Charles Brenner, PhD

Portrait
Professor of Biochemistry
Professor of Internal Medicine

Contact Information

Primary Office
4-403 BSB
Iowa City, IA 52242
319-335-7934

Lab
4-339 BSB
Iowa City, IA 52242
319-384-4099

Fax
319-335-9570

Education

BA, Biology, Wesleyan University
PhD, Cancer Biology, Stanford University
Postdoctoral Fellow, Chemistry and Biochemistry (X-Ray Crystallography), Brandeis University

Education/Training Program Affiliations

Department of Biochemistry PhD, Interdisciplinary Graduate Program in Genetics, Interdisciplinary Graduate Program in Molecular Medicine, Interdisciplinary Graduate Program in Translational Biomedicine, Medical Scientist Training Program

Center, Program and Institute Affiliations

Center for Biocatalysis and Bioprocessing, Fraternal Order of Eagles Diabetes Research Center, Holden Comprehensive Cancer Center, Iowa Neuroscience Institute, UI Obesity Research and Education Initiative

Research Summary

Cellular function and differentiation depend on an ability to read environmental cues and to execute a gene expression program that is appropriate to time, place and context. Nutrient availability is among the most important signals to which cells respond. Importantly, nutrients are not only transmitted from outside an organism, i.e., by feeding, but are also transmitted from cell to cell and from tissue to tissue. Metabolic control of gene expression is critical to the maintenance of cellular longevity. Dysregulation of the nutritional control of gene expression underlies a series of conditions including nondetection of satiety, which can lead to obesity and diabetes, and diseases such as cancer. Our laboratory is engaged in several projects that dissect specific problems in the metabolic control of gene expression. In particular, we are interested in how changing environmental conditions lead to reversible transfer of two carbon, i.e. acetyl, and one carbon, i.e. methyl, groups to proteins and DNA, respectively. These processes are fundamentally important because two carbon transfers link carbohydrate and fat metabolism to nicotinamide adenine dinucleotide (NAD) biosynthesis and because one carbon transfers link the folate cycle and methionine biosynthesis to S-adenosyl methionine metabolism. Trainees in our group are engaged in interdisciplinary projects, performing protein purification, enzymology, structural biology, yeast and somatic cell genetics, genomics, and chemical biology.

Publications

Matasic, D. S., Brenner, C. & London, B. (2018). Emerging potential benefits of modulating NAD+ metabolism in cardiovascular disease. American journal of physiology. Heart and circulatory physiology, 314(4), H839-H852. PMID: 29351465.

Fangmann, D., Theismann, E. M., Türk, K., Schulte, D. M., Relling, I., Hartmann, K., Keppler, J. K., Knipp, J. R., Rehman, A., Heinsen, F. A., Franke, A., Lenk, L., Freitag-Wolf, S., Appel, E., Gorb, S., Brenner, C., Seegert, D., Waetzig, G. H., Rosenstiel, P., Schreiber, S., Schwarz, K. & Laudes, M. (2018). Targeted Microbiome Intervention by Microencapsulated Delayed-Release Niacin Beneficially Affects Insulin Sensitivity in Humans. Diabetes care, 41(3), 398-405. PMID: 29212824.

Diguet, N., Trammell SAJ,, Tannous, C., Deloux, R., Piquereau, J., Mougenot, N., Gouge, A., Gressette, M., Manoury, B., Blanc, J., Breton, M., Decaux, J. F., Lavery, G., Baczkó, I., Zoll, J., Garnier, A., Li, Z., Brenner, C. & Mericskay, M. (2017). Nicotinamide Riboside Preserves Cardiac Function in a Mouse Model of Dilated Cardiomyopathy. Circulation. PMID: 29217642.

Vaur, P., Brugg, B., Mericskay, M., Li, Z., Schmidt, M. S., Vivien, D., Orset, C., Jacotot, E., Brenner, C. & Duplus, E. (2017). Nicotinamide riboside, a form of vitamin B3, protects against excitotoxicity-induced axonal degeneration. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 31(12), 5440-5452. PMID: 28842432.

Thakur, S., Brenner, C. (2017). KRAS-driven miR-29b expression is required for tumor suppressor gene silencing. Oncotarget, 8(43), 74755-74766. PMID: 29088821.

Sato, S., Solanas, G., Peixoto, F. O., Bee, L., Symeonidi, A., Schmidt, M. S., Brenner, C., Masri, S., Benitah, S. A. & Sassone-Corsi, P. (2017). Circadian Reprogramming in the Liver Identifies Metabolic Pathways of Aging. Cell, 170(4), 664-677.e11. PMID: 28802039.

