Adhesins, Escherichia coli
"Adhesins, Escherichia coli" 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.
Thin, filamentous protein structures, including proteinaceous capsular antigens (fimbrial antigens), that mediate adhesion of E. coli to surfaces and play a role in pathogenesis. They have a high affinity for various epithelial cells.
Adhesins, Escherichia coli
- Adhesins, Escherichia coli
- Escherichia coli Adhesins
- Adhesin, E coli
- E coli Adhesin
- Adhesin, Escherichia coli
- Escherichia coli Adhesin
Below are MeSH descriptors whose meaning is more general than "Adhesins, Escherichia coli".
- Chemicals and Drugs [D]
- Amino Acids, Peptides, and Proteins [D12]
- Proteins [D12.776]
- Bacterial Proteins [D12.776.097]
- Bacterial Outer Membrane Proteins [D12.776.097.120]
- Adhesins, Bacterial [D12.776.097.120.050]
- Adhesins, Escherichia coli [D12.776.097.120.050.040]
- Escherichia coli Proteins [D12.776.097.275]
- Adhesins, Escherichia coli [D12.776.097.275.500]
- Membrane Proteins [D12.776.543]
- Bacterial Outer Membrane Proteins [D12.776.543.100]
- Adhesins, Bacterial [D12.776.543.100.050]
- Adhesins, Escherichia coli [D12.776.543.100.050.040]
- Biological Factors [D23]
- Antigens [D23.050]
- Antigens, Bacterial [D23.050.161]
- Adhesins, Bacterial [D23.050.161.050]
- Adhesins, Escherichia coli [D23.050.161.050.040]
Below are MeSH descriptors whose meaning is more specific than "Adhesins, Escherichia coli".
This graph shows the total number of publications written about "Adhesins, Escherichia coli" by people in Harvard Catalyst Profiles by year, and whether "Adhesins, Escherichia coli" was a major or minor topic of these publication.
To see the data from this visualization as text, click here.
|Year||Major Topic||Minor Topic||Total|
Below are the most recent publications written about "Adhesins, Escherichia coli" by people in Profiles.
Conformational switch of the bacterial adhesin FimH in the absence of the regulatory domain: Engineering a minimalistic allosteric system. J Biol Chem. 2018 02 02; 293(5):1835-1849.
Target-directed Dynamic Combinatorial Chemistry: A Study on Potentials and Pitfalls as Exemplified on a Bacterial Target. Chemistry. 2017 Aug 25; 23(48):11570-11577.
Selective depletion of uropathogenic E. coli from the gut by a FimH antagonist. Nature. 2017 06 22; 546(7659):528-532.
Synthesis and Preliminary Studies of a Novel Negative Allosteric Modulator, 7-((2,5-Dioxopyrrolidin-1-yl)methyl)-4-(2-fluoro-4-[11C]methoxyphenyl) quinoline-2-carboxamide, for Imaging of Metabotropic Glutamate Receptor 2. ACS Chem Neurosci. 2017 09 20; 8(9):1937-1948.
Cytotoxic Necrotizing Factor-1 (CNF1) does not promote E. coli infection in a murine model of ascending pyelonephritis. BMC Microbiol. 2017 05 25; 17(1):127.
Urinary Tract Infection: Which Conformation of the Bacterial Lectin FimH Is Therapeutically Relevant? J Med Chem. 2017 07 13; 60(13):5646-5662.
The Conformational Variability of FimH: Which Conformation Represents the Therapeutic Target? Chembiochem. 2016 06 02; 17(11):1012-20.
Catch-bond mechanism of the bacterial adhesin FimH. Nat Commun. 2016 Mar 07; 7:10738.
FimH antagonists: bioisosteres to improve the in vitro and in vivo PK/PD profile. J Med Chem. 2015 Mar 12; 58(5):2221-39.
Positively selected FimH residues enhance virulence during urinary tract infection by altering FimH conformation. Proc Natl Acad Sci U S A. 2013 Sep 24; 110(39):15530-7.