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Modification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding.
Visperas, Patrick R; Winger, Jonathan A; Horton, Timothy M; Shah, Neel H; Aum, Diane J; Tao, Alyssa; Barros, Tiago; Yan, Qingrong; Wilson, Christopher G; Arkin, Michelle R; Weiss, Arthur; Kuriyan, John.
Afiliação
  • Visperas PR; *Department of Molecular and Cell Biology and Department of Chemistry, California Institute of Quantitative Biosciences and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, U.S.A.
  • Winger JA; *Department of Molecular and Cell Biology and Department of Chemistry, California Institute of Quantitative Biosciences and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, U.S.A.
  • Horton TM; *Department of Molecular and Cell Biology and Department of Chemistry, California Institute of Quantitative Biosciences and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, U.S.A.
  • Shah NH; *Department of Molecular and Cell Biology and Department of Chemistry, California Institute of Quantitative Biosciences and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, U.S.A.
  • Aum DJ; *Department of Molecular and Cell Biology and Department of Chemistry, California Institute of Quantitative Biosciences and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, U.S.A.
  • Tao A; *Department of Molecular and Cell Biology and Department of Chemistry, California Institute of Quantitative Biosciences and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, U.S.A.
  • Barros T; *Department of Molecular and Cell Biology and Department of Chemistry, California Institute of Quantitative Biosciences and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, U.S.A.
  • Yan Q; *Department of Molecular and Cell Biology and Department of Chemistry, California Institute of Quantitative Biosciences and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, U.S.A.
  • Wilson CG; †Department of Pharmaceutical Chemistry, Small Molecule Discovery Center, University of California, San Francisco, CA 94158, U.S.A.
  • Arkin MR; †Department of Pharmaceutical Chemistry, Small Molecule Discovery Center, University of California, San Francisco, CA 94158, U.S.A.
  • Weiss A; ‡Department of Medicine, Rosalind Russell and Ephrain P. Engleman Rheumatology Research Center for Arthritis and Howard Hughes Medical Institute, University of California, San Francisco, CA 94143, U.S.A.
  • Kuriyan J; *Department of Molecular and Cell Biology and Department of Chemistry, California Institute of Quantitative Biosciences and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, U.S.A.
Biochem J ; 465(1): 149-61, 2015 Jan 01.
Article em En | MEDLINE | ID: mdl-25287889
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfopeptídeos / Proteínas Tirosina Quinases / Domínios de Homologia de src / Cisteína / Peptídeos e Proteínas de Sinalização Intracelular / Proteína-Tirosina Quinase ZAP-70 Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Revista: Biochem J Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Estados Unidos
Texto completo
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfopeptídeos / Proteínas Tirosina Quinases / Domínios de Homologia de src / Cisteína / Peptídeos e Proteínas de Sinalização Intracelular / Proteína-Tirosina Quinase ZAP-70 Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Revista: Biochem J Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Estados Unidos