes in the medium osmolarity to achieve the reciprocal expression of ompF and ompC PMID: 16618701
16. D127 is not a key residue in the control mechanism of the voltage-dependent gating of OmpF PMID: 16858566
17. OmpF or OmpC can function in the translocon complex of the colicin E2 R-domain and its BtuB receptor PMID: 17548346
18. Colicin is closely associated with the OmpF-lipid interface, providing evidence that this peripheral pathway may play a role in colicin transmembrane transport. PMID: 18334212
19. The incremental electron density could be modelled as an extended poly-glycine peptide of at least seven residues. It overlapped the Mg2+ binding site obtained without T83, explaining the absence of peptide binding in the presence of Mg2+. PMID: 18636093

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KEGG: ecj:JW0912

STRING: 316385.ECDH10B_0999