PDGF receptor as a specific in vivo target for low M(r) phosphotyrosine protein phosphatase.
about
Site-selective regulation of platelet-derived growth factor beta receptor tyrosine phosphorylation by T-cell protein tyrosine phosphataseEph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responsesCrystal structure and putative substrate identification for the Entamoeba histolytica low molecular weight tyrosine phosphatase.Glutaredoxin modulates platelet-derived growth factor-dependent cell signaling by regulating the redox status of low molecular weight protein-tyrosine phosphataseCloning of murine low molecular weight phosphotyrosine protein phosphatase cDNA: identification of a new isoformExpression, purification and preliminary crystal analysis of the human low Mr phosphotyrosine protein phosphatase isoform 1.Mechanisms of platelet-derived growth factor-induced chemotaxis.Low-molecular-weight protein tyrosine phosphatase is a positive component of the fibroblast growth factor receptor signaling pathway.Protein tyrosine phosphatases as potential therapeutic targets.Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilisKnocking down low molecular weight protein tyrosine phosphatase (LMW-PTP) reverts chemoresistance through inactivation of Src and Bcr-Abl proteins.Protein phosphorylation by semisynthesis: from paper to practice.Low molecular weight protein tyrosine phosphatase isoforms regulate breast cancer cells migration through a RhoA dependent mechanism.Redox regulation of protein kinases.Low molecular weight protein tyrosine phosphatase (LMWPTP) upregulation mediates malignant potential in colorectal cancer.Regulation of TCR signalling by tyrosine phosphatases: from immune homeostasis to autoimmunity.The role of low-molecular-weight protein tyrosine phosphatase (LMW-PTP ACP1) in oncogenesis.Phosphorylation of the platelet-derived growth factor receptor-beta and epidermal growth factor receptor by G protein-coupled receptor kinase-2. Mechanisms for selectivity of desensitization.The platelet-derived growth factor receptor-beta phosphorylates and activates G protein-coupled receptor kinase-2. A mechanism for feedback inhibition.Insulin inhibits platelet-derived growth factor-induced cell proliferation.Low molecular weight protein-tyrosine phosphatase is involved in growth inhibition during cell differentiation.Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation.Tyrosine-phosphorylated caveolin is a physiological substrate of the low M(r) protein-tyrosine phosphatase.Identification of p130cas as an in vivo substrate of receptor protein-tyrosine phosphatase alpha.Sequence-specific recognition of peptide substrates by the low Mr phosphotyrosine protein phosphatase isoforms.Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion.Low molecular weight protein-tyrosine phosphatase controls the rate and the strength of NIH-3T3 cells adhesion through its phosphorylation on tyrosine 131 or 132.The low M(r) protein-tyrosine phosphatase is involved in Rho-mediated cytoskeleton rearrangement after integrin and platelet-derived growth factor stimulation.Insight into the role of low molecular weight phosphotyrosine phosphatase (LMW-PTP) on platelet-derived growth factor receptor (PDGF-r) signaling. LMW-PTP controls PDGF-r kinase activity through TYR-857 dephosphorylation.Low molecular weight protein-tyrosine phosphatase tyrosine phosphorylation by c-Src during platelet-derived growth factor-induced mitogenesis correlates with its subcellular targeting.The Src and signal transducers and activators of transcription pathways as specific targets for low molecular weight phosphotyrosine-protein phosphatase in platelet-derived growth factor signaling.Protein tyrosine phosphatase LMW-PTP exhibits distinct roles between vascular endothelial and smooth muscle cells.Oxidation and inactivation of low molecular weight protein tyrosine phosphatase by the anticancer drug Aplidin.The inactivation mechanism of low molecular weight phosphotyrosine-protein phosphatase by H2O2.The solution structure of Escherichia coli Wzb reveals a novel substrate recognition mechanism of prokaryotic low molecular weight protein-tyrosine phosphatases.
P2860
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P2860
PDGF receptor as a specific in vivo target for low M(r) phosphotyrosine protein phosphatase.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
PDGF receptor as a specific in vivo target for low M
@nl
PDGF receptor as a specific in ...... otyrosine protein phosphatase.
@en
type
label
PDGF receptor as a specific in vivo target for low M
@nl
PDGF receptor as a specific in ...... otyrosine protein phosphatase.
@en
prefLabel
PDGF receptor as a specific in vivo target for low M
@nl
PDGF receptor as a specific in ...... otyrosine protein phosphatase.
@en
P2093
P2860
P1433
P1476
PDGF receptor as a specific in ...... otyrosine protein phosphatase.
@en
P2093
Chiarugi P
P2860
P356
10.1016/0014-5793(95)00947-8
P407
P577
1995-09-01T00:00:00Z