(Q28307065)

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Protein-tyrosine phosphatase (PTP) wedge domain peptides: a novel approach for inhibition of PTP function and augmentation of protein-tyrosine kinase function

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Protein-tyrosine phosphatase (PTP) wedge domain peptides: a novel approach for inhibition of PTP function and augmentation of protein-tyrosine kinase function (English)

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author name string

Youmei Xie

1

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Stephen M Massa

2

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Sonya E Ensslen-Craig

3

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Denice L Major

4

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Tao Yang

5

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Michelle A Tisi

6

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Vicki D Derevyanny

7

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William O Runge

8

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Brijesh P Mehta

9

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Laura A Moore

10

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Susann M Brady-Kalnay

11

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Frank M Longo

12

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language of work or name

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publication date

16 June 2006

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Journal of Biological Chemistry

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281

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24

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16482-92

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Creutzfeldt-Jakob disease: analysis of the MRI signal.

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Combinatorial control of the specificity of protein tyrosine phosphatases

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Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases

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Deficient LAR expression decreases basal forebrain cholinergic neuronal size and hippocampal cholinergic innervation

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Delayed peripheral nerve regeneration and central nervous system collateral sprouting in leucocyte common antigen-related protein tyrosine phosphatase-deficient mice

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Receptor protein tyrosine phosphatases in nervous system development

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Caveolin interacts with Trk A and p75(NTR) and regulates neurotrophin signaling pathways

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Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization

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Crystal structure of the tandem phosphatase domains of RPTP LAR

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Peptide modulators of protein-protein interactions in intracellular signaling

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Protein transduction technology

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The transmembrane protein-tyrosine phosphatase LAR modulates signaling by multiple receptor tyrosine kinases

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A novel neurotrophic property of glucagon-like peptide 1: a promoter of nerve growth factor-mediated differentiation in PC12 cells

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PTP mu-dependent growth cone rearrangement is regulated by Cdc42

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PTPmu signaling via PKCdelta is instructive for retinal ganglion cell guidance

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PTP mu expression and catalytic activity are required for PTP mu-mediated neurite outgrowth and repulsion

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Receptor protein tyrosine phosphatases regulate neural development and axon guidance

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PTPmu regulates N-cadherin-dependent neurite outgrowth

1 reference

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Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation

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Regulatory mechanisms for receptor protein tyrosine phosphatases

1 reference

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The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu

1 reference

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The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma

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Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine phosphatase domains of various RPTPs

1 reference

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Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases

1 reference

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Intramolecular interactions between the juxtamembrane domain and phosphatase domains of receptor protein-tyrosine phosphatase RPTPmu. Regulation of catalytic activity

1 reference

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The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains

1 reference

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Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins

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SHP-1 negatively regulates neuronal survival by functioning as a TrkA phosphatase

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Identifiers

10.1074/JBC.M603131200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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