Wilsbacher, J. L., Cheng, M., Cheng, D., Trammell SAJ,, Shi, Y., Guo, J., Koeniger, S. L., Kovar, P. J., He, Y., Selvaraju, S., Heyman, H. R., Sorensen, B. K., Clark, R. F., Hansen, T. M., Longenecker, K. L., Raich, D., Korepanova, A. V., Cepa, S., Towne, D. L., Abraham, V. C., Tang, H., Richardson, P. L., McLoughlin, S. M., Badagnani, I., Curtin, M. L., Michaelides, M. R., Maag, D., Buchanan, F. G., Chiang, G. G., Gao, W., Rosenberg, S. H., Brenner, C. & Tse, C. (2017). Discovery and Characterization of Novel Nonsubstrate and Substrate NAMPT Inhibitors. Molecular cancer therapeutics, 16(7), 1236-1245. PMID: 28468779.

Fletcher, R. S., Ratajczak, J., Doig, C. L., Oakey, L. A., Callingham, R., Da Silva Xavier, G., Garten, A., Elhassan, Y. S., Redpath, P., Migaud, M. E., Philp, A., Brenner, C., Canto, C. & Lavery, G. G. (2017). Nicotinamide riboside kinases display redundancy in mediating nicotinamide mononucleotide and nicotinamide riboside metabolism in skeletal muscle cells. Molecular metabolism, 6(8), 819-832. PMID: 28752046.

Hamity, M. V., White, S. R., Walder, R. Y., Schmidt, M. S., Brenner, C. & Hammond, D. L. (2017). Nicotinamide riboside, a form of vitamin B3 and NAD+ precursor, relieves the nociceptive and aversive dimensions of paclitaxel-induced peripheral neuropathy in female rats. Pain, 158(5), 962-972. PMID: 28346814.

Ratajczak, J., Joffraud, M., Trammell, S. A., Ras, R., Canela, N., Boutant, M., Kulkarni, S. S., Rodrigues, M., Redpath, P., Migaud, M. E., Auwerx, J., Yanes, O., Brenner, C. & Cantó, C. (2016). NRK1 controls nicotinamide mononucleotide and nicotinamide riboside metabolism in mammalian cells. Nature communications, 7, 13103. PMID: 27725675.

Trammell, S. A., Schmidt, M. S., Weidemann, B. J., Redpath, P., Jaksch, F., Dellinger, R. W., Li, Z., Abel, E. D., Migaud, M. E. & Brenner, C. (2016). Nicotinamide riboside is uniquely and orally bioavailable in mice and humans. Nature communications, 7, 12948. PMID: 27721479.

Trammell, S. A., Weidemann, B. J., Chadda, A., Yorek, M. S., Holmes, A., Coppey, L. J., Obrosov, A., Kardon, R. H., Yorek, M. A. & Brenner, C. (2016). Nicotinamide Riboside Opposes Type 2 Diabetes and Neuropathy in Mice. Scientific reports, 6, 26933. PMID: 27230286.

Trammell, S. A., Yu, L., Redpath, P., Migaud, M. E. & Brenner, C. (2016). Nicotinamide Riboside Is a Major NAD+ Precursor Vitamin in Cow Milk. The Journal of nutrition, 146(5), 957-63. PMID: 27052539.

Mei, S., Brenner, C. (2015). Calorie restriction-mediated replicative lifespan extension in yeast is non-cell autonomous. PLoS Biol, 13(1), e1002048. PMID: 25633578.

Trammell, S. A., Brenner, C. (2015). NNMT: A Bad Actor in Fat Makes Good in Liver. Cell Metabolism, 22, 200-201. DOI: 10.1016/j.cmet.2015.07.017.

Boylston, J. A., Brenner, C. (2014). A Knockdown with Smoke Model Reveals Fhit as a Repressor of Heme Oxygenase 1. (Vols. 13). pp. 2913-30. Cell Cycle. DOI: 10.4161/15384101.2014.946858.

Brenner, C. (2014). Boosting NAD to Spare Hearing. Cell Metabolism, 21, 926-927. PMID: 25470539.

Brenner, C. (2014). Histidine Triad Superfamily (version 2.0). John Wiley & Sons Ltd (Eds.) Chichester: Encyclopedia of Life Sciences. DOI: 10.1002/9780470015902.a0020545.pub2.

Brenner, C. (2014). Metabolism: Targeting a fat-accumulation gene. Nature, 508, 194-195. PMID: 24717510.

