Structural analysis of receptor tyrosine kinases (Q28198048)

Progress in Biophysics and Molecular Biology

Europe PubMed Central

title

Structural analysis of receptor tyrosine kinases (English)

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author name string

S R Hubbard

series ordinal

1

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language of work or name

English

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publication date

1999

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published in

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volume

71

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issue

3-4

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page(s)

343-58

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cites work

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Shc Binding to Nerve Growth Factor Receptor Is Mediated by the Phosphotyrosine Interaction Domain

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Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

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A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor

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An epidermal growth factor receptor/Jak2 tyrosine kinase domain chimera induces tyrosine phosphorylation of Stat5 and transduces a growth signal in hematopoietic cells

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Self-phosphorylation of epidermal growth factor receptor is an intermolecular reaction

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Three protein kinase structures define a common motif

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Signal transduction by receptors with tyrosine kinase activity

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Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation

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Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor

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Catalytic specificity of protein-tyrosine kinases is critical for selective signalling

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Mutations of Ros differentially effecting signal transduction pathways leading to cell growth versus transformation

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

10354703

1 reference

Consolidated OpenCitations Corpus – April 2017