James J. Champoux (died 13 May 2019[1]) was an American microbiologist who worked at University of Washington[2] and an Elected Fellow of the American Association for the Advancement of Science.[3]

Education

He earned his B.S. at University of Washington and his Ph.D. at Stanford University.[4]

Research

His interests were retroviruses and topoisomerases[4] and his highest cited paper is DNA Topoisomerases: Structure, Function, and Mechanism[5] at 2260 times, according to Google Scholar.[6]

Publications

  • Effects of DNA and protein size on substrate cleavage by human tyrosyl-DNA phosphodiesterase 1. Interthal H, Champoux JJ The Biochemical Journal. 2011 Jun; 436 3: 559-66
  • Multiple nucleotide preferences determine cleavage-site recognition by the HIV-1 and M-MuLV RNases H. Schultz SJ, Zhang M, Champoux JJ Journal of Molecular Biology. 2010 Mar; 397 1: 161-78
  • Preferred sequences within a defined cleavage window specify DNA 3' end-directed cleavages by retroviral RNases H. Schultz SJ, Zhang M, Champoux JJ The Journal of Biological Chemistry. 2009 Nov; 284 47: 32225-38
  • Assays for the preferential binding of human topoisomerase I to supercoiled DNA. Yang Z, Champoux JJ Methods in Molecular Biology. 2009 ; 582 : 49-57
  • Mutational analysis of the preferential binding of human topoisomerase I to supercoiled DNA. Yang Z, Carey JF, Champoux JJ The FEBS journal. 2009 Oct; 276 20: 5906-19

References

  1. "Remembering Dr. James Champoux". University of Washington Honors Program. 22 May 2019. Retrieved 26 May 2019.
  2. "James Champoux Lab". washington.edu. Retrieved December 22, 2017.
  3. "AAAS Names 8 UW Researchers as Fellows in 2017". washington.edu. November 22, 2017. Retrieved December 22, 2017.
  4. 1 2 "James J. Champoux". washington.edu. Retrieved December 22, 2017.
  5. James J. Champoux. DNA Topoisomerases: Structure, Function, and Mechanism, Vol. 70:369-413 (Volume publication date July 2001). Annual review of Biochemistry
  6. "James Champoux". scholar.google.com. Retrieved February 24, 2018.
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