John Kuriyan in 2015, portrait via the Royal Society
|Institutions||University of California, Berkeley|
|Thesis||The structure and flexibility of myoglobin : molecular dynamics and x-ray crystallography (1986)|
John Kuriyan is Chancellor's Professor at the University of California, Berkeley in the departments of Molecular and Cell Biology (MCB) and Chemistry. He is also a Faculty Scientist in Berkeley Lab's Physical Biosciences Division, a Howard Hughes Medical Institute investigator, and a member of the National Academy of Sciences.
Research and career
Kuriyan did postdoctoral research work for one year supervised by Karplus at Harvard before becoming an assistant professor at the Rockefeller University. As of 2015[update] Kuriyan's laboratory studies the structure and mechanism of enzymes and other proteins that transduce cellular signals and perform DNA replication. The laboratory primarily uses x-ray crystallography to determine 3-D protein structures as well as biochemical, biophysical, and computational techniques to uncover the mechanisms used by these proteins.
Awards and honors
In 1989, Kuriyan was named a Pew Scholar in the Biomedical Sciences, a program supporting promising young researchers in the areas of basic and clinical sciences relevant to human health advancements. Kuriyan was the recipient of the 2005 Loundsbery Award by the National Academy of Sciences, a recognition presented annually to a single scientific investigator, under the age of 45, who has made significant contributions to medicine or biology. Additional awards include the Cornelius Rhoads Memorial Award from the American Association for Cancer Research (1999), the Eli Lilly Award in Biological Chemistry of the American Chemical Society (1998), the Dupont-Merck Award of the Protein Society (1997), and the Schering-Plough Award of the American Society for Biochemistry and Molecular Biology (1994). In 2009 he received the ASBMB Merck award for his contributions to structural biology. Kuriyan was elected a Foreign Member of the Royal Society (ForMemRS) in 2015. He was elected to the National Academy of Medicine in 2018.
- The molecules of life: physical and chemical principles with Konforti, Boyana; Wemmer, David (2013)
- Mechanisms of RAS activation at the membrane (2006)
- Crystallographic R factor refinement by molecular dynamics
- Structural mechanism for STI-571 inhibition of abelson tyrosine kinase
- Multiple BCR-ABL kinase domain mutations confer polyclonal resistance to the tyrosine kinase inhibitor imatinib (STI571) in chronic phase and blast crisis chronic myeloid leukemia
- The conformational plasticity of protein kinases
- An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
- "John Kuriyan". www.nasonline.org.
- "John Kuriyan - Royal Society". royalsociety.org.
- Kuriyan, John (1986). The structure and flexibility of myoglobin: molecular dynamics and x-ray crystallography (Thesis). OCLC 15862419.
- "Richard Lounsbery Award". www.nasonline.org. Retrieved 2020-02-08.
- Journal of the National Cancer Institute: JNCI. U.S. Department of Health, Education, and Welfare, Public Health Service, National Institutes of Health. May 1999. p. 830.
- "National Academy of Medicine Elects 85 New Members". National Academy of Medicine. 15 October 2018. Retrieved 2 May 2019.
- Kuriyan, John; Konforti, Boyana; Wemmer, David (2013). The molecules of life: physical and chemical principles. ISBN 978-0-8153-4188-8. OCLC 779577263.
- Kuriyan, John; Harvard University; Department of Chemistry and Chemical Biology (2006), Mechanisms of RAS activation at the membrane, OCLC 232369650
- Brünger, Axel T.; Kuriyan, John; Karplus, Martin (1987-01-23). "Crystallographic R Factor Refinement by Molecular Dynamics". Science. 235 (4787): 458–460. Bibcode:1987Sci...235..458B. doi:10.1126/science.235.4787.458. ISSN 0036-8075. PMID 17810339.
- Schindler, T.; Bornmann, W.; Pellicena, P.; Miller, W. T.; Clarkson, B.; Kuriyan, J. (2000-09-15). "Structural mechanism for STI-571 inhibition of abelson tyrosine kinase". Science (New York, N.Y.). 289 (5486): 1938–1942. Bibcode:2000Sci...289.1938S. doi:10.1126/science.289.5486.1938. ISSN 0036-8075. PMID 10988075.
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