Mei, S., Brenner, C. (2014). Quantification of Protein Copy Number in Yeast: the NAD+ Metabolome. PLoS One, 9, e106496. PMID: 25188219.

Wu, B., Mei, S. & Brenner, C. (2014). RFTS-deleted DNMT1 enhances tumorigenicity with focal hypermethylation and global hypomethylation. Cell Cycle, 13. DOI: 10.4161/15384101.2014.950886.

Huang, J., Stewart, A., Maity, B., Hagen, J., Fagan, R., Yang, J., Quelle, D., Brenner, C. & Fisher, R. (2014). RGS6 Suppresses Ras-induced Cellular Transformation by Facilitating Tip60-mediated Dnmt1 Degradation and Promoting Apoptosis. Oncogene, 33(27), 3604-11. PMID: 23995786.

Wu, B. K., Brenner, C. (2014). Suppression of TET1-Dependent DNA Demethylation is Essential for KRAS-Mediated Transformation. Cell Reports, 9, 1827-1840. PMID: 25466250.

Brenner, C. (2014). Understanding faculty salaries. ASBMB Today, 13, 28-29.

Fagan, R. L., Wu, M., Chedin, F. & Brenner, C. (2013). An ultrasensitive high throughput screen for DNA methyltransferase 1-targeted molecular probes. PLoS One, 8(11), e78752. PMID: 24236046.

Mei, S. C., Brenner, C. (2013). NAD as a Genotype-Specific Drug Target. Chem Biol, 20(11), 1307-8. PMID: 24267273.

Kennelly, P. J., Bond, J. S., Masters, B. S., Brenner, C. & Raben, D. M. (2013). Desperately seeking Flexner: time to reemphasize basic science in medical education. Acad Med, 88(10), 1405-6. PMID: 24064614.

Fagan, R. L., Cryderman, D. E., Kopelovich, L., Wallrath, L. L. & Brenner, C. (2013). Laccaic Acid A is a Direct, DNA-Competitive Inhibitor of DNA Methyltransferase 1. The Journal of biological chemistry, 228, 23858-23867. PMID: 23839987.

Bogan, K. L., Brenner, C. (2013). Biochemistry: Niacin and NAD(P). W. J. Lennarz , M. D. Lane (Eds.) pp. 172-178. Encyclopedia of Biological Chemistry.

Brenner, C. (2013). Changes in chemistry and biochemistry education: creative responses to medical college admissions test revisions in the age of the genome. Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology, 41(1), 1-4. PMID: 23281187.

Brenner, C. (2013). Demystifying the Chalk Talk. ASBMB Today, 12(8), 33-35.

Ghanta, S., Grossmann, R. E. & Brenner, C. M. (2013). Mitochondrial protein acetylation as a cell-intrinsic, evolutionary driver of fat storage: chemical and metabolic logic of acetyl-lysine modifications. (Vols. 48). pp. 561-574. Critical Rev Biochem & Mol Biol. PMID: 24050258.

Brenner, C. (2013). Rethinking Premedical and Health Professional Curricula in Light of MCAT 2015. Journal of Chemical Education.

Trammell, S., Brenner, C. (2013). Targeted, LCMC-based Metabolomics for Quantitative Measurement of NAD+ Metabolites. Computational and Structural Biotechnology Journal, 4, e201301012. PMID: 24688693.

Midtkandal, R. R., Redpath, P., Trammell, S. A., Macdonald, S. J., Brenner, C. & Migaud, M. E. (2012). Novel synthetic route to the C-nucleoside, 2-deoxy benzamide riboside. Bioorganic & medicinal chemistry letters, 22(16), 5204-7. PMID: 22795628.

Brenner, C., Ringe, D. (2012). Response to the New MCAT: ASBMB Premedical Curriculum. pp. 12-14. ASBMB Today.

Boylston, J., Brenner, C. (2012). Fhit. S. Choi (Eds.) pp. chapter 68, part 7, 613-616. Encyclopedia of Signaling Molecules.

Syeda, F., Fagan, R. L., Wean, M., Avvakumov, G. V., Walker, J. R., Xue, S., Dhe-Paganon, S. & Brenner, C. (2011). The replication focus targeting sequence (RFTS) domain is a DNA-competitive inhibitor of Dnmt1. The Journal of biological chemistry, 286(17), 15344-51. PMID: 21389349.

Belenky, P., Stebbins, R., Bogan, K. L., Evans, C. R. & Brenner, C. (2011). Nrt1 and Tna1-independent export of NAD+ precursor vitamins promotes NAD+ homeostasis and allows engineering of vitamin production. PloS one, 6(5), e19710. PMID: 21589930.

