Back to search

Structural characterization of the 1,4-dihydropyridine receptor of the voltage-dependent Ca2+ channel from rabbit skeletal muscle. Evidence for two distinct high molecular weight subunits.

Data up to Jan 2025

Published1987
Citations231
References17

Total Citations Per Year

Abstract

References (17)

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1970 • 253,849 citations

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.

1979 • 54,907 citations

A dot-immunobinding assay for monoclonal and other antibodies

1982 • 2,219 citations

Improved technique utilizing nonfat dry milk for analysis of proteins and nucleic acids transferred to nitrocellulose

1984 • 1,697 citations

Calcium channel modulation by neurotransmitters, enzymes and drugs

1983 • 1,267 citations

Calcium Channels in Excitable Cell Membranes

1983 • 725 citations

Purification of the calcium antagonist receptor of the voltage-sensitive calcium channel from skeletal muscle transverse tubules

1984 • 469 citations

Purified dihydropyridine-binding site from skeletal muscle t-tubules is a functional calcium channel

1986 • 405 citations

[3H]nitrendipine receptors in skeletal muscle.

1983 • 381 citations

[42] Assay for calcium channels

1985 • 191 citations

Further characterization of light and heavy sarcoplasmic reticulum vesicles. Identification of the ‘sarcoplasmic reticulum feet’ associated with heavy sarcoplasmic reticulum vesicles

1980 • 187 citations

1,4‐Dihydropyridine Ca2+ channel antagonists and activators: A comparison of binding characteristics with pharmacology

1984 • 182 citations

Monoclonal Antibodies

1981 • 181 citations

Isolation of transverse tubules by fractionation of triad junctions of skeletal muscle.

1977 • 163 citations

The 1,4-dihydropyridine receptor associated with the skeletal muscle voltage-dependent Ca2+ channel. Purification and subunit composition.

1985 • 163 citations

Purification of morphologically intact triad structures from skeletal muscle.

1983 • 109 citations

Immunochemical analysis of subunit structures of 1,4-dihydropyridine receptors associated with voltage-dependent calcium channels in skeletal, cardiac, and smooth muscles

1986 • 96 citations

Cited By (0)

Loading...
Structural characterization of the 1,4-dihydropyridine receptor of the voltage-dependent… (1987) – Journal of Biological Chemistry | Metascience Observatory Explorer