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Malignant-hyperthermia susceptibility is associated with a mutation of the alpha 1-subunit of the human dihydropyridine-sensitive L-type voltage-dependent calcium-channel receptor in skeletal muscleMutually exclusive exon splicing of the cardiac calcium channel alpha 1 subunit gene generates developmentally regulated isoforms in the rat heart.The beta 1a subunit is essential for the assembly of dihydropyridine-receptor arrays in skeletal muscle.Mutations in the alpha1 subunit of an L-type voltage-activated Ca2+ channel cause myotonia in Caenorhabditis elegansMolecular diversity of Ca2+ channel alpha 1 subunits from the marine ray Discopyge ommataDeduced amino acid sequence of a putative sodium channel from the scyphozoan jellyfish Cyanea capillata.Molecular mechanism of use-dependent calcium channel block by phenylalkylamines: role of inactivation.Predominance of the alpha1D subunit in L-type voltage-gated Ca2+ channels of hair cells in the chicken's cochlea.In vivo labeling of L-type Ca2+ channels by fluorescent dihydropyridines: evidence for a functional, extracellular heparin-binding site.Characterization of the two size forms of the alpha 1 subunit of skeletal muscle L-type calcium channels.Structural requirements of the dihydropyridine receptor alpha1S II-III loop for skeletal-type excitation-contraction coupling.Nine L-type amino acid residues confer full 1,4-dihydropyridine sensitivity to the neuronal calcium channel alpha1A subunit. Role of L-type Met1188.Calcium channels: the beta-subunit increases the affinity of dihydropyridine and Ca2+ binding sites of the alpha 1-subunit.Calcium channel block by (-)devapamil is affected by the sequence environment and composition of the phenylalkylamine receptor site.Endogenous calcium channels in human embryonic kidney (HEK293) cells.Molecular cloning and functional expression of a skeletal muscle dihydropyridine receptor from Rana catesbeiana.Insect calcium channels. Molecular cloning of an alpha 1-subunit from housefly (Musca domestica) muscle.Functional expression and characterization of skeletal muscle dihydropyridine receptors in Xenopus oocytes.Two amino acid residues in the IIIS5 segment of L-type calcium channels differentially contribute to 1,4-dihydropyridine sensitivity.Transfer of high sensitivity for benzothiazepines from L-type to class A (BI) calcium channels.Transfer of L-type calcium channel IVS6 segment increases phenylalkylamine sensitivity of alpha1A.Amino acids in segment IVS6 and beta-subunit interaction support distinct conformational changes during Ca(v)2.1 inactivation.Native-type DHP-sensitive calcium channel currents are produced by cloned rat aortic smooth muscle and cardiac alpha 1 subunits expressed in Xenopus laevis oocytes and are regulated by alpha 2- and beta-subunits.
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on February 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Calcium channels from Cyprinus carpio skeletal muscle.
@en
Calcium channels from Cyprinus carpio skeletal muscle.
@nl
type
label
Calcium channels from Cyprinus carpio skeletal muscle.
@en
Calcium channels from Cyprinus carpio skeletal muscle.
@nl
prefLabel
Calcium channels from Cyprinus carpio skeletal muscle.
@en
Calcium channels from Cyprinus carpio skeletal muscle.
@nl
P2093
P2860
P356
P1476
Calcium channels from Cyprinus carpio skeletal muscle
@en
P2093
A Schwartz
F Scheffauer
K Friedrich
R Staudinger
P2860
P304
P356
10.1073/PNAS.88.3.727
P407
P577
1991-02-01T00:00:00Z