Scholars@Duke

• Background
• 

  Education, Training, & Certifications

  • Ph.D., University of Wisconsin - Madison 1984
• 

  Duke Appointment History

  • Consulting Professor in the Department of Biochemistry, Biochemistry, Basic Science Departments 2011
• Recognition
• 

  In the News

  • NOV 19, 2020

    Researchers Peer Inside Deadly Pathogen’s Burglary Kit

  • SEP 21, 2018

    School of Medicine News Blog

    Basic Science Day Showcases Wide Spectrum of Discovery Research at Duke

  • SEP 6, 2017

    Molecular Map Shows How to Disable Dangerous Bioweapon

  • JUN 14, 2016

    Protein Structures Pave The Way For Broad-Spectrum Antifungals

  • JUL 29, 2015

    Structures Reveal Basis of Recurring Urinary Tract Infections
• 

  Awards & Honors

  • AAAS Fellow. American Association for the Advancement of Science. 2011
  • Fellow of the American Academy of Microbiology. The American Academy of Microbiology (AAM). 2007
• Research
• 

  Selected Grants

  • Structural studies of virulence activation in Francisella tularensis awarded by National Institutes of Health 2020 - 2023
  • Structural Elucidation of the Novel RNA Polymerase Underlying Francisella Tularensis Virulence awarded by National Institutes of Health 2020 - 2022
  • Molecular Mycology and Pathogenesis Training Program awarded by National Institutes of Health 2019 - 2021
  • SALMONELLA HIJACKING OF STAT3 AND CONSEQUENCES FOR DISEASE awarded by National Institutes of Health 2019 - 2021
  • Organization and Function of Cellular Structure awarded by National Institutes of Health 1975 - 2020
  • Biology of the HMW1 and HMW2 Adhesins of H. Influenzae awarded by Children's Hospital of Philadelphia 2013 - 2020
  • Investigating a Novel Co-regulation of Multi-Drug Efflux Pumps and Polysaccharide Capsule in E. coli awarded by National Institutes of Health 2017 - 2018
  • Defining the structural mechanisms of Hfq binding to cognate nucleic acids awarded by National Institutes of Health 2015 - 2017
  • Structural Biology and Biophysics Training Program awarded by National Institutes of Health 1994 - 2015
  • High sensitivity multi-purpose electron paramagnetic resonance spectroscopy for biotechnological and biomedical research awarded by North Carolina Biotechnology Center 2014 - 2015
• 