Bogan, K. L., Brenner, C. (2010). 5'-Nucleotidases and their New Roles in NAD+ and Phosphate Metabolism. New Journal of Chemistry, 34, 845-853.

Evans, C., Bogan, K. L., Song, P., Burant, C. F., Kennedy, R. T. & Brenner, C. (2010). NAD+ metabolite levels as a function of vitamins and calorie restriction: evidence for different mechanisms of longevity. BMC chemical biology, 10, 2. PMID: 20175898.

Bogan, K. L., Evans, C., Belenky, P., Song, P., Burant, C. F., Kennedy, R. & Brenner, C. (2009). Identification of Isn1 and Sdt1 as glucose- and vitamin-regulated nicotinamide mononucleotide and nicotinic acid mononucleotide [corrected] 5'-nucleotidases responsible for production of nicotinamide riboside and nicotinic acid riboside. The Journal of biological chemistry, 284(50), 34861-9. PMID: 19846558.

Gazzaniga, F., Stebbins, R., Chang, S. Z., McPeek, M. A. & Brenner, C. (2009). Microbial NAD metabolism: lessons from comparative genomics. Microbiology and molecular biology reviews : MMBR, 73(3), 529-41, Table of Contents. PMID: 19721089.

Belenky, P., Christensen, K. C., Gazzaniga, F., Pletnev, A. A. & Brenner, C. (2009). Nicotinamide riboside and nicotinic acid riboside salvage in fungi and mammals. Quantitative basis for Urh1 and purine nucleoside phosphorylase function in NAD+ metabolism. The Journal of biological chemistry, 284(1), 158-64. PMID: 19001417.

Brooks, L., Heimsath, E. G., Loring, G. L. & Brenner, C. (2008). FHA-RING ubiquitin ligases in cell division cycle control. pp. 3458-66 + cover. Cellular and molecular life sciences : CMLS. PMID: 18597043.

Linster, C. L., Adler, L. N., Webb, K., Christensen, K. C., Brenner, C. & Clarke, S. G. (2008). A second GDP-L-galactose phosphorylase in arabidopsis en route to vitamin C. Covalent intermediate and substrate requirements for the conserved reaction. The Journal of biological chemistry, 283(27), 18483-92. PMID: 18463094.

Belenky, P. A., Moga, T. G. & Brenner, C. (2008). Saccharomyces cerevisiae YOR071C encodes the high affinity nicotinamide riboside transporter Nrt1. The Journal of biological chemistry, 283(13), 8075-9. PMID: 18258590.

Fuller, R. S., Bambara, R. A., Baker, T., Funnell, B., Wahle, E., O'Donnell, M., Kaiser, A., Skarstad, K., Konforti, B., Maki, S., Katayama, T., Sekimizu, K., Weiner, J. H., Davis, R. W., Rowen, L., Goodman, M. F., Spudich, J., Pfeffer, S., Richardson, C. C., Polaczek, P., Calendar, R., Kolodner, R., Griffith, J., Stillman, B., Modrich, P., Brenner, C. & Yanofsky, C. (2008). A Tribute to Arthur Kornberg, 1918-2007. pp. 2-17. Nature Structural and Molecular Biology.

Bogan, K. L., Brenner, C. (2008). Nicotinic acid, nicotinamide, and nicotinamide riboside: a molecular evaluation of NAD+ precursor vitamins in human nutrition. Annual review of nutrition, 28, 115-30. PMID: 18429699.

Loring, G. L., Christensen, K. C., Gerber, S. A. & Brenner, C. (2008). Yeast Chfr homologs retard cell cycle at G1 and G2/M via Ubc4 and Ubc13/Mms2-dependent ubiquitination. Cell cycle (Georgetown, Tex.), 7(1), 96-105. PMID: 18202552.

Tempel, W., Rabeh, W. M., Bogan, K. L., Belenky, P., Wojcik, M., Seidle, H. F., Nedyalkova, L., Yang, T., Sauve, A. A., Park, H. W. & Brenner, C. (2007). Nicotinamide riboside kinase structures reveal new pathways to NAD+. PLoS biology, 5(10), e263. PMID: 17914902.

Linster, C. L., Gomez, T. A., Christensen, K. C., Adler, L. N., Young, B. D., Brenner, C. & Clarke, S. G. (2007). Arabidopsis VTC2 encodes a GDP-L-galactose phosphorylase, the last unknown enzyme in the Smirnoff-Wheeler pathway to ascorbic acid in plants. The Journal of biological chemistry, 282(26), 18879-85. PMID: 17462988.

