The MARCKS brothers: a family of protein kinase C substrates.
about
Identification of an actin binding region and a protein kinase C phosphorylation site on human fascinA novel lipid-anchored A-kinase Anchoring Protein facilitates cAMP-responsive membrane eventsElectrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesiclesKinome analysis of host response to mycobacterial infection: a novel technique in proteomicsAn early stage of Mason-Pfizer monkey virus budding is regulated by the hydrophobicity of the Gag matrix domain coreEpstein-Barr virus infection induces expression in B lymphocytes of a novel gene encoding an evolutionarily conserved 55-kilodalton actin-bundling proteinAdducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neuronsApical accumulation of MARCKS in neural plate cells during neurulation in the chick embryoImpact of Leishmania metalloprotease GP63 on macrophage signalingMARCKS-like protein is an initiating molecule in axolotl appendage regeneration.A novel effect of MARCKS phosphorylation by activated PKC: the dephosphorylation of its serine 25 in chick neuroblasts.The NMDA Receptor NR1 C1 Region Bound to Calmodulin: Structural Insights into Functional Differences between Homologous DomainsMyristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayersRegulation of the AKAP79-protein kinase C interaction by Ca2+/CalmodulinIdentification and characterization of cathepsin B as the cellular MARCKS cleaving enzymeThe MARCKS family of phospholipid binding proteins: regulation of phospholipase D and other cellular componentsc-Jun N-terminal kinase phosphorylation of MARCKSL1 determines actin stability and migration in neurons and in cancer cellsPRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich protein kinase C substrate protein in intact cellsAdducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and CThe myristoylated alanine-rich C-kinase substrate (MARCKS) is sequentially phosphorylated by conventional, novel and atypical isotypes of protein kinase CPICK1, an anchoring protein that specifically targets protein kinase Calpha to mitochondria selectively upon serum stimulation in NIH 3T3 cellsEffect of phorbol ester and platelet-derived growth factor on protein kinase C in rat hepatic stellate cellsHypertension-associated point mutations in the adducin alpha and beta subunits affect actin cytoskeleton and ion transportDynamic adhesions and MARCKS in melanoma cellsMARCKS-like protein, a membrane protein identified for its expression in developing neural retina, plays a role in regulating retinal cell proliferationFunctional Diversification of the Four MARCKS Family Members in Zebrafish Neural DevelopmentElectrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins.A novel adapter protein employs a phosphotyrosine binding domain and exceptionally basic N-terminal domains to capture and localize an atypical protein kinase C: characterization of Caenorhabditis elegans C kinase adapter 1, a protein that avidly biSignal processing in migrating T24 human bladder carcinoma cells: role of the autocrine interleukin-8 loop.Structural properties and mechanisms that govern association of C kinase adapter 1 with protein kinase C3 and the cell periphery.Calmodulin levels are dynamically regulated in living vascular smooth muscle cells.Synthesis and dephosphorylation of MARCKS in the late stages of megakaryocyte maturation drive proplatelet formation.Inhibition of myristoylated alanine-rich C kinase substrate (MARCKS) protein inhibits ozone-induced airway neutrophilia and inflammation.Activation of the Epstein-Barr virus transcription factor BZLF1 by 12-O-tetradecanoylphorbol-13-acetate-induced phosphorylation.Signalling pathways in the brain: cellular transduction of mood stabilisation in the treatment of manic-depressive illness.Pyk2 activation triggers epidermal growth factor receptor signaling and cell motility after wounding sheets of epithelial cells.Peptides derived from MARCKS block coagulation complex assembly on phosphatidylserine.Genetic mechanisms underlying the regulation of urinary sodium excretion and arterial blood pressure: the role of adducin.A relationship between protein kinase C phosphorylation and calmodulin binding to the metabotropic glutamate receptor subtype 7.
P2860
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P2860
The MARCKS brothers: a family of protein kinase C substrates.
description
1992 nî lūn-bûn
@nan
1992 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
The MARCKS brothers: a family of protein kinase C substrates.
@ast
The MARCKS brothers: a family of protein kinase C substrates.
@en
type
label
The MARCKS brothers: a family of protein kinase C substrates.
@ast
The MARCKS brothers: a family of protein kinase C substrates.
@en
prefLabel
The MARCKS brothers: a family of protein kinase C substrates.
@ast
The MARCKS brothers: a family of protein kinase C substrates.
@en
P1433
P1476
The MARCKS brothers: a family of protein kinase C substrates.
@en
P2093
P304
P356
10.1016/0092-8674(92)90546-O
P407
P577
1992-11-01T00:00:00Z