(Q24322758)

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Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide

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Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide (English)

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crystal structure

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phosphorylation

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Klaus Fütterer

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K Fütterer

1

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author name string

J Wong

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R A Grucza

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A C Chan

4

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G Waksman

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language of work or name

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publication date

21 August 1998

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Journal of Molecular Biology

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281

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3

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523-37

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Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement

1 reference

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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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Reconstitution of Syk function by the ZAP-70 protein tyrosine kinase

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Protein tyrosine kinase Syk is associated with and activated by the IL-2 receptor: possible link with the c-myc induction pathway

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Conformation of Polypeptides and Proteins

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

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Crystal structure of the tyrosine phosphatase SHP-2

1 reference

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Regulation of antigen receptor signal transduction by protein tyrosine kinases

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Molecular mechanisms in B cell antigen receptor signaling

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Complex complexes: signaling at the TCR.

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Antigen receptor tail clue.

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

1 reference

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Immunoreceptor DAP12 bearing a tyrosine-based activation motif is involved in activating NK cells

1 reference

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Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

1 reference

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Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck

1 reference

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Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor

1 reference

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Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2

1 reference

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Tyrosine kinases in activation of the MAP kinase cascade by G-protein-coupled receptors

1 reference

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Granulocyte colony-stimulating factor receptor signaling involves the formation of a three-component complex with Lyn and Syk protein-tyrosine kinases

1 reference

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Analysis of the interaction of ZAP-70 and syk protein-tyrosine kinases with the T-cell antigen receptor by plasmon resonance

1 reference

https://api.crossref.org/works/10.1006%2FJMBI.1998.1964

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syk kinase activation by a src kinase-initiated activation loop phosphorylation chain reaction

1 reference

https://api.crossref.org/works/10.1006%2FJMBI.1998.1964

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Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation

1 reference

https://api.crossref.org/works/10.1006%2FJMBI.1998.1964

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Phosphoinositide 3-Kinase and p72 Noncovalently Associate with the Low Affinity Fc Receptor on Human Platelets through an Immunoreceptor Tyrosine-based Activation Motif

1 reference

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Phosphoinositide 3-kinase and p72syk noncovalently associate with the low affinity Fc gamma receptor on human platelets through an immunoreceptor tyrosine-based activation motif. Reconstitution with synthetic phosphopeptides

1 reference

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Differential intrinsic enzymatic activity of Syk and Zap-70 protein-tyrosine kinases

1 reference

https://api.crossref.org/works/10.1006%2FJMBI.1998.1964

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Interaction of phosphorylated FcepsilonRIgamma immunoglobulin receptor tyrosine activation motif-based peptides with dual and single SH2 domains of p72syk. Assessment of binding parameters and real time binding kinetics

1 reference

https://api.crossref.org/works/10.1006%2FJMBI.1998.1964

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ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity

1 reference

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Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling

1 reference

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Transfection of Syk protein tyrosine kinase reconstitutes high affinity IgE receptor-mediated degranulation in a Syk-negative variant of rat basophilic leukemia RBL-2H3 cells

1 reference

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Functional role for Syk tyrosine kinase in natural killer cell-mediated natural cytotoxicity

1 reference

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A critical role for Syk in signal transduction and phagocytosis mediated by Fcgamma receptors on macrophages

1 reference

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Regulation of the pp72syk protein tyrosine kinase by platelet integrin alpha IIb beta 3

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The Fc receptor gamma-chain and the tyrosine kinase Syk are essential for activation of mouse platelets by collagen

1 reference

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

1 reference

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Generalized method of determining heavy-atom positions using the difference Patterson function

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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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Accurate bond and angle parameters for X-ray protein structure refinement

1 reference

https://api.crossref.org/works/10.1006%2FJMBI.1998.1964

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The CCP4 suite: programs for protein crystallography

1 reference

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Raster3D Version 2.0. A program for photorealistic molecular graphics

1 reference

https://api.crossref.org/works/10.1006%2FJMBI.1998.1964

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Current approaches to macromolecular crystallization

1 reference

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Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases

1 reference

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Interaction of p72syk with the gamma and beta subunits of the high-affinity receptor for immunoglobulin E, Fc epsilon RI

1 reference

https://api.crossref.org/works/10.1006%2FJMBI.1998.1964

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Clustering of Syk is sufficient to induce tyrosine phosphorylation and release of allergic mediators from rat basophilic leukemia cells

1 reference

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Initiation and processing of signals from the B cell antigen receptor

1 reference

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10.1006/JMBI.1998.1964

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

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