Comparable 30-kDa apamin binding polypeptides may fulfill equivalent roles within putative subtypes of small conductance Ca(2+)-activated K+ channels.-Reference-Cited by-同舟云学术

Comparable 30-kDa apamin binding polypeptides may fulfill equivalent roles within putative subtypes of small conductance Ca(2+)-activated K+ channels.

Published:1994-07 Issue:27 Volume:269 Page:18053-18061
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Wadsworth J.D.,Doorty K.B.,Strong P.N.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference36 articles.

1. Polypeptide constitution of receptors for apamin, a neurotoxin which blocks a class of Ca2+ -activated K+ channels

2. Leiurotoxin I (scyllatoxin), a peptide ligand for Ca2(+)-activated K+ channels. Chemical synthesis, radiolabeling, and receptor characterization.

3. Scyllatoxin, a blocker of calcium-activated potassium channels: structure-function relationships and brain localization of the binding sites

4. Potassium Channel Modulators;Brewster,1992

5. Effects of quinine and apamin on the calcium-dependent potassium permeability of mammalian hepatocytes and red cells.

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