Dephosphorylation increases insulin-stimulated receptor kinase activity in skeletal muscle of obese Zucker rats (Q77952724)

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9 December 2019

title

Dephosphorylation increases insulin-stimulated receptor kinase activity in skeletal muscle of obese Zucker rats (English)

1 reference

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9 December 2019

author name string

Q Zhou

series ordinal

1

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9 December 2019

P L Dolan

series ordinal

2

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9 December 2019

G L Dohm

series ordinal

3

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9 December 2019

publication date

1 April 1999

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Molecular and Cellular Biochemistry

9 December 2019

published in

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9 December 2019

volume

194

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9 December 2019

page(s)

209-216

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9 December 2019

issue

1-2

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https://scigraph.springernature.com/pub.10.1023/a:1006942831223

9 December 2019

exact match

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cites work

A defective intramolecular autoactivation cascade may cause the reduced kinase activity of the skeletal muscle insulin receptor from patients with non-insulin-dependent diabetes mellitus

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Defective insulin receptor tyrosine kinase in human skeletal muscle in obesity and type 2 (non-insulin-dependent) diabetes mellitus

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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

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Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

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Insulin receptor signaling is augmented by antisense inhibition of the protein tyrosine phosphatase LAR.

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Glycemia and exercise training alter glucose transport and GLUT4 in the Zucker rat.

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Expression of the major isoenzyme of protein kinase-C in skeletal muscle, nPKC theta, varies with muscle type and in response to fructose-induced insulin resistance

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A cascade of tyrosine autophosphorylation in the beta-subunit activates the phosphotransferase of the insulin receptor.

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Insulin receptor kinase in human skeletal muscle from obese subjects with and without noninsulin dependent diabetes

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IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha- and obesity-induced insulin resistance

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Effect of exercise on synthesis and degradation of muscle protein

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Chronic activation of protein kinase C in soleus muscles and other tissues of insulin-resistant type II diabetic Goto-Kakizaki (GK), obese/aged, and obese/Zucker rats. A mechanism for inhibiting glycogen synthesis

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Early metabolic defects in persons at increased risk for non-insulin-dependent diabetes mellitus.

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Purification and partial sequence analysis of pp185, the major cellular substrate of the insulin receptor tyrosine kinase

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Exercise training and clenbuterol reduce insulin resistance of obese Zucker rats.

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Glucose uptake and GLUT-4 protein distribution in skeletal muscle of the obese Zucker rat.

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Phorbol ester-induced serine phosphorylation of the insulin receptor decreases its tyrosine kinase activity

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Protein kinase C directly phosphorylates the insulin receptor in vitro and reduces its protein-tyrosine kinase activity

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Alterations in the expression and cellular localization of protein kinase C isozymes epsilon and theta are associated with insulin resistance in skeletal muscle of the high-fat-fed rat

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Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free system

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Tumor-promoting phorbol esters increase the Km of the ATP-binding site of the insulin receptor kinase from rat adipocytes.

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12 December 2020

Impaired insulin signaling in skeletal muscles from transgenic mice expressing kinase-deficient insulin receptors

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12 December 2020

Excessive insulin receptor serine phosphorylation in cultured fibroblasts and in skeletal muscle. A potential mechanism for insulin resistance in the polycystic ovary syndrome

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12 December 2020

Dephosphorylation of the insulin receptor partially restores the decreased autophosphorylation in streptozotocin induced diabetic rats.

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12 December 2020

Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor

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12 December 2020