  External Relationships

  • John Innes Centre, Norwich England
• Publications & Artistic Works
• 

  Selected Publications

  • Academic Articles

    • Travis, Brady A., Kathryn M. Ramsey, Samantha M. Prezioso, Thomas Tallo, Jamie M. Wandzilak, Allen Hsu, Mario Borgnia, et al. “Structural Basis for Virulence Activation of Francisella tularensis.” Mol Cell, November 12, 2020. https://doi.org/10.1016/j.molcel.2020.10.035.
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    • Arshad, Mehreen, Grace A. Beggs, Richard G. Brennan, and Patrick C. Seed. “Optimization of a non-canonical anti-infective: Interrogation of the target binding pocket for a small molecule inhibitor of E. coli polysaccharide capsule expression.” Antimicrob Agents Chemother, October 19, 2020. https://doi.org/10.1128/AAC.01208-20.
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    • Dorman, Charles J., Maria A. Schumacher, Matthew J. Bush, Richard G. Brennan, and Mark J. Buttner. “When is a transcription factor a NAP?” Curr Opin Microbiol 55 (June 2020): 26–33. https://doi.org/10.1016/j.mib.2020.01.019.
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    • Orans, Jillian, Alexander R. Kovach, Kirsten E. Hoff, Nicola M. Horstmann, and Richard G. Brennan. “Crystal structure of an Escherichia coli Hfq Core (residues 2-69)-DNA complex reveals multifunctional nucleic acid binding sites.” Nucleic Acids Res 48, no. 7 (April 17, 2020): 3987–97. https://doi.org/10.1093/nar/gkaa149.
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    • Beggs, Grace A., Richard G. Brennan, and Mehreen Arshad. “MarR family proteins are important regulators of clinically relevant antibiotic resistance.” Protein Sci 29, no. 3 (March 2020): 647–53. https://doi.org/10.1002/pro.3769.
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    • Gallagher, Kelley A., Maria A. Schumacher, Matthew J. Bush, Maureen J. Bibb, Govind Chandra, Neil A. Holmes, Wenjie Zeng, et al. “c-di-GMP Arms an Anti-σ to Control Progression of Multicellular Differentiation in Streptomyces.” Mol Cell 77, no. 3 (February 6, 2020): 586-599.e6. https://doi.org/10.1016/j.molcel.2019.11.006.
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    • Gibbs, Kyle D., Erica J. Washington, Sarah L. Jaslow, Jeffrey S. Bourgeois, Matthew W. Foster, Robyn Guo, Richard G. Brennan, and Dennis C. Ko. “The Salmonella Secreted Effector SarA/SteE Mimics Cytokine Receptor Signaling to Activate STAT3.” Cell Host Microbe 27, no. 1 (January 8, 2020): 129-139.e4. https://doi.org/10.1016/j.chom.2019.11.012.
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    • Beggs, Grace A., Yaramah M. Zalucki, Nicholas Gene Brown, Sheila Rastegari, Rebecca K. Phillips, Timothy Palzkill, William M. Shafer, Muthiah Kumaraswami, and Richard G. Brennan. “Structural, Biochemical, and In Vivo Characterization of MtrR-Mediated Resistance to Innate Antimicrobials by the Human Pathogen Neisseria gonorrhoeae.” J Bacteriol 201, no. 20 (October 15, 2019). https://doi.org/10.1128/JB.00401-19.
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    • Claeys, Hannes, Son Lang Vi, Xiaosa Xu, Namiko Satoh-Nagasawa, Andrea L. Eveland, Alexander Goldshmidt, Regina Feil, et al. “Control of meristem determinacy by trehalose 6-phosphate phosphatases is uncoupled from enzymatic activity.” Nat Plants 5, no. 4 (April 2019): 352–57. https://doi.org/10.1038/s41477-019-0394-z.
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    • Schumacher, Maria A., Chris D. den Hengst, Matthew J. Bush, T. B. K. Le, Ngat T. Tran, Govind Chandra, Wenjie Zeng, Brady Travis, Richard G. Brennan, and Mark J. Buttner. “The MerR-like protein BldC binds DNA direct repeats as cooperative multimers to regulate Streptomyces development.” Nat Commun 9, no. 1 (March 19, 2018): 1139. https://doi.org/10.1038/s41467-018-03576-3.
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    • Cuthbert, Bonnie J., Wilma Ross, Amy E. Rohlfing, Simon L. Dove, Richard L. Gourse, Richard G. Brennan, and Maria A. Schumacher. “Dissection of the molecular circuitry controlling virulence in Francisella tularensis.” Genes Dev 31, no. 15 (August 1, 2017): 1549–60. https://doi.org/10.1101/gad.303701.117.
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    • Miao, Yi, Jennifer L. Tenor, Dena L. Toffaletti, Stacey A. Maskarinec, Jiuyu Liu, Richard E. Lee, John R. Perfect, and Richard G. Brennan. “Structural and In Vivo Studies on Trehalose-6-Phosphate Synthase from Pathogenic Fungi Provide Insights into Its Catalytic Mechanism, Biological Necessity, and Potential for Novel Antifungal Drug Design.” Mbio 8, no. 4 (July 25, 2017). https://doi.org/10.1128/mBio.00643-17.
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    • Schumacher, Maria A., Wenjie Zeng, Kim C. Findlay, Mark J. Buttner, Richard G. Brennan, and Natalia Tschowri. “The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD2-(c-di-GMP)4 complex.” Nucleic Acids Research 45, no. 11 (June 2017): 6923–33. https://doi.org/10.1093/nar/gkx287.
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    • Thammahong, Arsa, Srisombat Puttikamonkul, John R. Perfect, Richard G. Brennan, and Robert A. Cramer. “Central Role of the Trehalose Biosynthesis Pathway in the Pathogenesis of Human Fungal Infections: Opportunities and Challenges for Therapeutic Development.” Microbiology and Molecular Biology Reviews : Mmbr 81, no. 2 (June 2017). https://doi.org/10.1128/mmbr.00053-16.
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    • Perfect, John R., Jennifer L. Tenor, Yi Miao, and Richard G. Brennan. “Trehalose pathway as an antifungal target.” Virulence 8, no. 2 (February 17, 2017): 143–49. https://doi.org/10.1080/21505594.2016.1195529.
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    • Miao, Yi, Jennifer L. Tenor, Dena L. Toffaletti, Erica J. Washington, Jiuyu Liu, William R. Shadrick, Maria A. Schumacher, Richard E. Lee, John R. Perfect, and Richard G. Brennan. “Structures of trehalose-6-phosphate phosphatase from pathogenic fungi reveal the mechanisms of substrate recognition and catalysis.” Proc Natl Acad Sci U S A 113, no. 26 (June 28, 2016): 7148–53. https://doi.org/10.1073/pnas.1601774113.
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    • Schumacher, Maria A., Pooja Balani, Jungki Min, Naga Babu Chinnam, Sonja Hansen, Marin Vulić, Kim Lewis, and Richard G. Brennan. “HipBA-promoter structures reveal the basis of heritable multidrug tolerance.” Nature 524, no. 7563 (August 6, 2015): 59–64. https://doi.org/10.1038/nature14662.
