Characteristics of the F52 protein, a MARCKS homologue.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference28 articles.
1. Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain
2. Phosphorylation-regulated calmodulin binding to a prominent cellular substrate for protein kinase C
3. Phosphorylation-dependent binding of a synthetic MARCKS peptide to calmodulin.
4. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium–calmodulin
5. The human myristoylated alanine-rich C kinase substrate (MARCKS) gene (MACS). Analysis of its gene product, promoter, and chromosomal localization
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1. Multisolitons-like patterns in a one-dimensional MARCKS protein cyclic model;Journal of Theoretical Biology;2024-02
2. Pattern formation in a one-dimensional MARCKS protein cyclic model with spatially inhomogeneous diffusion coefficients;The European Physical Journal Plus;2023-11-06
3. Myristoylated alanine-rich C kinase substrate-like protein-1 regulates epithelial sodium channel activity in renal distal convoluted tubule cells;American Journal of Physiology-Cell Physiology;2020-09-01
4. MARCKS-related protein regulates cytoskeletal organization at cell-cell and cell-substrate contacts in epithelial cells;Journal of Cell Science;2017-01-01
5. The prognostic value of MARCKS-like 1 in lymph node-negative breast cancer;Breast Cancer Research and Treatment;2012-07-08
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