Myristoylated alanine-rich C kinase substrate (MARCKS) is involved in myoblast fusion through its regulation by protein kinase Calpha and calpain proteolytic cleavage.
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Functional analysis of novel phosphorylation sites of CREB-binding protein using mass spectrometry and mammalian two-hybrid assaysMARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactionsC6ORF32 is upregulated during muscle cell differentiation and induces the formation of cellular filopodiaLongSAGE analysis of skeletal muscle at three prenatal stages in Tongcheng and Landrace pigsFibroblast Migration Is Regulated by Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Protein.Calpain-10 Activity Underlies Angiotensin II-Induced Aldosterone Production in an Adrenal Glomerulosa Cell ModelLipocalin-type prostaglandin D2 synthase protein regulates glial cell migration and morphology through myristoylated alanine-rich C-kinase substrate: prostaglandin D2-independent effectsIn Vitro Neutrophil Migration Requires Protein Kinase C-Delta (δ-PKC)-Mediated Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Phosphorylation.MARCKS silencing differentially affects human vascular smooth muscle and endothelial cell phenotypes to inhibit neointimal hyperplasia in saphenous vein.Targeting calpain in synaptic plasticity.ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins.MARCKS is involved in methylmercury-induced decrease in cell viability and nitric oxide production in EA.hy926 cellsELF-MF transiently increases skeletal myoblast migration: possible role of calpain system.Calpain and MARCKS protein regulation of airway mucin secretionTranscriptional profile of GTP-mediated differentiation of C2C12 skeletal muscle cells.MARCKS dephosphorylation is involved in bradykinin-induced neurite outgrowth in neuroblastoma SH-SY5Y cells.The MARCKS protein amount is differently regulated by calpain during toxic effects of methylmercury between SH-SY5Y and EA.hy926 cells.Cleavage of the myristoylated alanine-rich C kinase substrate (MARCKS) by cysteine cathepsins in cells and tissues of stefin B-deficient mice.N-terminal cleavage fragment of focal adhesion kinase is required to activate the survival signalling pathway in cultured myoblasts under oxidative stress.
P2860
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P2860
Myristoylated alanine-rich C kinase substrate (MARCKS) is involved in myoblast fusion through its regulation by protein kinase Calpha and calpain proteolytic cleavage.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Myristoylated alanine-rich C k ...... calpain proteolytic cleavage.
@en
type
label
Myristoylated alanine-rich C k ...... calpain proteolytic cleavage.
@en
prefLabel
Myristoylated alanine-rich C k ...... calpain proteolytic cleavage.
@en
P2093
P2860
P356
P1433
P1476
Myristoylated alanine-rich C k ...... calpain proteolytic cleavage.
@en
P2093
Karine Vuillier-Devillers
Patrick Cottin
Sandrine Dulong
Sebastien Goudenege
Stéphane Manenti
Sylvie Poussard
P2860
P304
P356
10.1042/BJ20040347
P407
P577
2004-09-01T00:00:00Z