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    • Schindler, Bryan D., Susan M. Seo, Ivan Birukou, Richard G. Brennan, and Glenn W. Kaatz. “Mutations within the mepA operator affect binding of the MepR regulatory protein and its induction by MepA substrates in Staphylococcus aureus.” J Bacteriol 197, no. 6 (March 2015): 1104–14. https://doi.org/10.1128/JB.02558-14.
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    • Reniere, Michelle L., Aaron T. Whiteley, Keri L. Hamilton, Sonya M. John, Peter Lauer, Richard G. Brennan, and Daniel A. Portnoy. “Glutathione activates virulence gene expression of an intracellular pathogen.” Nature 517, no. 7533 (January 8, 2015): 170–73. https://doi.org/10.1038/nature14029.
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    • Cuthbert, Bonnie J., Richard G. Brennan, and Maria A. Schumacher. “Structural and Biochemical Characterization of the Francisella tularensis Pathogenicity Regulator, Macrophage Locus Protein A (MglA).” Plos One 10, no. 6 (2015): e0128225. https://doi.org/10.1371/journal.pone.0128225.
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    • Kovach, Alexander R., Kirsten E. Hoff, John T. Canty, Jillian Orans, and Richard G. Brennan. “Recognition of U-rich RNA by Hfq from the Gram-positive pathogen Listeria monocytogenes.” Rna 20, no. 10 (October 2014): 1548–59. https://doi.org/10.1261/rna.044032.113.
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    • Tschowri, Natalia, Maria A. Schumacher, Susan Schlimpert, Naga Babu Chinnam, Kim C. Findlay, Richard G. Brennan, and Mark J. Buttner. “Tetrameric c-di-GMP mediates effective transcription factor dimerization to control Streptomyces development.” Cell 158, no. 5 (August 28, 2014): 1136–47. https://doi.org/10.1016/j.cell.2014.07.022.
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    • Birukou, Ivan, Susan M. Seo, Bryan D. Schindler, Glenn W. Kaatz, and Richard G. Brennan. “Structural mechanism of transcription regulation of the Staphylococcus aureus multidrug efflux operon mepRA by the MarR family repressor MepR.” Nucleic Acids Res 42, no. 4 (February 2014): 2774–88. https://doi.org/10.1093/nar/gkt1215.
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    • Robinson, Kirsten E., Jillian Orans, Alexander R. Kovach, Todd M. Link, and Richard G. Brennan. “Mapping Hfq-RNA interaction surfaces using tryptophan fluorescence quenching.” Nucleic Acids Res 42, no. 4 (February 2014): 2736–49. https://doi.org/10.1093/nar/gkt1171.
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    • Birukou, Ivan, Nam K. Tonthat, Susan M. Seo, Bryan D. Schindler, Glenn W. Kaatz, and Richard G. Brennan. “The molecular mechanisms of allosteric mutations impairing MepR repressor function in multidrug-resistant strains of Staphylococcus aureus.” Mbio 4, no. 5 (August 27, 2013): e00528–e00513. https://doi.org/10.1128/mBio.00528-13.
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    • Schindler, Bryan D., Susan M. Seo, Pauline L. Jacinto, Muthiah Kumaraswami, Ivan Birukou, Richard G. Brennan, and Glenn W. Kaatz. “Functional consequences of substitution mutations in MepR, a repressor of the Staphylococcus aureus MepA multidrug efflux pump gene.” J Bacteriol 195, no. 16 (August 2013): 3651–62. https://doi.org/10.1128/JB.00565-13.
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    • Xie, Tong-Xin, Ge Zhou, Mei Zhao, Daisuke Sano, Samar A. Jasser, Richard G. Brennan, and Jeffrey N. Myers. “Serine substitution of proline at codon 151 of TP53 confers gain of function activity leading to anoikis resistance and tumor progression of head and neck cancer cells.” Laryngoscope 123, no. 6 (June 2013): 1416–23. https://doi.org/10.1002/lary.23846.
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    • Rajagopalan, S., S. J. Teter, P. H. Zwart, R. G. Brennan, K. J. Phillips, and P. J. Kiley. “Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity.” Nature Structural and Molecular Biology 20, no. 6 (2013): 740–47. https://doi.org/10.1038/nsmb.2568.
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    • Horstmann, Nicola, Jillian Orans, Poul Valentin-Hansen, Samuel A. Shelburne, and Richard G. Brennan. “Structural mechanism of Staphylococcus aureus Hfq binding to an RNA A-tract.” Nucleic Acids Res 40, no. 21 (November 2012): 11023–35. https://doi.org/10.1093/nar/gks809.
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    • Schumacher, Maria A., JungKi Min, Todd M. Link, Ziqiang Guan, Weijun Xu, Young-Ho Ahn, Erik J. Soderblom, et al. “Role of unusual P loop ejection and autophosphorylation in HipA-mediated persistence and multidrug tolerance.” Cell Rep 2, no. 3 (September 27, 2012): 518–25. https://doi.org/10.1016/j.celrep.2012.08.013.
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    • Amato, Angélica A., Senapathy Rajagopalan, Jean Z. Lin, Bruno M. Carvalho, Ana C. M. Figueira, Jenny Lu, Stephen D. Ayers, et al. “GQ-16, a novel peroxisome proliferator-activated receptor γ (PPARγ) ligand, promotes insulin sensitization without weight gain.” J Biol Chem 287, no. 33 (August 10, 2012): 28169–79. https://doi.org/10.1074/jbc.M111.332106.
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    • Hansen, Sonja, Marin Vulić, Jungki Min, Tien-Jui Yen, Maria A. Schumacher, Richard G. Brennan, and Kim Lewis. “Regulation of the Escherichia coli HipBA toxin-antitoxin system by proteolysis.” Plos One 7, no. 6 (2012): e39185. https://doi.org/10.1371/journal.pone.0039185.
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    • Le, Tung B. K., Maria A. Schumacher, David M. Lawson, Richard G. Brennan, and Mark J. Buttner. “The crystal structure of the TetR family transcriptional repressor SimR bound to DNA and the role of a flexible N-terminal extension in minor groove binding.” Nucleic Acids Res 39, no. 21 (November 2011): 9433–47. https://doi.org/10.1093/nar/gkr640.
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    • Horstmann, Nicola, Pranoti Sahasrabhojane, Bryce Suber, Muthiah Kumaraswami, Randall J. Olsen, Anthony Flores, James M. Musser, Richard G. Brennan, and Samuel A. Shelburne. “Distinct single amino acid replacements in the control of virulence regulator protein differentially impact streptococcal pathogenesis.” Plos Pathogens 7, no. 10 (October 20, 2011): e1002311. https://doi.org/10.1371/journal.ppat.1002311.
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    • Shelburne, Samuel A., Pranoti Sahasrobhajane, Bryce Suber, David B. Keith, Michael T. Davenport, Nicola Horstmann, Muthiah Kumaraswami, Randall J. Olsen, Richard G. Brennan, and James M. Musser. “Niche-specific contribution to streptococcal virulence of a MalR-regulated carbohydrate binding protein.” Mol Microbiol 81, no. 2 (July 2011): 500–514. https://doi.org/10.1111/j.1365-2958.2011.07708.x.
