"Hemolysin Proteins" 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.
Proteins from BACTERIA and FUNGI that are soluble enough to be secreted to target ERYTHROCYTES and insert into the membrane to form beta-barrel pores. Biosynthesis may be regulated by HEMOLYSIN FACTORS.
Below are MeSH descriptors whose meaning is more general than "Hemolysin Proteins".
Below are MeSH descriptors whose meaning is more specific than "Hemolysin Proteins".
This graph shows the total number of publications written about "Hemolysin Proteins" by people in this website by year, and whether "Hemolysin Proteins" was a major or minor topic of these publications.
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|Year||Major Topic||Minor Topic||Total|
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Below are the most recent publications written about "Hemolysin Proteins" by people in Profiles.
A listeriolysin O subunit vaccine is protective against Listeria monocytogenes. Vaccine. 2020 08 10; 38(36):5803-5813.
An Intermolecular p-Stacking Interaction Drives Conformational Changes Necessary to ß-Barrel Formation in a Pore-Forming Toxin. mBio. 2019 07 02; 10(4).
The Structural Basis for a Transition State That Regulates Pore Formation in a Bacterial Toxin. mBio. 2019 04 23; 10(2).
The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support ß-Barrel Pore Insertion. J Biol Chem. 2015 Jul 17; 290(29):17733-17744.
Perfringolysin O: The Underrated Clostridium perfringens Toxin? Toxins (Basel). 2015 May 14; 7(5):1702-21.
Conformational changes during pore formation by the perforin-related protein pleurotolysin. PLoS Biol. 2015 Feb; 13(2):e1002049.
Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration. J Mol Biol. 2014 Feb 20; 426(4):785-92.
Disulfide-bond scanning reveals assembly state and ß-strand tilt angle of the PFO ß-barrel. Nat Chem Biol. 2013 Jun; 9(6):383-9.
The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assembly. PLoS Pathog. 2012; 8(7):e1002787.
The pore-forming toxin listeriolysin O mediates a novel entry pathway of L. monocytogenes into human hepatocytes. PLoS Pathog. 2011 Nov; 7(11):e1002356.