Charles Brenner

Charles Brenner
Not to be confused with Charles Brenner (psychiatrist)

Charles Brenner born October 30, 1961 is the Roy J. Carver Chair and head 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 Iowa in 2009.[1]

Brenner has made multiple contributions to molecular biology, beginning with purification and characterization of the Kex2 proprotein convertase at Stanford.[2] 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,[3][4] characterization of DNA methyltransferase Dnmt1,[5] 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+,[6][7] for which Brenner was recognized with a William E.M. Lands lectureship at University of Michigan. Brenner is author of more than 80 publications and the senior editor of the 2004 book, Oncogenomics: Molecular Approaches to Cancer.


  • Charles Brenner and David Duggan (2004) Oncogenomics: Molecular Approaches to Cancer. John Wiley & Sons, Hoboken, NJ. ISBN 0471225924


  1. ^ Charles Brenner CV
  2. ^ 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. 
  3. ^ 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. 
  4. ^ 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. 
  5. ^ 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. PMC 3083197. PMID 21389349. 
  6. ^ 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. 
  7. ^ 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. 

External links

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