Dissociation of phosphorylation and translocation of a myristoylated protein kinase C substrate (MARCKS protein) in C6 glioma and N1E-115 neuroblastoma cells.
about
Identification and characterization of cathepsin B as the cellular MARCKS cleaving enzymeThe MARCKS family of phospholipid binding proteins: regulation of phospholipase D and other cellular componentsMyristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich protein kinase C substrate protein in intact cellsMyelin-mediated inhibition of oligodendrocyte precursor differentiation can be overcome by pharmacological modulation of Fyn-RhoA and protein kinase C signallingRegulation of PI3K by PKC and MARCKS: Single-Molecule Analysis of a Reconstituted Signaling PathwayRegulation of mucin secretion and inflammation in asthma: a role for MARCKS protein?Overexpression of the myristoylated alanine-rich C-kinase substrate inhibits cell adhesion to extracellular matrix components.Calbindin expression in renal tubular epithelial cells. Altered sodium phosphate co-transport in association with cytoskeletal rearrangement.Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions.Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes.Ca2+ x calmodulin prevents myristoylated alanine-rich kinase C substrate protein phosphorylation by protein kinase Cs in C6 rat glioma cells.Overexpression of myristoylated alanine-rich C-kinase substrate enhances activation of phospholipase D by protein kinase C in SK-N-MC human neuroblastoma cells.Chromaffin cell F-actin disassembly and potentiation of catecholamine release in response to protein kinase C activation by phorbol esters is mediated through myristoylated alanine-rich C kinase substrate phosphorylation.Phosphorylation of myristoylated alanine-rich C kinase substrate is involved in the cAMP-dependent amylase release in parotid acinar cells.Myristoylated alanine-rich C kinase substrate (MARCKS): a multirole signaling protein in cancers.Protein kinase C prevents oligodendrocyte differentiation: modulation of actin cytoskeleton and cognate polarized membrane traffic.
P2860
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P2860
Dissociation of phosphorylation and translocation of a myristoylated protein kinase C substrate (MARCKS protein) in C6 glioma and N1E-115 neuroblastoma cells.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Dissociation of phosphorylatio ...... d N1E-115 neuroblastoma cells.
@en
Dissociation of phosphorylatio ...... ted protein kinase C substrate
@nl
type
label
Dissociation of phosphorylatio ...... d N1E-115 neuroblastoma cells.
@en
Dissociation of phosphorylatio ...... ted protein kinase C substrate
@nl
prefLabel
Dissociation of phosphorylatio ...... d N1E-115 neuroblastoma cells.
@en
Dissociation of phosphorylatio ...... ted protein kinase C substrate
@nl
P2093
P2860
P1476
Dissociation of phosphorylatio ...... d N1E-115 neuroblastoma cells.
@en
P2093
P2860
P304
P356
10.1111/J.1471-4159.1993.TB03303.X
P407
P577
1993-04-01T00:00:00Z