"Charybdotoxin" 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 37-amino acid residue peptide isolated from the scorpion Leiurus quinquestriatus hebraeus. It is a neurotoxin that inhibits calcium activated potassium channels.
| Descriptor ID |
D018999
|
| MeSH Number(s) |
D12.644.115 D20.888.065.830.150 D23.946.833.065.830.150
|
| Concept/Terms |
Charybdotoxin- Charybdotoxin
- CTX Toxin
- Toxin, CTX
- Quinquestriatus Toxin
- Toxin, Quinquestriatus
- ChTX
|
Below are MeSH descriptors whose meaning is more general than "Charybdotoxin".
Below are MeSH descriptors whose meaning is more specific than "Charybdotoxin".
This graph shows the total number of publications written about "Charybdotoxin" by people in this website by year, and whether "Charybdotoxin" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1995 | 0 | 1 | 1 |
| 2003 | 0 | 1 | 1 |
| 2008 | 1 | 0 | 1 |
| 2013 | 1 | 0 | 1 |
| 2014 | 0 | 1 | 1 |
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Below are the most recent publications written about "Charybdotoxin" by people in Profiles.
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Vel?zquez-Marrero C, Seale GE, Treistman SN, Martin GE. Large conductance voltage- and Ca2+-gated potassium (BK) channel ?4 subunit influences sensitivity and tolerance to alcohol by altering its response to kinases. J Biol Chem. 2014 Oct 17; 289(42):29261-72.
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Hua Z, Kobertz WR. Chemical derivatization and purification of peptide-toxins for probing ion channel complexes. Methods Mol Biol. 2013; 995:19-30.
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Morin TJ, Kobertz WR. Counting membrane-embedded KCNE beta-subunits in functioning K+ channel complexes. Proc Natl Acad Sci U S A. 2008 Feb 05; 105(5):1478-82.
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Feinberg-Zadek PL, Treistman SN. Beta-subunits are important modulators of the acute response to alcohol in human BK channels. Alcohol Clin Exp Res. 2007 May; 31(5):737-44.
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Kim LA, Furst J, Butler MH, Xu S, Grigorieff N, Goldstein SA. Ito channels are octomeric complexes with four subunits of each Kv4.2 and K+ channel-interacting protein 2. J Biol Chem. 2004 Feb 13; 279(7):5549-54.
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Brugnara C, Armsby CC, De Franceschi L, Crest M, Euclaire MF, Alper SL. Ca(2+)-activated K+ channels of human and rabbit erythrocytes display distinctive patterns of inhibition by venom peptide toxins. J Membr Biol. 1995 Sep; 147(1):71-82.