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Three-dimensional structure of different functional forms of the Vibrio cholerae hemolysin oligomer: a cryo-electron microscopic study
scientific journal article
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scholarly article
1 reference
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PubMed
PubMed ID
19854900
retrieved
24 January 2017
title
Three-dimensional structure of different functional forms of the Vibrio cholerae hemolysin oligomer: a cryo-electron microscopic study
(English)
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PubMed
PubMed ID
19854900
retrieved
24 January 2017
main subject
Vibrio cholerae
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author name string
Somnath Dutta
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
19854900
retrieved
24 January 2017
Budhaditya Mazumdar
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
19854900
retrieved
24 January 2017
Kalyan K. Banerjee
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
19854900
retrieved
24 January 2017
Amar N. Ghosh
series ordinal
4
1 reference
stated in
PubMed
PubMed ID
19854900
retrieved
24 January 2017
language of work or name
English
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publication date
1 January 2010
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stated in
PubMed
PubMed ID
19854900
retrieved
24 January 2017
published in
Journal of Bacteriology
1 reference
stated in
PubMed
PubMed ID
19854900
retrieved
24 January 2017
volume
192
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stated in
PubMed
PubMed ID
19854900
retrieved
24 January 2017
issue
1
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stated in
PubMed
PubMed ID
19854900
retrieved
24 January 2017
page(s)
169–178
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stated in
PubMed
PubMed ID
19854900
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24 January 2017
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Vibrio cholerae cytolysin is composed of an alpha-hemolysin-like core
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Three-dimensional reconstruction of metal replicas of the Helicobacter pylori vacuolating cytotoxin
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In vitro proteolytic processing and activation of the recombinant precursor of El Tor cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases.
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Two-step processing for activation of the cytolysin/hemolysin of Vibrio cholerae O1 biotype El Tor: nucleotide sequence of the structural gene (hlyA) and characterization of the processed products.
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Characterization of Vibrio cholerae El Tor cytolysin as an oligomerizing pore-forming toxin
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Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore
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Interaction of the Vibrio cholerae cytolysin (VCC) with cholesterol, some cholesterol esters, and cholesterol derivatives: a TEM study
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Vibrio cholerae hemolysin. Implication of amphiphilicity and lipid-induced conformational change for its pore-forming activity
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Vibrio cholerae cytolysin: assembly and membrane insertion of the oligomeric pore are tightly linked and are not detectably restricted by membrane fluidity.
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Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane.
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27 November 2018
Cholera
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stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2798276
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27 November 2018
A 11.5 A single particle reconstruction of GroEL using EMAN
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/19854900
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Carbohydrate-mediated regulation of interaction of Vibrio cholerae hemolysin with erythrocyte and phospholipid vesicle
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/19854900
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Two forms of Vibrio cholerae O1 El Tor hemolysin derived from identical precursor protein
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/19854900
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/JB.00930-09
1 reference
stated in
PubMed
PubMed ID
19854900
retrieved
24 January 2017
PMCID
2798276
0 references
PubMed ID
19854900
1 reference
stated in
PubMed
PubMed ID
19854900
retrieved
24 January 2017
ResearchGate publication ID
38034346
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