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The PTB domain: a new protein module implicated in signal transduction
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instance of
scholarly article
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review article
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title
The PTB domain: a new protein module implicated in signal transduction
(English)
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author name string
P van der Geer
series ordinal
1
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T Pawson
series ordinal
2
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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
20
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issue
7
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page(s)
277-80
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cites work
Protein modules and signalling networks
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https://api.crossref.org/works/10.1016%2FS0968-0004%2800%2989043-X
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7 January 2021
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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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7 January 2021
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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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reference URL
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7 January 2021
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A phosphotyrosine interaction domain
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Polyoma middle-sized T antigen can be phosphorylated on tyrosine at multiple sites in vitro
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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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7 January 2021
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The erbB gene of avian erythroblastosis virus is a member of the src gene family
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7 January 2021
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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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7 January 2021
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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
1 reference
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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