Belenky, P., Racette, F. G., Bogan, K. L., McClure, J. M., Smith, J. S. & Brenner, C. (2007). Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+. Cell, 129(3), 473-84. PMID: 17482543.

Robu, M. E., Larson, J. D., Nasevicius, A., Beiraghi, S., Brenner, C., Farber, S. A. & Ekker, S. C. (2007). p53 activation by knockdown technologies. PLoS genetics, 3(5), e78. PMID: 17530925.

Brenner, C. (2007). Histidine Triad Superfamily. M. Cox (Eds.) pp. article a0020545. Encyclopedia of Life Sciences.

Belenky, P., Bogan, K. L. & Brenner, C. (2007). NAD+ metabolism in health and disease. Trends in biochemical sciences, 32(1), 12-19. PMID: 17161604.

Wojcik, M., Seidle, H. F., Bieganowski, P. & Brenner, C. (2006). Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste. The Journal of biological chemistry, 281(44), 33395-402. PMID: 16954203.

Parsons, A. B., Lopez, A., Givoni, I. E., Williams, D. E., Gray, C. A., Porter, J., Chua, G., Sopko, R., Brost, R. L., Ho, C. H., Wang, J., Ketela, T., Brenner, C., Brill, J. A., Fernandez, G. E., Lorenz, T. C., Payne, G. S., Ishihara, S., Ohya, Y., Andrews, B., Hughes, T. R., Frey, B. J., Graham, T. R., Andersen, R. J. & Boone, C. (2006). Exploring the mode-of-action of bioactive compounds by chemical-genetic profiling in yeast. Cell, 126(3), 611-25. PMID: 16901791.

Bieganowski, P., Seidle, H. F., Wojcik, M. & Brenner, C. (2006). Synthetic lethal and biochemical analyses of NAD and NADH kinases in Saccharomyces cerevisiae establish separation of cellular functions. The Journal of biological chemistry, 281(32), 22439-45. PMID: 16760478.

Martin, J., Magnino, F., Schmidt, K., Piguet, A. C., Lee, J. S., Semela, D., St-Pierre, M. V., Ziemiecki, A., Cassio, D., Brenner, C., Thorgeirsson, S. S. & Dufour, J. F. (2006). Hint2, a mitochondrial apoptotic sensitizer down-regulated in hepatocellular carcinoma. Gastroenterology, 130(7), 2179-88. PMID: 16762638.

Milano, S. K., Kim, Y. M., Stefano, F. P., Benovic, J. L. & Brenner, C. (2006). Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding. The Journal of biological chemistry, 281(14), 9812-23. PMID: 16439357.

Brenner, C. (2005). Evolution of NAD biosynthetic enzymes. (9), pp. 1239-40. Structure (London, England : 1993). PMID: 16154080.

Seidle, H. F., Bieganowski, P. & Brenner, C. (2005). Disease-associated mutations inactivate AMP-lysine hydrolase activity of Aprataxin. The Journal of biological chemistry, 280(22), 20927-31. PMID: 15790557.

Chou, T. F., Bieganowski, P., Shilinski, K., Cheng, J., Brenner, C. & Wagner, C. R. (2005). 31P NMR and genetic analysis establish hinT as the only Escherchia coli purine nucleoside phosphoramidase and as essential for growth under high salt conditions. The Journal of biological chemistry, 280(15), 15356-61. PMID: 15703176.

Parks, K. P., Seidle, H., Wright, N., Sperry, J. B., Bieganowski, P., Howitz, K., Wright, D. L. & Brenner, C. (2004). Altered specificity of Hint-W123Q supports a role for Hint inhibition by ASW in avian sex determination. Physiological genomics, 20(1), 12-14. PMID: 15507519.

Clements, P. M., Breslin, C., Deeks, E. D., Byrd, P. J., Ju, L., Bieganowski, P., Brenner, C., Moreira, M. C., Taylor, A. M. & Caldecott, K. W. (2004). The ataxia-oculomotor apraxia 1 gene product has a role distinct from ATM and interacts with the DNA strand break repair proteins XRCC1 and XRCC4. DNA repair, 3(11), 1493-502. PMID: 15380105.

Bieganowski, P., Shilinski, K., Tsichlis, P. N. & Brenner, C. (2004). Cdc123 and checkpoint forkhead associated with RING proteins control the cell cycle by controlling eIF2gamma abundance. The Journal of biological chemistry, 279(43), 44656-66. PMID: 15319434.

