John Kuriyan
Appearance
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John Kuriyan | |
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![]() John Kuriyan in 2015, portrait via the Royal Society | |
Alma mater |
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Awards |
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Scientific career | |
Institutions | Vanderbilt University School of Medicine |
Thesis | The structure and flexibility of myoglobin : molecular dynamics and x-ray crystallography (1986) |
Doctoral advisor | |
Website |
John Kuriyan is the dean of basic sciences and a professor of biochemistry at
National Academy of Sciences[1] and he has also been on the Life Sciences jury for the Infosys Prize in 2009, 2019 and 2020.[3]
Education
Kuriyan received his B.S. in chemistry from Juniata College in Pennsylvania, followed by his PhD in physical chemistry at the Massachusetts Institute of Technology supervised by Gregory Petsko and Martin Karplus.[4]
Research and career
![]() | This section of a biography of a living person does not include any references or sources. (May 2022) |
Kuriyan did
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
![](http://upload.wikimedia.org/wikipedia/commons/thumb/4/4e/John_Kuriyan.jpg/220px-John_Kuriyan.jpg)
In 1989, Kuriyan was named a
Foreign Member of the Royal Society (ForMemRS) in 2015.[2]
He was elected to the National Academy of Medicine in 2018.[7]
Books
- The molecules of life: physical and chemical principles with Konforti, Boyana; Wemmer, David (2013)[8]
- Mechanisms of RAS activation at the membrane (2006)[9]
Publications
![]() | This section of a poorly sourced must be removed immediately from the article and its talk page, especially if potentially libelous. )Find sources: "John Kuriyan" – news · newspapers · books · scholar · JSTOR (May 2022) |
- Crystallographic R factor refinement by molecular dynamics[10]
- Structural mechanism for STI-571 inhibition of abelson tyrosine kinase[11]
- 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
References
- ^ a b "John Kuriyan". www.nasonline.org.
- ^ a b "John Kuriyan - Royal Society". royalsociety.org.
- ^ "Infosys Prize - Jury 2020". www.infosys-science-foundation.com. Retrieved 2020-12-10.
- 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.
- OCLC 779577263.
- OCLC 232369650
- S2CID 38261757.
- PMID 10988075.