(Q37544348)

English

Structural basis for differential recognition of tyrosine-phosphorylated sites in the linker for activation of T cells (LAT) by the adaptor Gads

scientific article published on 18 March 2004

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scholarly article

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Europe PubMed Central

PMC publication ID

20 August 2017

Structural basis for differential recognition of tyrosine-phosphorylated sites in the linker for activation of T cells (LAT) by the adaptor Gads (English)

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

phosphorylation

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author name string

Sangwoo Cho

1

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

C Alejandro Velikovsky

2

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

Chittoor P Swaminathan

3

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

Jon C D Houtman

4

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

Lawrence E Samelson

5

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

Roy A Mariuzza

6

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Europe PubMed Central

PMC publication ID

20 August 2017

language of work or name

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publication date

18 March 2004

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Europe PubMed Central

PMC publication ID

20 August 2017

The EMBO Journal

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Europe PubMed Central

PMC publication ID

20 August 2017

23

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Europe PubMed Central

PMC publication ID

20 August 2017

7

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

1441-1451

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

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1 reference

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The importance of three membrane-distal tyrosines in the adaptor protein NTAL/LAB

1 reference

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Adaptors as central mediators of signal transduction in immune cells

1 reference

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LAB: a new membrane-associated adaptor molecule in B cell activation

1 reference

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Non-T cell activation linker (NTAL): a transmembrane adaptor protein involved in immunoreceptor signaling

1 reference

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Molecular recognition by SH2 domains

1 reference

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1 reference

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1 reference

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1 reference

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Association of Grb2, Gads, and phospholipase C-gamma 1 with phosphorylated LAT tyrosine residues. Effect of LAT tyrosine mutations on T cell angigen receptor-mediated signaling

1 reference

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1 reference

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1 reference

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Essential role of LAT in T cell development

1 reference

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Structural and conformational requirements for high-affinity binding to the SH2 domain of Grb2(1)

1 reference

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Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc

1 reference

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

1 reference

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LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation

1 reference

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Thermodynamic and structural analysis of phosphotyrosine polypeptide binding to Grb2-SH2

1 reference

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ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling

1 reference

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Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode

1 reference

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Rapid identification of phosphopeptide ligands for SH2 domains. Screening of peptide libraries by fluorescence-activated bead sorting

1 reference

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How to measure and predict the molar absorption coefficient of a protein

1 reference

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SH2 domains recognize specific phosphopeptide sequences

1 reference

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1 reference

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Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav

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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Minimal requirement of tyrosine residues of linker for activation of T cells in TCR signaling and thymocyte development.

1 reference

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Requirement for the leukocyte-specific adapter protein SLP-76 for normal T cell development

1 reference

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Identification of the minimal tyrosine residues required for linker for activation of T cell function

1 reference

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Impaired viability and profound block in thymocyte development in mice lacking the adaptor protein SLP-76.

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Alternative Modes of Tyrosyl Phosphopeptide Binding to a Src Family SH2 Domain: Implications for Regulation of Tyrosine Kinase Activity†

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Calorimetric examination of high-affinity Src SH2 domain-tyrosyl phosphopeptide binding: dissection of the phosphopeptide sequence specificity and coupling energetics

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/15029250

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1 reference

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1 reference

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12 December 2020

based on heuristic

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Identifiers

10.1038/SJ.EMBOJ.7600168

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

20 August 2017

ResearchGate publication ID

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