(Q28211088)

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Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain

scientific article (publication date: 15 July 1992)

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18 September 2019

Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain (English)

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18 September 2019

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N. Hashimoto

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13 September 2022

E. P. Feener

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W. R. Zhang

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B. J. Goldstein

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1 July 1992

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18 September 2019

15 July 1992

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13 September 2022

full work available at URL

http://intl.jbc.org/cgi/content/abstract/267/20/13811

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Journal of Biological Chemistry

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18 September 2019

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18 September 2019

13811-13814

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18 September 2019

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18 September 2019

After insulin binds

1

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The insulin receptor and the molecular mechanism of insulin action

2

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Studies on the autophosphorylation of the insulin receptor from human placenta. Analysis of the sites phosphorylated by two-dimensional peptide mapping

6

1 reference

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Protein‐Tyrosine phosphatases and the regulation of insulin action

11

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Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes

12

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Site-specific dephosphorylation and deactivation of the human insulin receptor tyrosine kinase by particulate and soluble phosphotyrosyl protein phosphatases

15

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Dephosphorylation of autophosphorylated insulin and epidermal-growth-factor receptors by two major subtypes of protein-tyrosine-phosphatase from human placenta

16

1 reference

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Microinjection of a protein-tyrosine-phosphatase inhibits insulin action in Xenopus oocytes

18

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Purification and characterization of a soluble catalytic fragment of the human transmembrane leukocyte antigen related (LAR) protein tyrosine phosphatase from an Escherichia coli expression system.

20

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Catalytic domains of the LAR and CD45 protein tyrosine phosphatases from Escherichia coli expression systems: purification and characterization for specificity and mechanism

22

1 reference

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

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Identification of skeletal muscle protein-tyrosine phosphatases by amplification of conserved cDNA sequences

24

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A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen

25

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Identification of an additional member of the protein-tyrosine-phosphatase family: evidence for alternative splicing in the tyrosine phosphatase domain

26

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Cloning and expression of a widely expressed receptor tyrosine phosphatase

27

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Cloning and expression of a protein-tyrosine-phosphatase

29

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Cloning of a cDNA for a major human protein-tyrosine-phosphatase

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Purification and characterization of a higher-molecular-mass form of protein phosphotyrosine phosphatase (PTP 1B) from placental membranes.

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The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence

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Determinants of membrane protein topology

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A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila

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Phosphorylation of the insulin receptor in cultured hepatoma cells and a solubilized system

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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Approaches to the molecular cloning of protein-tyrosine phosphatases in insulin-sensitive tissues

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Cloning and chromosomal assignment of a widely expressed human receptor-like protein-tyrosine phosphatase

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18 September 2019

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