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Three-dimensional structure of the tyrosine kinase c-Src
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title
Three-dimensional structure of the tyrosine kinase c-Src
(English)
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author
Wenqing Xu
object named as
W Xu
series ordinal
1
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author name string
S C Harrison
series ordinal
2
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M J Eck
series ordinal
3
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language of work or name
English
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publication date
13 February 1997
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published in
Nature
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volume
385
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issue
6617
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page(s)
595-602
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cites work
Viral oncogenes
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Structure-function relationships in Src family and related protein tyrosine kinases
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Protein modules and signalling networks
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Solution structure of the SH3 domain of Src and identification of its ligand-binding site
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High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
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Identification of a ten-amino acid proline-rich SH3 binding site
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The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity
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SH2 domains recognize specific phosphopeptide sequences
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Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms
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Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck
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Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src
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Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src
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The when and how of Src regulation
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Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
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Active and inactive protein kinases: structural basis for regulation
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Structure of the regulatory domains of the Src-family tyrosine kinase Lck
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Modular peptide recognition domains in eukaryotic signaling
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Correlation of the phosphorylation states of pp60c-src with tyrosine kinase activity: the intramolecular pY530-SH2 complex retains significant activity if Y419 is phosphorylated
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1 reference
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Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel p130Cas-related protein, Sin.
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Identifiers
DOI
10.1038/385595A0
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stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1239921
Dimensions Publication ID
1032796118
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OpenCitations bibliographic resource ID
1239921
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1239921
PubMed publication ID
9024657
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1239921
ResearchGate publication ID
14184463
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