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. PMID: 15137942.

Krakowiak, A., Pace, H. C., Blackburn, G. M., Adams, M., Mekhalfia, A., Kaczmarek, R., Baraniak, J., Stec, W. J. & Brenner, C. (2004). Biochemical, crystallographic, and mutagenic characterization of hint, the AMP-lysine hydrolase, with novel substrates and inhibitors. The Journal of biological chemistry, 279(18), 18711-6. PMID: 14982931.

Maiolatesi, T. M., Brenner, C. (2004). Chemical and Genetic Methods to Validate Drug Targets in Nonmammalian Organisms. C. Brenner , D. Duggan , J. Wiley , N. Y. Sons (Eds.) pp. Chapter 10. Oncogenomics: Molecular Approaches to Cancer.

Brenner, C. (2004). Chemical genomics in yeast. (9), pp. 240. Genome biology. PMID: 15345040.

Brenner, C. (2004). Oncogenomics: Molecular Approaches to Cancer.

Brenner, C. (2004). Precariously on the Cusp of Oncogenomics. J. Wiley , N. Y. Sons (Eds.) pp. Chapter 1. Oncogenomics: Molecular Approaches to Cancer.

Kwasnicka, D. A., Krakowiak, A., Thacker, C., Brenner, C. & Vincent, S. R. (2003). Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and Hint-related 7meGMP-directed hydrolase, DCS-1. The Journal of biological chemistry, 278(40), 39051-8. PMID: 12871939.

Brenner, C. (2003). Subtleties among subtilases. The structural biology of Kex2 and furin-related prohormone convertases. EMBO reports, 4(10), 937-8. PMID: 14528262.

Bieganowski, P., Pace, H. C. & Brenner, C. (2003). Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase. The Journal of biological chemistry, 278(35), 33049-55. PMID: 12771147.

Bieganowski, P., Brenner, C. (2003). The reported human NADsyn2 is ammonia-dependent NAD synthetase from a pseudomonad. The Journal of biological chemistry, 278(35), 33056-9. PMID: 12777395.

Trapasso, F., Krakowiak, A., Cesari, R., Arkles, J., Yendamuri, S., Ishii, H., Vecchione, A., Kuroki, T., Bieganowski, P., Pace, H. C., Huebner, K., Croce, C. M. & Brenner, C. (2003). Designed FHIT alleles establish that Fhit-induced apoptosis in cancer cells is limited by substrate binding. Proceedings of the National Academy of Sciences of the United States of America, 100(4), 1592-7. PMID: 12574506.

Pace, H. C., Brenner, C. (2003). Feminizing chicks: a model for avian sex determination based on titration of Hint enzyme activity and the predicted structure of an Asw-Hint heterodimer. Genome biology, 4(3), R18. PMID: 12620103.

Owczarek, A., Kaczmarek, R., MikoÅ?ajczyk, B., Wasilewska, E., KorczyÅ?ski, D., Baraniak, J., KozioÅ?kiewicz, M., Stec, W. J. & Brenner, C. (2003). Stereochemical analysis of diastereomeric 1,3-bis(adenosine-5'-O-phosphorothioyl)glycerols. (8-May), pp. 797-9. Nucleosides, nucleotides & nucleic acids. PMID: 14565281.

Brenner, C. (2002). Catalysis in the nitrilase superfamily. Current opinion in structural biology, 12(6), 775-82. PMID: 12504683.

Brenner, C. (2002). Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. Biochemistry, 41(29), 9003-14. PMID: 12119013.

Rubio-Texeira, M., Varnum, J. M., Bieganowski, P. & Brenner, C. (2002). Control of dinucleoside polyphosphates by the FHIT-homologous HNT2 gene, adenine biosynthesis and heat shock in Saccharomyces cerevisiae. BMC molecular biology, 3, 7. PMID: 12028594.

Bieganowski, P., Garrison, P. N., Hodawadekar, S. C., Faye, G., Barnes, L. D. & Brenner, C. (2002). Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3. The Journal of biological chemistry, 277(13), 10852-60. PMID: 11805111.

Milano, S. K., Pace, H. C., Kim, Y. M., Brenner, C. & Benovic, J. (2002). Scaffolding Functions of Arrestin-2 Revealed by Crystal Structure and Mutagenesis. Biochemistry, 41, 3321-3328.

Dahéron, L., Zenz, T., Siracusa, L. D., Brenner, C. & Calabretta, B. (2001). Molecular cloning of Ian4: a BCR/ABL-induced gene that encodes an outer membrane mitochondrial protein with GTP-binding activity. Nucleic acids research, 29(6), 1308-16. PMID: 11238997.

