"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 |
|---|
| 1995 | 0 | 1 | 1 |
| 1996 | 2 | 0 | 2 |
| 1997 | 2 | 0 | 2 |
| 1998 | 1 | 0 | 1 |
| 1999 | 3 | 0 | 3 |
| 2000 | 2 | 1 | 3 |
| 2001 | 1 | 0 | 1 |
| 2002 | 1 | 0 | 1 |
| 2003 | 3 | 0 | 3 |
| 2004 | 4 | 1 | 5 |
| 2005 | 2 | 2 | 4 |
| 2008 | 0 | 1 | 1 |
| 2009 | 1 | 0 | 1 |
| 2010 | 2 | 1 | 3 |
| 2018 | 1 | 0 | 1 |
| 2021 | 2 | 1 | 3 |
| 2022 | 0 | 3 | 3 |
To return to the timeline,
click here.
Below are the most recent publications written about "Porins" by people in Profiles.
-
Identification of amino acid domains of Borrelia burgdorferi P66 that are surface exposed and important for localization, oligomerization, and porin function of the protein. Front Cell Infect Microbiol. 2022; 12:991689.
-
Systematic Analysis of Mobile Genetic Elements Mediating ?-Lactamase Gene Amplification in Noncarbapenemase-Producing Carbapenem-Resistant Enterobacterales Bloodstream Infections. mSystems. 2022 10 26; 7(5):e0047622.
-
Human Monoclonal Antibodies to Escherichia coli Outer Membrane Protein A Porin Domain Cause Aggregation but Do Not Alter In Vivo Bacterial Burdens in a Murine Sepsis Model. Infect Immun. 2022 06 16; 90(6):e0017622.
-
Lsm12 is an NAADP receptor and a two-pore channel regulatory protein required for calcium mobilization from acidic organelles. Nat Commun. 2021 08 06; 12(1):4739.
-
IS26-mediated amplification of blaOXA-1 and blaCTX-M-15 with concurrent outer membrane porin disruption associated with de novo carbapenem resistance in a recurrent bacteraemia cohort. J Antimicrob Chemother. 2021 01 19; 76(2):385-395.
-
Functional and structural characterization of Hyp730, a highly conserved and dormancy-specific hypothetical membrane protein. Microbiologyopen. 2021 01; 10(1):e1154.
-
Characterization of Stress and Innate Immunity Resistance of Wild-Type and ?p66 Borrelia burgdorferi. Infect Immun. 2018 02; 86(2).
-
Single-virus tracking reveals a spatial receptor-dependent search mechanism. Biophys J. 2011 Jun 22; 100(12):2875-82.
-
Rotavirus disrupts calcium homeostasis by NSP4 viroporin activity. mBio. 2010 Nov 30; 1(5).
-
C-reactive protein adversely alters the protein-protein interaction of the endothelial isoform of nitric oxide synthase. Clin Chem. 2010 Aug; 56(8):1345-8.