"Porins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Porins are protein molecules that were originally found in the outer membrane of GRAM-NEGATIVE BACTERIA and that form multi-meric channels for the passive DIFFUSION of WATER; IONS; or other small molecules. Porins are present in bacterial CELL WALLS, as well as in plant, fungal, mammalian and other vertebrate CELL MEMBRANES and MITOCHONDRIAL MEMBRANES.
| Descriptor ID |
D018272
|
| MeSH Number(s) |
D12.776.157.530.400.500 D12.776.543.550.450.730 D12.776.543.585.400.730
|
| Concept/Terms |
|
Below are MeSH descriptors whose meaning is more general than "Porins".
Below are MeSH descriptors whose meaning is more specific than "Porins".
This graph shows the total number of publications written about "Porins" by people in this website by year, and whether "Porins" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1997 | 1 | 0 | 1 |
| 2009 | 1 | 0 | 1 |
| 2013 | 1 | 0 | 1 |
| 2016 | 1 | 1 | 2 |
| 2017 | 0 | 1 | 1 |
| 2021 | 0 | 1 | 1 |
To return to the timeline,
click here.
Below are the most recent publications written about "Porins" by people in Profiles.
-
Cysteine-based crosslinking approach for characterization of oligomeric pore-forming proteins in the mitochondrial membranes. Methods Enzymol. 2021; 649:371-396.
-
Synergy between Active Efflux and Outer Membrane Diffusion Defines Rules of Antibiotic Permeation into Gram-Negative Bacteria. mBio. 2017 10 31; 8(5).
-
Breaking the Permeability Barrier of Escherichia coli by Controlled Hyperporination of the Outer Membrane. Antimicrob Agents Chemother. 2016 12; 60(12):7372-7381.
-
Consensus computational network analysis for identifying candidate outer membrane proteins from Borrelia spirochetes. BMC Microbiol. 2016 07 11; 16(1):141.
-
Structural modeling and physicochemical characterization provide evidence that P66 forms a ß-barrel in the Borrelia burgdorferi outer membrane. J Bacteriol. 2014 Feb; 196(4):859-72.
-
Oligomerization of membrane-bound Bcl-2 is involved in its pore formation induced by tBid. Apoptosis. 2009 Oct; 14(10):1145-53.
-
Tromp1, a putative rare outer membrane protein, is anchored by an uncleaved signal sequence to the Treponema pallidum cytoplasmic membrane. J Bacteriol. 1997 Aug; 179(16):5076-86.