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Calelectrins are a ubiquitous family of Ca2+-binding proteins purified by Ca2+-dependent hydrophobic affinity chromatography by a mechanism distinct from that of calmodulin

Data up to Jan 2025

Published1984
Citations27
References13

Total Citations Per Year

Abstract

References (13)

A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding

1976 • 225,752 citations

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1976 • 200,127 citations

Ca2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatography

1982 • 877 citations

Calcium-induced exposure of a hydrophobic surface on calmodulin

1980 • 520 citations

Conformational transition accompanying the binding of calcium(2+) ion to the protein activator of 3',5'-cyclic adenosine monophosphate phosphodiesterase

1977 • 472 citations

Calcium-dependent protein binding to phenothiazine columns.

1982 • 159 citations

Calcium binding domains of calmodulin. Sequence of fill as determined with terbium luminescence.

1982 • 113 citations

Metal‐Binding Properties of Calmodulin

1982 • 94 citations

Isolation from Cholinergic Synapses of a Protein That Binds to Membranes in a Calcium‐Dependent Manner

1982 • 93 citations

Calelectrin self-aggregates and promotes membrane aggregation in the presence of calcium.

1982 • 79 citations

Calelectrin, a Calcium‐Dependent Membrane‐Binding Protein Associated with Secretory Granules in Torpedo Cholinergic Electromotor Nerve Endings and Rat Adrenal Medulla

1983 • 40 citations

Calcium binding proteins and cellular regulation

1982 • 36 citations

Calelectrin in human blood cells.

1983 • 21 citations

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Calelectrins are a ubiquitous family of Ca2+-binding proteins purified by Ca2+-dependent… (1984) – Biochemical and Biophysical Research Communications | Metascience Observatory Explorer