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    • Schumacher, Maria A., Mareen Sprehe, Maike Bartholomae, Wolfgang Hillen, and Richard G. Brennan. “Structures of carbon catabolite protein A-(HPr-Ser46-P) bound to diverse catabolite response element sites reveal the basis for high-affinity binding to degenerate DNA operators.” Nucleic Acids Res 39, no. 7 (April 2011): 2931–42. https://doi.org/10.1093/nar/gkq1177.
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    • Peters, Kate M., Benjamin E. Brooks, Maria A. Schumacher, Ronald A. Skurray, Richard G. Brennan, and Melissa H. Brown. “A single acidic residue can guide binding site selection but does not govern QacR cationic-drug affinity.” Plos One 6, no. 1 (January 17, 2011): e15974. https://doi.org/10.1371/journal.pone.0015974.
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    • Cho, Kyucheol, Travis G. Vaught, Hong Ji, Dongmin Gu, Catherine Papasakelariou-Yared, Nicola Horstmann, Jean Marie Jennings, et al. “Xenopus Kazrin interacts with ARVCF-catenin, spectrin and p190B RhoGAP, and modulates RhoA activity and epithelial integrity.” J Cell Sci 123, no. Pt 23 (December 1, 2010): 4128–44. https://doi.org/10.1242/jcs.072041.
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    • Olsen, Anders Steno, Jakob Møller-Jensen, Richard G. Brennan, and Poul Valentin-Hansen. “C-terminally truncated derivatives of Escherichia coli Hfq are proficient in riboregulation.” J Mol Biol 404, no. 2 (November 26, 2010): 173–82. https://doi.org/10.1016/j.jmb.2010.09.038.
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    • Kumaraswami, Muthiah, Kate J. Newberry, and Richard G. Brennan. “Conformational plasticity of the coiled-coil domain of BmrR is required for bmr operator binding: the structure of unliganded BmrR.” J Mol Biol 398, no. 2 (April 30, 2010): 264–75. https://doi.org/10.1016/j.jmb.2010.03.011.
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    • Shelburne, Samuel A., Randall J. Olsen, Bryce Suber, Pranoti Sahasrabhojane, Paul Sumby, Richard G. Brennan, and James M. Musser. “A combination of independent transcriptional regulators shapes bacterial virulence gene expression during infection.” Plos Pathogens 6, no. 3 (March 19, 2010): e1000817. https://doi.org/10.1371/journal.ppat.1000817.
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    • Nakano, Michiko M., Ann Lin, Cole S. Zuber, Kate J. Newberry, Richard G. Brennan, and Peter Zuber. “Promoter recognition by a complex of Spx and the C-terminal domain of the RNA polymerase alpha subunit.” Plos One 5, no. 1 (January 13, 2010): e8664. https://doi.org/10.1371/journal.pone.0008664.
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    • Nakano, M. M., A. Lin, C. S. Zuber, K. J. Newberry, R. G. Brennan, and P. Zuber. “Promoter recognition by a complex of Spx and the C-terminal domain of the RNA polymerase α subunit.” Plos One 5, no. 1 (2010). https://doi.org/10.1371/journal.pone.0008664.
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    • Link, T. M., P. Valentin-Hansen, and R. G. Brennan. “Structure of Escherichia coli Hfq bound to polyriboadenylate RNA.” Proceedings of the National Academy of Sciences 106, no. 46 (November 17, 2009): 19292–97. https://doi.org/10.1073/pnas.0908744106.
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    • Stoll, Kate E., William E. Draper, Joseph I. Kliegman, Misha V. Golynskiy, Rhoda A. T. Brew-Appiah, Rebecca K. Phillips, Hattie K. Brown, et al. “Characterization and structure of the manganese-responsive transcriptional regulator ScaR.” Biochemistry 48, no. 43 (November 3, 2009): 10308–20. https://doi.org/10.1021/bi900980g.
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    • Shelburne, S. A., D. Keith, N. Horstmann, P. Sumby, M. T. Davenport, E. A. Graviss, R. G. Brennan, and J. M. Musser. “A direct link between carbohydrate utilization and virulence in the major human pathogen group A Streptococcus (Proceedings of the National Academy of Sciences of the United States of America (2008) 105, 5, (1698-1703) DOI: 10.1073/pnas.0711767105).” Proceedings of the National Academy of Sciences of the United States of America 106, no. 21 (May 26, 2009): 8790. https://doi.org/10.1073/pnas.0903221106.
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    • Hassan, Karl A., Zhiqiang Xu, Ryan E. Watkins, Richard G. Brennan, Ronald A. Skurray, and Melissa H. Brown. “Optimized production and analysis of the staphylococcal multidrug efflux protein QacA.” Protein Expr Purif 64, no. 2 (April 2009): 118–24. https://doi.org/10.1016/j.pep.2008.11.009.
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    • Kumaraswami, Muthiah, Jason T. Schuman, Susan M. Seo, Glenn W. Kaatz, and Richard G. Brennan. “Structural and biochemical characterization of MepR, a multidrug binding transcription regulator of the Staphylococcus aureus multidrug efflux pump MepA.” Nucleic Acids Res 37, no. 4 (March 2009): 1211–24. https://doi.org/10.1093/nar/gkn1046.
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    • Schumacher, Maria A., Kevin M. Piro, Weijun Xu, Sonja Hansen, Kim Lewis, and Richard G. Brennan. “Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB.” Science (New York, N.Y.) 323, no. 5912 (January 2009): 396–401. https://doi.org/10.1126/science.1163806.
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    • Newberry, Kate J., Joy L. Huffman, Marshall C. Miller, Nora Vazquez-Laslop, Alex A. Neyfakh, and Richard G. Brennan. “Structures of BmrR-drug complexes reveal a rigid multidrug binding pocket and transcription activation through tyrosine expulsion.” J Biol Chem 283, no. 39 (September 26, 2008): 26795–804. https://doi.org/10.1074/jbc.M804191200.
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    • Peters, Kate M., Jason T. Schuman, Ronald A. Skurray, Melissa H. Brown, Richard G. Brennan, and Maria A. Schumacher. “QacR-cation recognition is mediated by a redundancy of residues capable of charge neutralization.” Biochemistry 47, no. 31 (August 5, 2008): 8122–29. https://doi.org/10.1021/bi8008246.
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    • Shelburne, Samuel A., David B. Keith, Michael T. Davenport, Nicola Horstmann, Richard G. Brennan, and James M. Musser. “Molecular characterization of group A Streptococcus maltodextrin catabolism and its role in pharyngitis.” Mol Microbiol 69, no. 2 (July 2008): 436–52. https://doi.org/10.1111/j.1365-2958.2008.06290.x.
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    • Amen, Melanie, Herbert M. Espinoza, Carol Cox, Xiaowen Liang, Jianbo Wang, Todd M. E. Link, Richard G. Brennan, James F. Martin, and Brad A. Amendt. “Chromatin-associated HMG-17 is a major regulator of homeodomain transcription factor activity modulated by Wnt/beta-catenin signaling.” Nucleic Acids Res 36, no. 2 (February 2008): 462–76. https://doi.org/10.1093/nar/gkm1047.
