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Phosphotyrosine interactome of the ErbB-receptor kinase family
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title
Phosphotyrosine interactome of the ErbB-receptor kinase family
(English)
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main subject
applied mathematics
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information system
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author name string
Waltraud X Schulze
series ordinal
1
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Lei Deng
series ordinal
2
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Matthias Mann
series ordinal
3
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language of work or name
English
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publication date
2005
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published in
Molecular Systems Biology
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volume
1
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page(s)
2005.0008
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issue
1
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The efficacy of Herceptin therapies is influenced by the expression of other erbB receptors, their ligands and the activation of downstream signalling proteins
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Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems.
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SH2 and PTB domains in tyrosine kinase signaling.
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28 September 2017
Phosphotyrosine-binding domains in signal transduction.
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PTB or not PTB -- that is the question.
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28 September 2017
Can we infer peptide recognition specificity mediated by SH3 domains?
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Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines.
1 reference
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28 September 2017
The ErbB receptor tyrosine family as signal integrators.
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28 September 2017
Adaptor-related proteins.
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28 September 2017
The EGF receptor as central transducer of heterologous signalling systems.
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28 September 2017
Epidermal growth factor receptors: critical mediators of multiple receptor pathways.
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PubMed Central
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28 September 2017
ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling.
1 reference
stated in
PubMed Central
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28 September 2017
Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr974-containing internalization motif.
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PubMed Central
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28 September 2017
Efficient coupling with phosphatidylinositol 3-kinase, but not phospholipase C gamma or GTPase-activating protein, distinguishes ErbB-3 signaling from that of other ErbB/EGFR family members.
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PubMed Central
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28 September 2017
SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase C gamma.
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PubMed Central
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28 September 2017
Tyrosine-phosphorylated epidermal growth factor receptor and cellular p130 provide high affinity binding substrates to analyze Crk-phosphotyrosine-dependent interactions in vitro.
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PubMed Central
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28 September 2017
Trypsin cleaves exclusively C-terminal to arginine and lysine residues.
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PubMed Central
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28 November 2018
Identifiers
DOI
10.1038/MSB4100012
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3681599
OpenCitations bibliographic resource ID
3681599
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3681599
PMCID
1681463
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3681599
PubMed ID
16729043
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3681599
ResearchGate publication ID
7053711
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