The MARCKS family of cellular protein kinase C substrates
about
A 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 coreThe role of lithium in the treatment of bipolar disorder: convergent evidence for neurotrophic effects as a unifying hypothesisPICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid systemAdducin 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 signalingA novel effect of MARCKS phosphorylation by activated PKC: the dephosphorylation of its serine 25 in chick neuroblasts.Functional involvement of protein kinase C-betaII and its substrate, myristoylated alanine-rich C-kinase substrate (MARCKS), in insulin-stimulated glucose transport in L6 rat skeletal muscle cellsDynamic adhesions and MARCKS in melanoma cellsElectrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins.Hippocampal infusions of MARCKS peptides impair memory of rats on the radial-arm mazeInhibition of myristoylated alanine-rich C kinase substrate (MARCKS) protein inhibits ozone-induced airway neutrophilia and inflammation.PhosphoMARCKS drives motility of mouse melanoma cells.Peptides derived from MARCKS block coagulation complex assembly on phosphatidylserine.Two myristoylated alanine-rich C-kinase substrate (MARCKS) paralogs are required for normal development in zebrafish.Myristoylated Alanine Rich C Kinase Substrate (MARCKS) is essential to β2-integrin dependent responses of equine neutrophils.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.Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results.Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: an electrostatic model and experimental results.A computational model for the electrostatic sequestration of PI(4,5)P2 by membrane-adsorbed basic peptides.Fluorescence correlation spectroscopy studies of Peptide and protein binding to phospholipid vesicles.The trk family of receptors mediates nerve growth factor and neurotrophin-3 effects in melanocytes.N-myristoylation regulates the axonal distribution of the Fragile X-related protein FXR2PCross-talk unfolded: MARCKS proteins.MARCKS deficiency in mice leads to abnormal brain development and perinatal death.NEUROBIOLOGY OF ADULT AND TEENAGE SUICIDESOD1 overexpression in vivo blocks hyperglycemia-induced specific PKC isoforms: substrate activation and consequent lipid peroxidation in diabetic embryopathyIdentification of a small molecule activator of novel PKCs for promoting glucose-dependent insulin secretion.The response of porcine monocyte derived macrophages and dendritic cells to Salmonella Typhimurium and lipopolysaccharideSequestration of phosphoinositides by mutated MARCKS effector domain inhibits stimulated Ca(2+) mobilization and degranulation in mast cells.Combined PKC and MEK inhibition in uveal melanoma with GNAQ and GNA11 mutations.MARCKS-dependent mucin clearance and lipid metabolism in ependymal cells are required for maintenance of forebrain homeostasis during aging.Regulation of peptide-calmodulin complexes by protein kinase C in vivoAngiotensin-II and MARCKS: a hydrogen peroxide- and RAC1-dependent signaling pathway in vascular endothelium.Protein kinase C-delta deficiency perturbs bone homeostasis by selective uncoupling of cathepsin K secretion and ruffled border formation in osteoclastsFunctional reconstitution in Escherichia coli of the yeast mitochondrial matrix peptidase from its two inactive subunits.
P2860
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P2860
The MARCKS family of cellular protein kinase C substrates
description
1993 nî lūn-bûn
@nan
1993 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
The MARCKS family of cellular protein kinase C substrates
@ast
The MARCKS family of cellular protein kinase C substrates
@en
The MARCKS family of cellular protein kinase C substrates
@nl
type
label
The MARCKS family of cellular protein kinase C substrates
@ast
The MARCKS family of cellular protein kinase C substrates
@en
The MARCKS family of cellular protein kinase C substrates
@nl
prefLabel
The MARCKS family of cellular protein kinase C substrates
@ast
The MARCKS family of cellular protein kinase C substrates
@en
The MARCKS family of cellular protein kinase C substrates
@nl
P1476
The MARCKS family of cellular protein kinase C substrates
@en
P2093
P J Blackshear
P304
P407
P577
1993-01-25T00:00:00Z