about
MYRbase: analysis of genome-wide glycine myristoylation enlarges the functional spectrum of eukaryotic myristoylated proteinsRole of protein kinase C isoforms in bile formation and cholestasisA conserved polybasic domain mediates plasma membrane targeting of Lgl and its regulation by hypoxiaA novel effect of MARCKS phosphorylation by activated PKC: the dephosphorylation of its serine 25 in chick neuroblasts.α-Tocopherol and Hippocampal Neural Plasticity in Physiological and Pathological Conditionsc-Jun N-terminal kinase phosphorylation of MARCKSL1 determines actin stability and migration in neurons and in cancer cellsMyelin-mediated inhibition of oligodendrocyte precursor differentiation can be overcome by pharmacological modulation of Fyn-RhoA and protein kinase C signallingReverse Signaling by Semaphorin-6A Regulates Cellular Aggregation and Neuronal MorphologyFunctional 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 cellsThe regulation of M1 muscarinic acetylcholine receptor desensitization by synaptic activity in cultured hippocampal neuronsAnalysis of protein phosphorylation in nerve terminal reveals extensive changes in active zone proteins upon exocytosisMARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactionsElectrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins.Actin polymerization in macrophages in response to oxidized LDL and apoptotic cells: role of 12/15-lipoxygenase and phosphoinositide 3-kinase.Actin filament assembly by myristoylated alanine-rich C kinase substrate-phosphatidylinositol-4,5-diphosphate signaling is critical for dendrite branchingThe MARCKS protein plays a critical role in phosphatidylinositol 4,5-bisphosphate metabolism and directed cell movement in vascular endothelial cellsA cascade of protein kinase C isozymes promotes cytoskeletal polarization in T cells.Diacylglycerol promotes centrosome polarization in T cells via reciprocal localization of dynein and myosin IIA cell motility screen reveals role for MARCKS-related protein in adherens junction formation and tumorigenesisMARCKS protein is phosphorylated and regulates calcium mobilization during human acrosomal exocytosis.Proteomic modeling for HIV-1 infected microglia-astrocyte crosstalk.Protein kinase Cepsilon is important for migration of neuroblastoma cellsSynthesis and dephosphorylation of MARCKS in the late stages of megakaryocyte maturation drive proplatelet formation.Laser capture microdissection and genetic analysis of carbon-labeled Kupffer cells.MARCKS regulates membrane targeting of Rab10 vesicles to promote axon development.High-resolution 1H MAS RFDR NMR of biological membranes.Hippocampal infusions of MARCKS peptides impair memory of rats on the radial-arm mazePrednisolone-induced differential gene expression in mouse liver carrying wild type or a dimerization-defective glucocorticoid receptor.MARCKS phosphorylation is modulated by a peptide mimetic of MARCKS effector domain leading to increased radiation sensitivity in lung cancer cell linesInhibition of myristoylated alanine-rich C kinase substrate (MARCKS) protein inhibits ozone-induced airway neutrophilia and inflammation.PhosphoMARCKS drives motility of mouse melanoma cells.NADPH oxidases regulate cell growth and migration in myeloid cells transformed by oncogenic tyrosine kinases.Myristoylation: An Important Protein Modification in the Immune ResponseDifferentiation-Associated Expression of Conventional Protein Kinase C Isoforms in Primary Cultures of Bone Marrow Cells Induced by M-CSF and G-CSF.Exosomes and microvesicles: identification and targeting by particle size and lipid chemical probes.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.Fluorescence correlation spectroscopy studies of Peptide and protein binding to phospholipid vesicles.Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer.LAP2 is widely overexpressed in diverse digestive tract cancers and regulates motility of cancer cells.
P2860
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P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Cross-talk unfolded: MARCKS proteins.
@ast
Cross-talk unfolded: MARCKS proteins.
@en
Cross-talk unfolded: MARCKS proteins.
@nl
type
label
Cross-talk unfolded: MARCKS proteins.
@ast
Cross-talk unfolded: MARCKS proteins.
@en
Cross-talk unfolded: MARCKS proteins.
@nl
prefLabel
Cross-talk unfolded: MARCKS proteins.
@ast
Cross-talk unfolded: MARCKS proteins.
@en
Cross-talk unfolded: MARCKS proteins.
@nl
P2093
P2860
P1433
P1476
Cross-talk unfolded: MARCKS proteins.
@en
P2093
Anna Arbuzova
Arndt A P Schmitz
Guy Vergères
P2860
P356
10.1042/0264-6021:3620001
P407
P577
2002-02-01T00:00:00Z