Charles Brenner

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Not to be confused with Charles Brenner (psychiatrist)
Charles Brenner
Born (1961-10-30)October 30, 1961
Residence Iowa City, IA
Nationality USA
Fields Enzymology
Metabolism
Institutions University of Iowa
Dartmouth Medical School
Thomas Jefferson University
Alma mater Wesleyan University (B.A.)
Stanford University (Ph.D)
Brandeis University (Post-Doctoral)
Thesis Specificity and Activity of the Kex2 Protease: From Yeast Genetics to Enzyme Kinetics (1993)
Doctoral advisor Robert S. Fuller
Other academic advisors Gregory A. Petsko
Dagmar Ringe
Doctoral students Shawn K. Milano
Peter Belenky
Katrina L. Bogan
Jennifer A. Boyston
Bo-Kuan Wu
Known for New steps in nicotinamide adenine dinucleotide metabolism
Influences Kunihiro Matsumoto
Arthur Kornberg
Notable awards William E.M. Lands Lectureship
Fellow of the American Association for the Advancement of Science
Beckman Young Investigators Award
Website
biochem.uiowa.edu/brenner

Charles Brenner born October 30, 1961 is the Roy J. Carver Chair of Biochemistry and a director of the Obesity Initiative at the University of Iowa. He is a graduate of Wesleyan University and a veteran of biotechnology companies, having worked at Chiron Corporation and DNAX Research Institute, prior to graduate school at Stanford University School of Medicine. Brenner conducted post-doctoral research at Brandeis University with Gregory Petsko and then took his first academic position at Thomas Jefferson University in 1996, moving to Dartmouth Medical School in 2003, where he served as Associate Director for Basic Sciences at Norris Cotton Cancer Center. He was recruited to chair biochemistry at Iowa in 2009.[1] In 2012, Brenner was asked by the President of the American Society for Biochemistry and Molecular Biology to develop new recommendations for the society for a pre-medical biochemistry curriculum that will be consistent with a revised MCAT examination.[2] These recommendations, which include development of inorganic, organic and biochemistry coursework that is more geared toward the chemistry of bioorganic functional groups, have been further refined in academic journals.[3][4]

Brenner has made multiple contributions to molecular biology and biochemistry, beginning with purification and characterization of the Kex2 proprotein convertase at Stanford.[5] He has been funded by agencies including the Leukemia & Lymphoma Society, the March of Dimes, the Burroughs Wellcome Fund, the Beckman Foundation, the Lung Cancer Research Foundation, the National Institutes of Health, and the National Science Foundation. Active research projects include molecular dissection of the function of the FHIT tumor suppressor gene,[6][7] characterization and inhibition of DNA methylation,[8][9][10] and discovery of new steps in nicotinamide adenine dinucleotide metabolism. Notably, the Brenner laboratory discovered that yeast and human enzymes use nicotinamide riboside to make NAD+,[11][12] for which Brenner was recognized with a William E.M. Lands lectureship at University of Michigan. This new form of B vitamin might have applications in preventing peripheral neuropathy.[13] Brenner is author of more than 100 publications and was the senior editor of the 2004 book, Oncogenomics: Molecular Approaches to Cancer.

Monograph[edit]

  • Charles Brenner and David Duggan (2004) Oncogenomics: Molecular Approaches to Cancer. John Wiley & Sons, Hoboken, NJ. ISBN 0-471-22592-4

References[edit]

  1. ^ Charles Brenner CV
  2. ^ Response to the new MCAT: ASBMB premedical curriculum recommendations ASBMB Today, March 2012
  3. ^ Brenner, C (2013). "Changes in Chemistry and Biochemistry Education: Creative Responses to MCAT Revisions in the Age of the Genome". Biochem. and Mol. Biol. Ed. 41 (1): 1–4. doi:10.1002/bmb.20653. PMID 23281187. 
  4. ^ Brenner, C (2013). "Rethinking Premedical and Health Professional Curricula in Light of MCAT 2015". J. Chem. Ed. 90 (7): 807–812. doi:10.1021/ed4002738. 
  5. ^ Brenner, C, Fuller, RS (1992). "Structural and Enzymatic Characterization of a Purified Prohormone-Processing Enzyme: Secreted, Soluble Kex2 Protease". Proc. Natl. Acad. Sci. 89 (3): 922–926. doi:10.1073/pnas.89.3.922. PMC 48357. PMID 1736307. 
  6. ^ Draganescu, A, Hodawadekar, SC, Gee, KR, Brenner, C (2000). "Fhit-Nucleotide Specificity Probed with Novel Fluorescent and Fluorogenic Substrates". J. Biol. Chem. 275 (7): 4555–4560. doi:10.1074/jbc.275.7.4555. PMC 2556043. PMID 10671479. 
  7. ^ Trapasso, F et al. (2003). "Designed FHIT Alleles Establish that Fhit-Induced Apoptosis in Cancer Cells is Limited by Substrate-Binding". Proc. Natl. Acad. Sci. 100 (4): 1592–1597. doi:10.1073/pnas.0437915100. PMC 149877. PMID 12574506. 
  8. ^ Syeda, F, Fagan, RL, Wean, M, Avvakumov, GV, Walker, JR, Xue, S, Dhe-Paganon S, Brenner, C (2011). "The Replication Focus Targeting Sequence (RFTS) Domain is a DNA-Competitive Inhibitor of Dnmt1". J. Biol. Chem. 286 (17): 15344–15351. doi:10.1074/jbc.M110.209882. PMC 3083197. PMID 21389349. 
  9. ^ Fagan, RL, Cryderman, DE, Kopelovich, L, Wallrath, LL, Brenner, C (2013). "Laccaic Acid A Is a Direct, DNA-competitive Inhibitor of DNA Methyltransferase 1". J. Biol. Chem. 288 (33): 23858–23867. doi:10.1074/jbc.M113.480517. PMID 23839987. 
  10. ^ Wu, B-K, Brenner, C (2014). "Suppression of TET1-Dependent DNA Demethylation Is Essential for KRAS-Mediated Transformation". Cell Reports 9. doi:10.1016/j.celrep.2014.10.063. 
  11. ^ Bieganowski, P, Brenner, C (2004). "Discoveries of Nicotinamide Riboside as a Nutrient and Conserved NRK Genes Establish a Preiss-Handler Independent Route to NAD+ in Fungi and Humans". Cell 117 (4): 495–502. doi:10.1016/S0092-8674(04)00416-7. PMID 15137942. 
  12. ^ Belenky, P et al. (2007). "Nicotinamide Riboside Promotes Sir2 Silencing and Extends Lifespan via Nrk and Urh1/Pnp1/Meu1 Pathways to NAD+". Cell 129 (3): 473–484. doi:10.1016/j.cell.2007.03.024. PMID 17482543. 
  13. ^ New Vitamin May Relieve a Painful Problem Focus April 20, 2008

External links[edit]