Insulin receptor and epidermal growth factor receptor dephosphorylation by three major rat liver protein-tyrosine phosphatases expressed in a recombinant bacterial system.

Insulin receptor and epidermal growth factor receptor dephosphorylation by three major rat liver protein-tyrosine phosphatases expressed in a recombinant bacterial system.

Item
http://www.wikidata.org/entity/Q41870720
Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signalingAssociation of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTP1CThe transmembrane protein-tyrosine phosphatase LAR modulates signaling by multiple receptor tyrosine kinasesEpidermal growth factor receptor mutation in combination with expression of MIG6 alters gefitinib sensitivity.Increased abundance of the receptor-type protein-tyrosine phosphatase LAR accounts for the elevated insulin receptor dephosphorylating activity in adipose tissue of obese human subjects.Redox paradox: insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targetsThe novel protein-tyrosine phosphatase PTP20 is a positive regulator of PC12 cell neuronal differentiation.Growth inhibition of human lung adenocarcinoma cells by antibodies against epidermal growth factor receptor and by ganglioside GM3: involvement of receptor-directed protein tyrosine phosphatase(s).Differential effects of leukocyte common antigen-related protein on biochemical and biological activities of RET-MEN2A and RET-MEN2B mutant proteins.Receptor-like protein-tyrosine phosphatase alpha specifically inhibits insulin-increased prolactin gene expression.LAR-PTPase cDNA transfection suppression of tumor growth of neu oncogene-transformed human breast carcinoma cells.Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway.Regulation of an hepatic low-M(r) membrane-associated protein-tyrosine phosphatase.Altered basal and insulin-stimulated phosphotyrosine phosphatase (PTPase) activity in skeletal muscle from NIDDM patients compared with control subjects.The dephosphorylation characteristics of the receptors for epidermal growth factor and platelet-derived growth factor in Swiss 3T3 cell membranes suggest differential regulation of receptor signalling by endogenous protein-tyrosine phosphatases.Hepatic very low density lipoprotein-ApoB overproduction is associated with attenuated hepatic insulin signaling and overexpression of protein-tyrosine phosphatase 1B in a fructose-fed hamster model of insulin resistance.
P2860

Insulin receptor and epidermal growth factor receptor dephosphorylation by three major rat liver protein-tyrosine phosphatases expressed in a recombinant bacterial system.

Item
http://www.wikidata.org/entity/Q41870720
description
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1992年の論文
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name
Insulin receptor and epidermal ...... recombinant bacterial system.
@en
type
label
Insulin receptor and epidermal ...... recombinant bacterial system.
@en
prefLabel
Insulin receptor and epidermal ...... recombinant bacterial system.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P478
P577
P5875
P698
P932
P356
P1433
P1476
Insulin receptor and epidermal ...... recombinant bacterial system.
@en
P2093
P2860
P304
P31
P356
P407
P478
P577
P5875
P698
P932