Pace, H. C., Brenner, C. (2001). Crystal structure of the worm NitFhit Rosetta Stone protein reveals a Nit tetramer binding two Fhit dimers. National Synchrontron Light Source 2000 Activity Report, 213-216.

Varnum, J. M., Baraniak, J., Kaczmarek, R., Stec, W. J. & Brenner, C. (2001). Di-, tri- and tetra-5'-O-phosphorothioadenosyl substituted polyols as inhibitors of Fhit: Importance of the alpha-beta bridging oxygen and beta phosphorus replacement. BMC chemical biology, 1(1), 3. PMID: 11701096.

Brenner, C. (2001). FHIT. T. E. Creighton (Eds.) pp. 1274-1275. Wiley Encyclopedia of Molecular Medicine.

Brenner, C. (2001). Public Sector Research as an Engine of Growth. pp. 22. Technology Times.

McLennan, A. G., Barnes, L. D., Blackburn, G. M., Brenner, C., Guranowski, A., Miller, A. D., Rovira, J. M., Rotllan, P., Soria, B., Tanner, J. A. & Sillero, A. (2001). Recent Progress in the Study of the Intracellular Functions of Diadenosine Polyphosphates. pp. 249-259. Drug Development Research.

Pace, H. C., Brenner, C. (2001). The nitrilase superfamily: classification, structure and function. Genome biology, 2(1), 0001.1-0001.9. PMID: 11380987.

Boyne, J. R., Yosuf, H. M., Bieganowski, P., Brenner, C. & Price, C. (2000). Yeast myosin light chain, Mlc1p, interacts with both IQGAP and class II myosin to effect cytokinesis. Journal of cell science, 113 Pt 24, 4533-43. PMID: 11082046.

Brenner, C. (2000). Condensing the RNA world. (10), pp. 486. Trends in biochemical sciences. PMID: 11050431.

Draganescu, A., Hodawadekar, S. C., Gee, K. R. & Brenner, C. (2000). Fhit-nucleotide specificity probed with novel fluorescent and fluorogenic substrates. The Journal of biological chemistry, 275(7), 4555-60. PMID: 10671479.

Brenner, C. (2000). A Cultivated Taste for Yeast. pp. 103.1-103.4. Genome Biology.

Pace, H. C., Hodawadekar, S. C., Draganescu, A., Huang, J., Bieganowski, P., Pekarsky, Y., Croce, C. M. & Brenner, C. (2000). Crystal structure of the worm NitFhit Rosetta Stone protein reveals a Nit tetramer binding two Fhit dimers. (15), pp. 907-17. Current biology : CB. PMID: 10959838.

Brenner, C. (2000). Fhitness and Cancer in the Mouse. pp. 294. Trends in Genetics.

Brenner, C., Bieganowski, P., Pace, H. C. & Huebner, K. (1999). The histidine triad superfamily of nucleotide-binding proteins. Journal of cellular physiology, 181(2), 179-87. PMID: 10497298.

Fernandes, M. J., Finnegan, A. A., Siracusa, L. D., Brenner, C., Iscove, N. N. & Calabretta, B. (1999). Characterization of a novel receptor that maps near the natural killer gene complex: demonstration of carbohydrate binding and expression in hematopoietic cells. Cancer research, 59(11), 2709-17. PMID: 10363996.

Huebner, K., Sozzi, G., Brenner, C., Pierotti, M. A. & Croce, C. M. (1999). Fhit Loss in Lung Cancer: Diagnostic and Therapeutic Implications. pp. 3-10 + cover. Advances in Oncology.

Brenner, C. (1999). Fhit-Substrate Complexes: A New Paradigm in Reversible Protein Phosphorylation. pp. 749-752. Phosphorous, Sulfur, and Silicon.

Bevan, A., Brenner, C. & Fuller, R. S. (1998). Quantitative assessment of enzyme specificity in vivo: P2 recognition by Kex2 protease defined in a genetic system. Proceedings of the National Academy of Sciences of the United States of America, 95(18), 10384-9. PMID: 9724712.

Pekarsky, Y., Campiglio, M., Siprashvili, Z., Druck, T., Sedkov, Y., Tillib, S., Draganescu, A., Wermuth, P., Rothman, J. H., Huebner, K., Buchberg, A. M., Mazo, A., Brenner, C. & Croce, C. M. (1998). Nitrilase and Fhit homologs are encoded as fusion proteins in Drosophila melanogaster and Caenorhabditis elegans. Proceedings of the National Academy of Sciences of the United States of America, 95(15), 8744-9. PMID: 9671749.