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    • Shelburne, Samuel A., David Keith, Nicola Horstmann, Paul Sumby, Michael T. Davenport, Edward A. Graviss, Richard G. Brennan, and James M. Musser. “A direct link between carbohydrate utilization and virulence in the major human pathogen group A Streptococcus.” Proceedings of the National Academy of Sciences of the United States of America 105, no. 5 (February 2008): 1698–1703. https://doi.org/10.1073/pnas.0711767105.
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    • Newberry, Kate J., Mayuree Fuangthong, Warunya Panmanee, Skorn Mongkolsuk, and Richard G. Brennan. “Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR.” Mol Cell 28, no. 4 (November 30, 2007): 652–64. https://doi.org/10.1016/j.molcel.2007.09.016.
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    • Brooks, Benjamin E., Kevin M. Piro, and Richard G. Brennan. “Multidrug-binding transcription factor QacR binds the bivalent aromatic diamidines DB75 and DB359 in multiple positions.” J Am Chem Soc 129, no. 26 (July 4, 2007): 8389–95. https://doi.org/10.1021/ja072576v.
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    • Schumacher, Maria A., Gerald Seidel, Wolfgang Hillen, and Richard G. Brennan. “Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose 6-phosphate and fructose 1,6-bisphosphate.” J Mol Biol 368, no. 4 (May 11, 2007): 1042–50. https://doi.org/10.1016/j.jmb.2007.02.054.
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    • Brennan, Richard G., and Todd M. Link. “Hfq structure, function and ligand binding.” Curr Opin Microbiol 10, no. 2 (April 2007): 125–33. https://doi.org/10.1016/j.mib.2007.03.015.
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    • DeWitt, Mark A., Joseph I. Kliegman, John D. Helmann, Richard G. Brennan, David L. Farrens, and Arthur Glasfeld. “The conformations of the manganese transport regulator of Bacillus subtilis in its metal-free state.” J Mol Biol 365, no. 5 (February 2, 2007): 1257–65. https://doi.org/10.1016/j.jmb.2006.10.080.
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    • Mattison, Kirsten, J Scott Wilbur, Magdalene So, and Richard G. Brennan. “Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helix-helix motifs.” J Biol Chem 281, no. 49 (December 8, 2006): 37942–51. https://doi.org/10.1074/jbc.M605198200.
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    • Kliegman, Joseph I., Sarah L. Griner, John D. Helmann, Richard G. Brennan, and Arthur Glasfeld. “Structural basis for the metal-selective activation of the manganese transport regulator of Bacillus subtilis.” Biochemistry 45, no. 11 (March 21, 2006): 3493–3505. https://doi.org/10.1021/bi0524215.
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    • Schumacher, Maria A., Gerald Seidel, Wolfgang Hillen, and Richard G. Brennan. “Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation.” J Biol Chem 281, no. 10 (March 10, 2006): 6793–6800. https://doi.org/10.1074/jbc.M509977200.
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    • Newberry, Kate J., Shunji Nakano, Peter Zuber, and Richard G. Brennan. “Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase.” Proceedings of the National Academy of Sciences of the United States of America 102, no. 44 (November 2005): 15839–44. https://doi.org/10.1073/pnas.0506592102.
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    • Hong, Minsun, Mayuree Fuangthong, John D. Helmann, and Richard G. Brennan. “Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family.” Mol Cell 20, no. 1 (October 7, 2005): 131–41. https://doi.org/10.1016/j.molcel.2005.09.013.
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    • Wilbur, J Scott, Peter T. Chivers, Kirsten Mattison, Laura Potter, Richard G. Brennan, and Magdalene So. “Neisseria gonorrhoeae FitA interacts with FitB to bind DNA through its ribbon-helix-helix motif.” Biochemistry 44, no. 37 (September 20, 2005): 12515–24. https://doi.org/10.1021/bi0511080.
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    • Hoffmann, Katherine M., Daniel Williams, William M. Shafer, and Richard G. Brennan. “Characterization of the multiple transferable resistance repressor, MtrR, from Neisseria gonorrhoeae.” J Bacteriol 187, no. 14 (July 2005): 5008–12. https://doi.org/10.1128/JB.187.14.5008-5012.2005.
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    • Ramos, Juan L., Manuel Martínez-Bueno, Antonio J. Molina-Henares, Wilson Terán, Kazuya Watanabe, Xiaodong Zhang, María Trinidad Gallegos, Richard Brennan, and Raquel Tobes. “The TetR family of transcriptional repressors.” Microbiol Mol Biol Rev 69, no. 2 (June 2005): 326–56. https://doi.org/10.1128/MMBR.69.2.326-356.2005.
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    • Schumacher, Maria A., Gregory S. Allen, Marco Diel, Gerald Seidel, Wolfgang Hillen, and Richard G. Brennan. “Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P.” Cell 118, no. 6 (September 17, 2004): 731–41. https://doi.org/10.1016/j.cell.2004.08.027.
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    • Schumacher, Maria A., Marshall C. Miller, and Richard G. Brennan. “Structural mechanism of the simultaneous binding of two drugs to a multidrug-binding protein.” Embo J 23, no. 15 (August 4, 2004): 2923–30. https://doi.org/10.1038/sj.emboj.7600288.
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    • Newberry, Kate J., and Richard G. Brennan. “The structural mechanism for transcription activation by MerR family member multidrug transporter activation, N terminus.” J Biol Chem 279, no. 19 (May 7, 2004): 20356–62. https://doi.org/10.1074/jbc.M400960200.
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    • Murray, David S., Maria A. Schumacher, and Richard G. Brennan. “Crystal structures of QacR-diamidine complexes reveal additional multidrug-binding modes and a novel mechanism of drug charge neutralization.” J Biol Chem 279, no. 14 (April 2, 2004): 14365–71. https://doi.org/10.1074/jbc.M313870200.
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    • Glasfeld, Arthur, Emmanuel Guedon, John D. Helmann, and Richard G. Brennan. “Structure of the manganese-bound manganese transport regulator of Bacillus subtilis.” Nat Struct Biol 10, no. 8 (August 2003): 652–57. https://doi.org/10.1038/nsb951.
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    • Schumacher, Maria A., and Richard G. Brennan. “Deciphering the molecular basis of multidrug recognition: crystal structures of the Staphylococcus aureus multidrug binding transcription regulator QacR.” Res Microbiol 154, no. 2 (March 2003): 69–77. https://doi.org/10.1016/S0923-2508(02)00013-X.
