(Q28288388)

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The PTB domain: a new protein module implicated in signal transduction

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The PTB domain: a new protein module implicated in signal transduction (English)

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author name string

P van der Geer

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T Pawson

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language of work or name

English

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publication date

July 1995

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published in

Trends in Biochemical Sciences

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volume

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issue

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page(s)

277-80

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cites work

Protein modules and signalling networks

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A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction

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Signal transduction. How receptors turn Ras on.

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7 January 2021

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An alternative to SH2 domains for binding tyrosine-phosphorylated proteins

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Characterization of an interaction between insulin receptor substrate 1 and the insulin receptor by using the two-hybrid system

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Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain

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7 January 2021

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A conserved amino-terminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides

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7 January 2021

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A phosphotyrosine interaction domain

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7 January 2021

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Polyoma middle-sized T antigen can be phosphorylated on tyrosine at multiple sites in vitro

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7 January 2021

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Transformation by polyoma virus middle T-antigen involves the binding and tyrosine phosphorylation of Shc.

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7 January 2021

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Autophosphorylation sites on the epidermal growth factor receptor.

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The erbB gene of avian erythroblastosis virus is a member of the src gene family

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Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses

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Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activity

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7 January 2021

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Identifiers

DOI

10.1016/S0968-0004(00)89043-X

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4401032

OpenCitations bibliographic resource ID

4401032

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4401032

PubMed publication ID

7545337

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4401032

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