Virulence Factors, Bordetella
"Virulence Factors, Bordetella" 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.
A set of BACTERIAL ADHESINS and TOXINS, BIOLOGICAL produced by BORDETELLA organisms that determine the pathogenesis of BORDETELLA INFECTIONS, such as WHOOPING COUGH. They include filamentous hemagglutinin; FIMBRIAE PROTEINS; pertactin; PERTUSSIS TOXIN; ADENYLATE CYCLASE TOXIN; dermonecrotic toxin; tracheal cytotoxin; Bordetella LIPOPOLYSACCHARIDES; and tracheal colonization factor.
Virulence Factors, Bordetella
- Virulence Factors, Bordetella
- Factors, Bordetella Virulence
- Bordetella Virulence Determinant
- Determinant, Bordetella Virulence
- Virulence Determinant, Bordetella
- Bordetella Virulence Factors
- Lymphocytosis-Promoting Factor-Hemagglutinin
- Factor-Hemagglutinin, Lymphocytosis-Promoting
- Lymphocytosis Promoting Factor Hemagglutinin
- LFP Hemagglutinin
- LP HA
- Leukocytosis-Promoting Factor Hemagglutinin
- Factor Hemagglutinin, Leukocytosis-Promoting
- Hemagglutinin, Leukocytosis-Promoting Factor
- Leukocytosis Promoting Factor Hemagglutinin
Below are MeSH descriptors whose meaning is more general than "Virulence Factors, Bordetella".
Below are MeSH descriptors whose meaning is more specific than "Virulence Factors, Bordetella".
This graph shows the total number of publications written about "Virulence Factors, Bordetella" by people in Harvard Catalyst Profiles by year, and whether "Virulence Factors, Bordetella" 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 "Virulence Factors, Bordetella" by people in Profiles.
Increasing FIM2/3 antigen-content improves efficacy of Bordetella pertussis vaccines in mice in vivo without altering vaccine-induced human reactogenicity biomarkers in vitro. Vaccine. 2019 01 03; 37(1):80-89.
Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water. Science. 2017 10 13; 358(6360):238-241.
ATP-independent control of autotransporter virulence protein transport via the folding properties of the secreted protein. Chem Biol. 2012 Feb 24; 19(2):287-96.
Structure-based prediction reveals capping motifs that inhibit ß-helix aggregation. Proc Natl Acad Sci U S A. 2011 Jul 05; 108(27):11099-104.
Slow formation of aggregation-resistant beta-sheet folding intermediates. Proteins. 2010 Mar; 78(4):812-24.
Vectorial transport and folding of an autotransporter virulence protein during outer membrane secretion. Mol Microbiol. 2009 Mar; 71(5):1323-32.
PGRP-LC and PGRP-LE have essential yet distinct functions in the drosophila immune response to monomeric DAP-type peptidoglycan. Nat Immunol. 2006 Jul; 7(7):715-23.
Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. Proc Natl Acad Sci U S A. 2006 Mar 28; 103(13):4918-23.
The C-type lectin fold as an evolutionary solution for massive sequence variation. Nat Struct Mol Biol. 2005 Oct; 12(10):886-92.
Cutting edge: Th2 cell trafficking into the allergic lung is dependent on chemoattractant receptor signaling. J Immunol. 2002 Jul 15; 169(2):651-5.