Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane.
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MicroRNA-200 family members differentially regulate morphological plasticity and mode of melanoma cell invasionMechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segmentEpstein-Barr virus-induced genes: first lymphocyte-specific G protein-coupled peptide receptorsIntracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasisThe myristoylation of TRIF-related adaptor molecule is essential for Toll-like receptor 4 signal transductionAmino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipidsOscillations in the lateral pressure of lipid monolayers induced by nonlinear chemical dynamics of the second messengers MARCKS and protein kinase CDifferential membrane binding of the human immunodeficiency virus type 1 matrix proteinApical accumulation of MARCKS in neural plate cells during neurulation in the chick embryoPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)A novel effect of MARCKS phosphorylation by activated PKC: the dephosphorylation of its serine 25 in chick neuroblasts.Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24)Identification and characterization of cathepsin B as the cellular MARCKS cleaving enzymePhosphorylation-dependent human immunodeficiency virus type 1 infection and nuclear targeting of viral DNAPhosphorylation of Vif and its role in HIV-1 replicationMyristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich protein kinase C substrate protein in intact cellsThe myristoylated alanine-rich C-kinase substrate (MARCKS) is sequentially phosphorylated by conventional, novel and atypical isotypes of protein kinase CMyelin-mediated inhibition of oligodendrocyte precursor differentiation can be overcome by pharmacological modulation of Fyn-RhoA and protein kinase C signallingA novel N-terminal domain directs membrane localization of mouse testis-specific calpastatinTrif-related adapter molecule is phosphorylated by PKC{epsilon} during Toll-like receptor 4 signalingMyristoylated, alanine-rich C-kinase substrate phosphorylation regulates growth cone adhesion and pathfindingDynamic adhesions and MARCKS in melanoma cellsMicrofilament reorganization during apoptosis: the role of Gas2, a possible substrate for ICE-like proteasesBiphasic modulation of protein kinase C and enhanced cell toxicity by amyloid beta peptide and anoxia in neuronal cultures.Membrane binding of the neuronal calcium sensor recoverin - modulatory role of the charged carboxy-terminus.Amphitropic proteins: regulation by reversible membrane interactions (review).PhosphoMARCKS drives motility of mouse melanoma cells.Myristoylation: An Important Protein Modification in the Immune ResponseFlagellar protein localization mediated by a calcium-myristoyl/palmitoyl switch mechanism.Myristoylated Alanine Rich C Kinase Substrate (MARCKS) is essential to β2-integrin dependent responses of equine neutrophils.Phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) protein is associated with bovine luteal oxytocin exocytosis.Two N-myristoyltransferase isozymes play unique roles in protein myristoylation, proliferation, and apoptosis.Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin.Myristoylated alanine rich C kinase substrate (MARCKS) heterozygous mutant mice exhibit deficits in hippocampal mossy fiber-CA3 long-term potentiation.Zonula occludens toxin modulates tight junctions through protein kinase C-dependent actin reorganization, in vitroThe phosphoinositide 3-kinase α selective inhibitor BYL719 enhances the effect of the protein kinase C inhibitor AEB071 in GNAQ/GNA11-mutant uveal melanoma cells.Modulation of intestinal permeability: a novel and innovative approach for the oral delivery of drugs, macromolecules and antigens.1,25-Dihydroxyvitamin D3 and 12-O-tetradecanoyl phorbol 13-acetate cause differential activation of Ca(2+)-dependent and Ca(2+)-independent isoforms of protein kinase C in rat colonocytes.Protein kinase C isoforms as specific targets for modulation of vascular smooth muscle function in hypertension.Cross-talk unfolded: MARCKS proteins.
P2860
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P2860
Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh-hant
name
Regulation by phosphorylation ...... rate with the plasma membrane.
@en
Regulation by phosphorylation ...... rate with the plasma membrane.
@nl
type
label
Regulation by phosphorylation ...... rate with the plasma membrane.
@en
Regulation by phosphorylation ...... rate with the plasma membrane.
@nl
prefLabel
Regulation by phosphorylation ...... rate with the plasma membrane.
@en
Regulation by phosphorylation ...... rate with the plasma membrane.
@nl
P2093
P356
P1433
P1476
Regulation by phosphorylation ...... rate with the plasma membrane.
@en
P2093
P2888
P304
P356
10.1038/351320A0
P407
P577
1991-05-01T00:00:00Z
P6179
1028226670