Pace, H. C., Garrison, P. N., Robinson, A. K., Barnes, L. D., Draganescu, A., Rösler, A., Blackburn, G. M., Siprashvili, Z., Croce, C. M., Huebner, K. & Brenner, C. (1998). Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit. Proceedings of the National Academy of Sciences of the United States of America, 95(10), 5484-9. PMID: 9576908.

Blackburn, G. M., Liu, X., Rosler, A. & Brenner, C. (1998). Two hydrolase resistant analogues of diadenosine 5',5"'-P1,P3-triphosphate for studies with Fhit, the human fragile histidine triad protein. Nucleosides & nucleotides, 17(3-Jan), 301-8. PMID: 9708352.

Brenner, C., Pace, H. C., Garrison, P. N., Robinson, A. K., Rosler, A., Liu, X. H., Blackburn, G. M., Croce, C. M., Huebner, K. & Barnes, L. D. (1997). Purification and crystallization of complexes modeling the active state of the fragile histidine triad protein. Protein engineering, 10(12), 1461-3. PMID: 9543008.

Brenner, C., Garrison, P., Gilmour, J., Peisach, D., Ringe, D., Petsko, G. A. & Lowenstein, J. M. (1997). Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Nature structural biology, 4(3), 231-8. PMID: 9164465.

Diefenbach-Jagger, H., Brenner, C., Kemp, B. E., Baron, W., McLean, J., Martin, T. J. & Moseley, J. M. (1995). Arg21 is the preferred kexin cleavage site in parathyroid-hormone-related protein. European journal of biochemistry / FEBS, 229(1), 91-8. PMID: 7744054.

Brenner, C., Bevan, A. & Fuller, R. S. (1994). Methods for Analyzing the Specificity and Activity of a Prohormone-Processing Enzyme, the Yeast Kex2 Protease (Kexin). pp. 152-167. Meth. Enz.

Brenner, C. (1994). Reducing the Energy Barrier to Crystallization. pp. 2471-2472. Protein Science.

Brenner, C., Bevan, A. & Fuller, R. S. (1993). One-step site-directed mutagenesis of the Kex2 protease oxyanion hole. Current biology : CB, 3(8), 498-506. PMID: 15335687.

Angliker, H., Wikstrom, P., Shaw, E., Brenner, C. & Fuller, R. S. (1993). The synthesis of inhibitors for processing proteinases and their action on the Kex2 proteinase of yeast. The Biochemical journal, 293 ( Pt 1), 75-81. PMID: 8328974.

Brenner, C., Fuller, R. S. (1992). Structural and Enzymatic Characterization of a Purified Prohormone-Processing Enzyme: Secreted, Soluble Kex2 Protease. Proc. Natl. Acad. Sci., 89, 922-926.

Fuller, R. S., Brenner, C., Gluschankof, P. & Wilcox, C. (1991). The Yeast Prohormone-Processing Kex2 Protease, an Enzyme with Specificity for Paired Basic Residues. H. Jörnvall , J. Höög , A. Gustavsson (Eds.) pp. 205-214. Methods in Protein Sequence Analysis.

Brenner, C., Nakayama, N., Goebl, M., Tanaka, K., Toh-e, A. & Matsumoto, K. (1988). CDC33 encodes mRNA cap-binding protein eIF-4E of Saccharomyces cerevisiae. Molecular and cellular biology, 8(8), 3556-3559. PMID: 3062383.

Matsumoto, K., Nakafuku, M., Nakayama, N., Miyajima, I., Kaibuchi, K., Miyajima, A., Brenner, C., Arai, K. & Kaziro, Y. (1988). The role of G proteins in yeast signal transduction. pp. 567-75. Cold Spring Harbor symposia on quantitative biology. PMID: 2855496.

Miyajima, I., Nakafuku, M., Nakayama, N., Brenner, C., Miyajima, A., Kaibuchi, K., Arai, K., Kaziro, Y. & Matsumoto, K. (1987). GPA1, a haploid-specific essential gene, encodes a yeast homolog of mammalian G protein which may be involved in mating factor signal transduction. Cell, 50(7), 1011-1019. PMID: 3113739.

Brake, A., Brenner, C., Najarian, R., Laybourn, P. & Merryweather, J. (1985). Structure of Genes Encoding Precursors of the Yeast Peptide Mating Pheromone a-Factor. M. J. Gething (Eds.) pp. 103-108. Protein Transport and Secretion.