The MARCKS family of phospholipid binding proteins: regulation of phospholipase D and other cellular components
about
The polybasic region that follows the plant homeodomain zinc finger 1 of Pf1 is necessary and sufficient for specific phosphoinositide bindingX MARCKS the spot: myristoylated alanine-rich C kinase substrate in neuronal function and diseaseMARCKS-like protein is an initiating molecule in axolotl appendage regeneration.c-Jun N-terminal kinase phosphorylation of MARCKSL1 determines actin stability and migration in neurons and in cancer cellsskNAC depletion stimulates myoblast migration and perturbs sarcomerogenesis by enhancing calpain 1 and 3 activityFunctional 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 cellsMARCKS-like protein, a membrane protein identified for its expression in developing neural retina, plays a role in regulating retinal cell proliferationTetrapod limb and sarcopterygian fin regeneration share a core genetic programmeMARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactionsMARCKS protein is phosphorylated and regulates calcium mobilization during human acrosomal exocytosis.Synthesis and dephosphorylation of MARCKS in the late stages of megakaryocyte maturation drive proplatelet formation.Proteomic analysis uncovers novel actions of the neurosecretory protein VGF in nociceptive processing.Phospholipase D2 Enhances Epidermal Growth Factor-Induced Akt Activation in EL4 Lymphoma Cells.Liberated PKA Catalytic Subunits Associate with the Membrane via Myristoylation to Preferentially Phosphorylate Membrane SubstratesTwo myristoylated alanine-rich C-kinase substrate (MARCKS) paralogs are required for normal development in zebrafish.Fibroblast Migration Is Regulated by Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Protein.Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusionPlasma membrane phosphoinositide organization by protein electrostatics.How cholesterol regulates endothelial biomechanics.Phosphoinositides: regulators of membrane traffic and protein function.Regulation of PI3K by PKC and MARCKS: Single-Molecule Analysis of a Reconstituted Signaling PathwayThe alpha1a-adrenergic receptor occupies membrane rafts with its G protein effectors but internalizes via clathrin-coated pits.Quantitative proteomics analysis of human endothelial cell membrane rafts: evidence of MARCKS and MRP regulation in the sphingosine 1-phosphate-induced barrier enhancement.Inhibition of native and recombinant nicotinic acetylcholine receptors by the myristoylated alanine-rich C kinase substrate peptide.MARCKS modulates radial progenitor placement, proliferation and organization in the developing cerebral cortexThe role of the ubiquitin proteasome system in ischemia and ischemic tolerance.A possible role of myristoylated alanine-rich C kinase substrate in endocytic pathway of Alzheimer's disease.Evaluation of the novel protein kinase C inhibitor sotrastaurin as immunosuppressive therapy after renal transplantation.Plasma membrane--cortical cytoskeleton interactions: a cell biology approach with biophysical considerations.Functional characterization of the tumor-suppressor MARCKS in colorectal cancer and its association with survival.MARCKS dephosphorylation is involved in bradykinin-induced neurite outgrowth in neuroblastoma SH-SY5Y cells.Human prostate cell lines from normal and tumourigenic epithelia differ in the pattern and control of choline lipid headgroups released into the medium on stimulation of protein kinase C.Modulation of angiotensin II-mediated cardiac remodeling by the MEF2A target gene Xirp2.Differential expression, localization and activity of MARCKS between mantle cell lymphoma and chronic lymphocytic leukemia.Regulation of a Coupled MARCKS-PI3K Lipid Kinase Circuit by Calmodulin: Single-Molecule Analysis of a Membrane-Bound Signaling Module.Mesenchymal stem cells require MARCKS protein for directed chemotaxis in vitro.Myristoylated alanine-rich C kinase substrate (MARCKS): a multirole signaling protein in cancers.MARCKS actin-binding capacity mediates actin filament assembly during mitosis in human hepatic stellate cells.MARCKSL1 Regulates Spine Formation in the Amygdala and Controls the Hypothalamic-Pituitary-Adrenal Axis and Anxiety-Like Behaviors.Role of MARCKS in regulated secretion from mast cells and airway goblet cells.
P2860
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P2860
The MARCKS family of phospholipid binding proteins: regulation of phospholipase D and other cellular components
description
2004 nî lūn-bûn
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2004 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2004年の論文
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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
name
The MARCKS family of phospholi ...... and other cellular components
@ast
The MARCKS family of phospholi ...... and other cellular components
@en
The MARCKS family of phospholi ...... and other cellular components
@nl
type
label
The MARCKS family of phospholi ...... and other cellular components
@ast
The MARCKS family of phospholi ...... and other cellular components
@en
The MARCKS family of phospholi ...... and other cellular components
@nl
prefLabel
The MARCKS family of phospholi ...... and other cellular components
@ast
The MARCKS family of phospholi ...... and other cellular components
@en
The MARCKS family of phospholi ...... and other cellular components
@nl
P2093
P2860
P3181
P356
P1476
The MARCKS family of phospholi ...... and other cellular components
@en
P2093
David M Byers
Harold W Cook
Meenakshi Sundaram
P2860
P304
P3181
P356
10.1139/O03-087
P407
P577
2004-02-01T00:00:00Z