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    • Allen, Gregory S., Katrin Steinhauer, Wolfgang Hillen, Jörg Stülke, and Richard G. Brennan. “Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae.” J Mol Biol 326, no. 4 (February 28, 2003): 1203–17. https://doi.org/10.1016/s0022-2836(02)01378-5.
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    • Godsey, Michael H., Ekaterina E. Zheleznova Heldwein, and Richard G. Brennan. “Structural biology of bacterial multidrug resistance gene regulators.” J Biol Chem 277, no. 43 (October 25, 2002): 40169–72. https://doi.org/10.1074/jbc.R200018200.
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    • Schumacher, Maria A., and Richard G. Brennan. “Structural mechanisms of multidrug recognition and regulation by bacterial multidrug transcription factors.” Mol Microbiol 45, no. 4 (August 2002): 885–93. https://doi.org/10.1046/j.1365-2958.2002.03039.x.
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    • Schumacher, Maria A., Robert F. Pearson, Thorleif Møller, Poul Valentin-Hansen, and Richard G. Brennan. “Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein.” Embo J 21, no. 13 (July 1, 2002): 3546–56. https://doi.org/10.1093/emboj/cdf322.
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    • Schumacher, M. A., M. C. Miller, S. Grkovic, M. H. Brown, R. A. Skurray, and R. G. Brennan. “Erratum: Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR (EMBO Journal (2002) 21 (1210-1218)).” Embo Journal 21, no. 9 (May 1, 2002): 2301. https://doi.org/10.1093/emboj/21.9.2301.
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    • Bashor, Caleb, John M. Denu, Richard G. Brennan, and Buddy Ullman. “Kinetic mechanism of adenine phosphoribosyltransferase from Leishmania donovani.” Biochemistry 41, no. 12 (March 26, 2002): 4020–31. https://doi.org/10.1021/bi0158730.
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    • Schumacher, Maria A., Marshall C. Miller, Steve Grkovic, Melissa H. Brown, Ronald A. Skurray, and Richard G. Brennan. “Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR.” Embo J 21, no. 5 (March 1, 2002): 1210–18. https://doi.org/10.1093/emboj/21.5.1210.
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    • Steinhauer, Katrin, Gregory S. Allen, Wolfgang Hillen, Jörg Stülke, and Richard G. Brennan. “Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae.” Acta Crystallogr D Biol Crystallogr 58, no. Pt 3 (March 2002): 515–18. https://doi.org/10.1107/s090744490102145x.
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    • Huffman, Joy L., and Richard G. Brennan. “Prokaryotic transcription regulators: more than just the helix-turn-helix motif.” Curr Opin Struct Biol 12, no. 1 (February 2002): 98–106. https://doi.org/10.1016/s0959-440x(02)00295-6.
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    • Huffman, Joy L., Fu Lu, Howard Zalkin, and Richard G. Brennan. “Role of residue 147 in the gene regulatory function of the Escherichia coli purine repressor.” Biochemistry 41, no. 2 (January 15, 2002): 511–20. https://doi.org/10.1021/bi0156660.
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    • Schumacher, Maria A., Caleb J. Bashor, Minsun Hong Song, Kanao Otsu, Shuren Zhu, Ronald J. Parry, Buddy Ullman, and Richard G. Brennan. “The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase.” Proc Natl Acad Sci U S A 99, no. 1 (January 8, 2002): 78–83. https://doi.org/10.1073/pnas.012399599.
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    • Møller, Thorleif, Thomas Franch, Peter Højrup, Douglas R. Keene, Hans Peter Bächinger, Richard G. Brennan, and Poul Valentin-Hansen. “Hfq: a bacterial Sm-like protein that mediates RNA-RNA interaction.” Mol Cell 9, no. 1 (January 2002): 23–30. https://doi.org/10.1016/s1097-2765(01)00436-1.
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    • Godsey, M. H., N. N. Baranova, A. A. Neyfakh, and R. G. Brennan. “Crystal structure of MtaN, a global multidrug transporter gene activator.” J Biol Chem 276, no. 50 (December 14, 2001): 47178–84. https://doi.org/10.1074/jbc.M105819200.
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    • Schumacher, M. A., M. C. Miller, S. Grkovic, M. H. Brown, R. A. Skurray, and R. G. Brennan. “Structural mechanisms of QacR induction and multidrug recognition.” Science 294, no. 5549 (December 7, 2001): 2158–63. https://doi.org/10.1126/science.1066020.
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    • Grkovic, S., M. H. Brown, M. A. Schumacher, R. G. Brennan, and R. A. Skurray. “The staphylococcal QacR multidrug regulator binds a correctly spaced operator as a pair of dimers.” J Bacteriol 183, no. 24 (December 2001): 7102–9. https://doi.org/10.1128/JB.183.24.7102-7109.2001.
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    • Huffman, J. L., A. Mokashi, H. P. Bächinger, and R. G. Brennan. “The basic helix-loop-helix domain of the aryl hydrocarbon receptor nuclear transporter (ARNT) can oligomerize and bind E-box DNA specifically.” J Biol Chem 276, no. 44 (November 2, 2001): 40537–44. https://doi.org/10.1074/jbc.M105675200.
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    • Schumacher, M. A., B. K. Hurlburt, and R. G. Brennan. “Erratum: Crystal structures of SarA, a pleiotropic regulator of virulence genes in S. aureus (Nature (20010 409 (215-219)).” Nature 414, no. 6859 (November 1, 2001): 85. https://doi.org/10.1038/35102089.
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    • Craig, J. C., M. A. Schumacher, S. E. Mansoor, D. L. Farrens, R. G. Brennan, and R. H. Goodman. “Consensus and variant cAMP-regulated enhancers have distinct CREB-binding properties.” J Biol Chem 276, no. 15 (April 13, 2001): 11719–28. https://doi.org/10.1074/jbc.M010263200.
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    • Heldwein, E. E., and R. G. Brennan. “Crystal structure of the transcription activator BmrR bound to DNA and a drug.” Nature 409, no. 6818 (January 18, 2001): 378–82. https://doi.org/10.1038/35053138.
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    • Schumacher, M. A., B. K. Hurlburt, and R. G. Brennan. “Crystal structures of SarA, a pleiotropic regulator of virulence genes in S. aureus.” Nature 409, no. 6817 (January 11, 2001): 215–19. https://doi.org/10.1038/35051623.
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    • Brennan, R. G. “Introduction: Multidrug resistance.” Seminars in Cell and Developmental Biology 12, no. 3 (January 1, 2001): 201–4. https://doi.org/10.1006/scdb.2000.0245.
