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John Kuriyan
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Articles

Crystal structure of an SH2–kinase construct of c-Abl and effect of the SH2 domain on kinase activity

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Sonja Lorenz, Patricia Deng, Oliver Hantschel, Giulio Superti-Furga, John Kuriyan
Journal: Biochemical Journal
Biochem J (2015) 468 (2): 283–291.
https://doi.org/10.1042/BJ20141492
Published: 22 May 2015
View articletitled, Crystal structure of an SH2–kinase construct of c-Abl and effect of the SH2 domain on kinase activity
Open the PDF for Crystal structure of an SH2–kinase construct of c-Abl and effect of the SH2 domain on kinase activity in another window
Includes: Supplementary data
Articles

Modification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding

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Patrick R. Visperas, Jonathan A. Winger, Timothy M. Horton, Neel H. Shah, Diane J. Aum, Alyssa Tao, Tiago Barros, Qingrong Yan, Christopher G. Wilson, Michelle R. Arkin, Arthur Weiss, John Kuriyan
Journal: Biochemical Journal
Biochem J (2015) 465 (1): 149–161.
https://doi.org/10.1042/BJ20140793
Published: 12 December 2014
View articletitled, Modification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding
Open the PDF for Modification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding in another window
Includes: Supplementary data
Articles

A highly efficient peptide substrate for EGFR activates the kinase by inducing aggregation

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Kate Engel, Tomoaki Sasaki, Qi Wang, John Kuriyan
Journal: Biochemical Journal
Biochem J (2013) 453 (3): 337–344.
https://doi.org/10.1042/BJ20130537
Published: 12 July 2013
View articletitled, A highly efficient peptide substrate for EGFR activates the kinase by inducing aggregation
Open the PDF for A highly efficient peptide substrate for EGFR activates the kinase by inducing aggregation in another window
Includes: Supplementary data