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The Marcks brothers: A family of protein kinase C substrates

Data up to Jan 2025

Published1992
Citations474
References19

Total Citations Per Year

Abstract

References (19)

MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium–calmodulin

1992 • 728 citations

Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane

1991 • 372 citations

Protein kinase C-stimulated phosphorylation in vitro of a Mr 80,000 protein phosphorylated in response to phorbol esters and growth factors in intact fibroblasts. Distinction from protein kinase C and prominence in brain.

1986 • 277 citations

Transmembrane molecular assemblies in cell-extracellular matrix interactions

1991 • 244 citations

Phosphorylation-regulated calmodulin binding to a prominent cellular substrate for protein kinase C

1989 • 241 citations

Rous sarcoma virus-transformed fibroblasts and cells of monocytic origin display a peculiar dot-like organization of cytoskeletal proteins involved in microfilament-membrane interactions*1

1987 • 216 citations

Stimulus-dependent myristoylation of a major substrate for protein kinase C

1988 • 216 citations

Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia.

1990 • 195 citations

Primary structure and domain organization of human alpha and beta adducin.

1991 • 145 citations

MacMARCKS, a novel member of the MARCKS family of protein kinase C substrates

1992 • 120 citations

Down-regulation of protein kinase C and of an endogenous 80-kDa substrate in transformed fibroblasts.

1987 • 119 citations

Myristoylated and Nonmyristoylated Forms of a Protein Are Phosphorylated by Protein Kinase C

1989 • 89 citations

The human myristoylated alanine-rich C kinase substrate (MARCKS) gene (MACS). Analysis of its gene product, promoter, and chromosomal localization

1991 • 85 citations

Molecular cloning and characterization of the acidic 80-kDa protein kinase C substrate from rat brain. Identification as a glycoprotein.

1991 • 78 citations

Characteristics of the F52 protein, a MARCKS homologue.

1992 • 72 citations

Gap-43 — What does it do in the growth cone?

1989 • 64 citations

A mouse brain cDNA encodes a novel protein with the protein kinase C phosphorylation site domain common to MARCKS

1991 • 49 citations

The expression of 80K/MARCKS, a major substrate of protein kinase C (PKC), is down-regulated through both PKC-dependent and -independent pathways. Effects of bombesin, platelet-derived growth factor, and cAMP.

1992 • 47 citations

A Protein Modulator Stimulates C Kinase‐Dependent Phosphorylation of a 90K Substrate in Synaptic Membranes

1986 • 40 citations

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