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    • Schumacher, M. A., R. H. Goodman, and R. G. Brennan. “The structure of a CREB bZIP.somatostatin CRE complex reveals the basis for selective dimerization and divalent cation-enhanced DNA binding.” J Biol Chem 275, no. 45 (November 10, 2000): 35242–47. https://doi.org/10.1074/jbc.M007293200.
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    • Godsey, M. H., N. N. Baranova, A. A. Neyfakh, and R. G. Brennan. “Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the multidrug transporter activation protein (MtaN) from Bacillus subtilis.” Acta Crystallogr D Biol Crystallogr 56, no. Pt 11 (November 2000): 1456–58. https://doi.org/10.1107/s0907444900010295.
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    • Zheleznova, E. E., J. H. Crosa, and R. G. Brennan. “Characterization of the DNA- and metal-binding properties of Vibrio anguillarum fur reveals conservation of a structural Zn(2+) ion.” J Bacteriol 182, no. 21 (November 2000): 6264–67. https://doi.org/10.1128/jb.182.21.6264-6267.2000.
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    • Brown, M., M. A. Schumacher, G. D. Wiens, R. G. Brennan, and M. B. Rittenberg. “The structural basis of repertoire shift in an immune response to phosphocholine.” J Exp Med 191, no. 12 (June 19, 2000): 2101–12. https://doi.org/10.1084/jem.191.12.2101.
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    • Schumacher, M. A., D. M. Scott, I. I. Mathews, S. E. Ealick, D. S. Roos, B. Ullman, and R. G. Brennan. “Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.” J Mol Biol 298, no. 5 (May 19, 2000): 875–93. https://doi.org/10.1006/jmbi.2000.3753.
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    • Cardinaux, J. R., J. C. Notis, Q. Zhang, N. Vo, J. C. Craig, D. M. Fass, R. G. Brennan, and R. H. Goodman. “Recruitment of CREB binding protein is sufficient for CREB-mediated gene activation.” Mol Cell Biol 20, no. 5 (March 2000): 1546–52. https://doi.org/10.1128/mcb.20.5.1546-1552.2000.
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    • Schumacher, M. A., D. M. Scott, I. I. Mathews, S. E. Ealick, D. S. Roos, B. Ullman, and R. G. Brennan. “Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.” J Mol Biol 296, no. 2 (February 18, 2000): 549–67. https://doi.org/10.1006/jmbi.1999.3474.
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    • Zheleznova, E. E., P. Markham, R. Edgar, E. Bibi, A. A. Neyfakh, and R. G. Brennan. “A structure-based mechanism for drug binding by multidrug transporters.” Trends Biochem Sci 25, no. 2 (February 2000): 39–43. https://doi.org/10.1016/s0968-0004(99)01514-5.
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    • Vazquez-Laslop, N., E. E. Zheleznova, P. N. Markham, R. G. Brennan, and A. A. Neyfakh. “Recognition of multiple drugs by a single protein: a trivial solution of an old paradox.” Biochem Soc Trans 28, no. 4 (2000): 517–20.
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    • Glasfeld, A., A. N. Koehler, M. A. Schumacher, and R. G. Brennan. “The role of lysine 55 in determining the specificity of the purine repressor for its operators through minor groove interactions.” J Mol Biol 291, no. 2 (August 13, 1999): 347–61. https://doi.org/10.1006/jmbi.1999.2946.
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    • Phillips, C. L., B. Ullman, R. G. Brennan, and C. P. Hill. “Crystal structures of adenine phosphoribosyltransferase from Leishmania donovani.” Embo J 18, no. 13 (July 1, 1999): 3533–45. https://doi.org/10.1093/emboj/18.13.3533.
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    • Rechtin, T. M., A. F. Gillaspy, M. A. Schumacher, R. G. Brennan, M. S. Smeltzer, and B. K. Hurlburt. “Characterization of the SarA virulence gene regulator of Staphylococcus aureus.” Mol Microbiol 33, no. 2 (July 1999): 307–16. https://doi.org/10.1046/j.1365-2958.1999.01474.x.
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    • Zheleznova, E. E., P. N. Markham, A. A. Neyfakh, and R. G. Brennan. “Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter.” Cell 96, no. 3 (February 5, 1999): 353–62. https://doi.org/10.1016/s0092-8674(00)80548-6.
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    • Lu, F., R. G. Brennan, and H. Zalkin. “Escherichia coli purine repressor: key residues for the allosteric transition between active and inactive conformations and for interdomain signaling.” Biochemistry 37, no. 45 (November 10, 1998): 15680–90. https://doi.org/10.1021/bi981617k.
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    • Lundblad, J. R., R. P. Kwok, M. E. Laurance, M. S. Huang, J. P. Richards, R. G. Brennan, and R. H. Goodman. “The human T-cell leukemia virus-1 transcriptional activator Tax enhances cAMP-responsive element-binding protein (CREB) binding activity through interactions with the DNA minor groove.” J Biol Chem 273, no. 30 (July 24, 1998): 19251–59. https://doi.org/10.1074/jbc.273.30.19251.
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    • Schumacher, M. A., D. Carter, D. M. Scott, D. S. Roos, B. Ullman, and R. G. Brennan. “Crystal structures of Toxoplasma gondii uracil phosphoribosyltransferase reveal the atomic basis of pyrimidine discrimination and prodrug binding.” Embo J 17, no. 12 (June 15, 1998): 3219–32. https://doi.org/10.1093/emboj/17.12.3219.
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    • Arvidson, D. N., F. Lu, C. Faber, H. Zalkin, and R. G. Brennan. “The structure of PurR mutant L54M shows an alternative route to DNA kinking.” Nat Struct Biol 5, no. 6 (June 1998): 436–41. https://doi.org/10.1038/nsb0698-436.
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    • Lu, F., M. A. Schumacher, D. N. Arvidson, A. Haldimann, B. L. Wanner, H. Zalkin, and R. G. Brennan. “Structure-based redesign of corepressor specificity of the Escherichia coli purine repressor by substitution of residue 190.” Biochemistry 37, no. 4 (January 27, 1998): 971–82. https://doi.org/10.1021/bi971942s.
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    • Zheleznova, E. E., P. N. Markham, A. A. Neyfakh, and R. G. Brennan. “Preliminary structural studies on the multi-ligand-binding domain of the transcription activator, BmrR, from Bacillus subtilis.” Protein Sci 6, no. 11 (November 1997): 2465–68. https://doi.org/10.1002/pro.5560061122.
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    • Schumacher, M. A., A. Glasfeld, H. Zalkin, and R. G. Brennan. “The X-ray structure of the PurR-guanine-purF operator complex reveals the contributions of complementary electrostatic surfaces and a water-mediated hydrogen bond to corepressor specificity and binding affinity.” J Biol Chem 272, no. 36 (September 5, 1997): 22648–53. https://doi.org/10.1074/jbc.272.36.22648.
