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Crystal structure of the Src family tyrosine kinase Hck
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scholarly article
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title
Crystal structure of the Src family tyrosine kinase Hck
(English)
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main subject
crystal structure
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author name string
F Sicheri
series ordinal
1
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I Moarefi
series ordinal
2
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J Kuriyan
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)
602-9
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cites work
Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cells
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Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin
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Functional overlap in the src gene family: inactivation of hck and fgr impairs natural immunity
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Protein modules and signalling networks
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Modular binding domains in signal transduction proteins
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Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
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Crystal structure of a Src-homology 3 (SH3) domain
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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
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Crystal structure of the tyrosine kinase domain of the human insulin receptor
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Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
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Active and inactive protein kinases: structural basis for regulation
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Left-handed polyproline II helices commonly occur in globular proteins.
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Structural basis for the binding of proline-rich peptides to SH3 domains
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High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
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Structure of the regulatory domains of the Src-family tyrosine kinase Lck
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Crystal structure of cyclin-dependent kinase 2
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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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SH2 domains recognize specific phosphopeptide sequences
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Measurement of the binding of tyrosyl phosphopeptides to SH2 domains: a reappraisal
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Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
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A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein
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Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
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Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactions
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Structural differences between repressed and derepressed forms of p60c-src
1 reference
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Cell cycle. Confirmational change.
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Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation
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Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src
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Cell transformation by pp60c-src mutated in the carboxy-terminal regulatory domain
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Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src
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Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement
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The Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, Hck
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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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Improved methods for building protein models in electron density maps and the location of errors in these models
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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
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Crystallographic refinement by simulated annealing. Application to a 2.8 A resolution structure of aspartate aminotransferase.
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inferred from DOI database lookup
Identifiers
DOI
10.1038/385602A0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4106238
Dimensions Publication ID
1034217411
0 references
OpenCitations bibliographic resource ID
4106238
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4106238
PubMed publication ID
9024658
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4106238
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