The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Porins and specific channels of bacterial outer membranes
Abstract
Summary: Porins and specific channels both produce water‐filled pores that allow the transmembrane diffusion of small solutes, but the latter contain specific ligandbinding sites within the channels. Recent structural studies show that many or most of these proteins exist as βbarrels with the βstrands traversing the thickness of the outer membrane. The channels often have diameters in the range of 1 nm, and thus the penetration rates of solutes through porin channels are likely to be affected strongly by what appear to be minor differences in the size, shape, hydrophobicity or charge of the solute molecule. With the specific channels, the presence of binding sites can accelerate very significantly the diffusion of some ligands when they are present at low concentrations. Thus these simple channels can sometimes achieve a surprising degree of real or apparent specificity. Recent data tend to favour the idea that these proteins are first exported into the periplasm, and then inserted into the outer membrane. Although lipopolysaccharides seem to play a significant role in the final assembly of the trimeric porins, the details of the targeting process still remain to be elucidated.
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Cites
Molecular basis of bacterial outer membrane permeability
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Self-citationProtein phosphorylation and regulation of adaptive responses in bacteria
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The structure of porin from Rhodobacter capsulatus at 1.8 Å resolution
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Structure And Function Of Porins From Gram Negative Bacteria
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Pore-forming activity of OmpA protein of Escherichia coli.
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Self-citationMizuno, T., & Mizushima, S. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb00681.x · Cited by 228
Vitamin B12 transport in Escherichia coli: energy coupling between membranes
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Cited by
Molecular Basis of Bacterial Outer Membrane Permeability Revisited
Nikaido, H. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.4.593-656.2003 · Cited by 4,316
Self-citationPrevention of Drug Access to Bacterial Targets: Permeability Barriers and Active Efflux
Nikaido, H. (1994) · Science · doi:10.1126/science.8153625 · Cited by 1,540
Self-citationCrystal structures explain functional properties of two E. coli porins
Cowan, S. W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R. A., Jansonius, J. N., & Rosenbusch, J. P. (1992) · Nature · doi:10.1038/358727a0 · Cited by 1,520
Saier, M. H., Tam, R., Reizer, A., & Reizer, J. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb00362.x · Cited by 371
Porins and specific diffusion channels in bacterial outer membranes.
Nikaido, H. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41716-9 · Cited by 370
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Metadata
- Authors
- Nikaido, H.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 1992-02
- Volume
- 6
- Issue
- 4
- Pages
- 435-442
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2121924211
- Cited by
- 340
- References
- 36
- FWCI
- 21.76
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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