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    • Schumacher, M. A., E. E. Zheleznova, K. S. Poundstone, R. Kluger, R. T. Jones, and R. G. Brennan. “Allosteric intermediates indicate R2 is the liganded hemoglobin end state.” Proc Natl Acad Sci U S A 94, no. 15 (July 22, 1997): 7841–44. https://doi.org/10.1073/pnas.94.15.7841.
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    • Glasfeld, A., M. A. Schumacher, K. Y. Choi, H. Zalkin, and R. G. Brennan. “A positively charged residue bound in the minor groove does not alter the bending of a DNA duplex.” Journal of the American Chemical Society 118, no. 51 (December 25, 1996): 13073–74. https://doi.org/10.1021/ja962416b.
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    • Schumacher, M. A., D. Carter, D. S. Roos, B. Ullman, and R. G. Brennan. “Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop.” Nat Struct Biol 3, no. 10 (October 1996): 881–87. https://doi.org/10.1038/nsb1096-881.
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    • Phillíps, C. L., B. Ullman, and R. G. Brennan. “Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase.” Proteins 25, no. 4 (August 1996): 510–13. https://doi.org/10.1002/prot.11.
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    • Richards, J. P., H. P. Bächinger, R. H. Goodman, and R. G. Brennan. “Analysis of the structural properties of cAMP-responsive element-binding protein (CREB) and phosphorylated CREB.” J Biol Chem 271, no. 23 (June 7, 1996): 13716–23. https://doi.org/10.1074/jbc.271.23.13716.
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    • Lewis, M., G. Chang, N. C. Horton, M. A. Kercher, H. C. Pace, M. A. Schumacher, R. G. Brennan, and P. Lu. “Crystal structure of the lactose operon repressor and its complexes with DNA and inducer.” Science (New York, N.Y.) 271, no. 5253 (March 1996): 1247–54. https://doi.org/10.1126/science.271.5253.1247.
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    • Nagadoi, A., S. Morikawa, H. Nakamura, M. Enari, K. Kobayashi, H. Yamamoto, G. Sampei, K. Mizobuchi, M. A. Schumacher, and R. G. Brennan. “Structural comparison of the free and DNA-bound forms of the purine repressor DNA-binding domain.” Structure 3, no. 11 (November 15, 1995): 1217–24. https://doi.org/10.1016/s0969-2126(01)00257-x.
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    • Schumacher, M. A., K. Y. Choi, F. Lu, H. Zalkin, and R. G. Brennan. “Mechanism of corepressor-mediated specific DNA binding by the purine repressor.” Cell 83, no. 1 (October 6, 1995): 147–55. https://doi.org/10.1016/0092-8674(95)90243-0.
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    • Schumacher, M. A., M. M. Dixon, R. Kluger, R. T. Jones, and R. G. Brennan. “Allosteric transition intermediates modelled by crosslinked haemoglobins.” Nature 375, no. 6526 (May 4, 1995): 84–87. https://doi.org/10.1038/375084a0.
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    • Nagadoi, A., K. Nakazawa, S. Morikawa, H. Nakamura, G. Sampei, K. Mizobuchi, H. Yamamoto, M. A. Schumacher, R. G. Brennan, and Y. Nishimura. “Conformational changes of purine repressor DNA-binding domain upon complexation with DNA.” Nucleic Acids Symp Ser, no. 34 (1995): 63–64.
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    • Brickey, D. A., J. G. Bann, Y. L. Fong, L. Perrino, R. G. Brennan, and T. R. Soderling. “Mutational analysis of the autoinhibitory domain of calmodulin kinase II.” J Biol Chem 269, no. 46 (November 18, 1994): 29047–54.
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    • Loriaux, M. M., R. G. Brennan, and R. H. Goodman. “Modulatory function of CREB.CREM alpha heterodimers depends upon CREM alpha phosphorylation.” J Biol Chem 269, no. 46 (November 18, 1994): 28839–43.
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    • Schumacher, M. A., K. Y. Choi, H. Zalkin, and R. G. Brennan. “Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices.” Science 266, no. 5186 (November 4, 1994): 763–70. https://doi.org/10.1126/science.7973627.
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    • Schumacher, M. A., K. Y. Choi, H. Zalkin, and R. G. Brennan. “Crystallization and preliminary X-ray analysis of an Escherichia coli purine repressor-hypoxanthine-DNA complex.” J Mol Biol 242, no. 3 (September 23, 1994): 302–5. https://doi.org/10.1006/jmbi.1994.1580.
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    • Kwok, R. P., J. R. Lundblad, J. C. Chrivia, J. P. Richards, H. P. Bächinger, R. G. Brennan, S. G. Roberts, M. R. Green, and R. H. Goodman. “Nuclear protein CBP is a coactivator for the transcription factor CREB.” Nature 370, no. 6486 (July 21, 1994): 223–26. https://doi.org/10.1038/370223a0.
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    • Loriaux, M. M., R. P. Rehfuss, R. G. Brennan, and R. H. Goodman. “Engineered leucine zippers show that hemiphosphorylated CREB complexes are transcriptionally active.” Proc Natl Acad Sci U S A 90, no. 19 (October 1, 1993): 9046–50. https://doi.org/10.1073/pnas.90.19.9046.
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    • Brennan, R. G. “The winged-helix DNA-binding motif: another helix-turn-helix takeoff.” Cell 74, no. 5 (September 10, 1993): 773–76. https://doi.org/10.1016/0092-8674(93)90456-z.
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    • Schumacher, M. A., J. R. Macdonald, J. Björkman, S. L. Mowbray, and R. G. Brennan. “Structural analysis of the purine repressor, an Escherichia coli DNA-binding protein.” J Biol Chem 268, no. 17 (June 15, 1993): 12282–88.
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    • Spiro, C., J. P. Richards, S. Chandrasekaran, R. G. Brennan, and C. T. McMurray. “Secondary structure creates mismatched base pairs required for high-affinity binding of cAMP response element-binding protein to the human enkephalin enhancer.” Proc Natl Acad Sci U S A 90, no. 10 (May 15, 1993): 4606–10. https://doi.org/10.1073/pnas.90.10.4606.
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    • Wilson, K. P., L. M. Shewchuk, R. G. Brennan, A. J. Otsuka, and B. W. Matthews. “Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.” Proc Natl Acad Sci U S A 89, no. 19 (October 1, 1992): 9257–61. https://doi.org/10.1073/pnas.89.19.9257.
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    • Schumacher, M. A., K. Y. Choi, H. Zalkin, and R. G. Brennan. “Crystallization and preliminary X-ray studies on the co-repressor binding domain of the Escherichia coli purine repressor.” J Mol Biol 225, no. 4 (June 20, 1992): 1131–33. https://doi.org/10.1016/0022-2836(92)90111-v.
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    • Brennan, R. G. “DNA recognition by the helix-turn-helix motif. Current Opinion in Structural Biology 1992, 2: 100...-108.” Current Opinion in Structural Biology 2, no. 1 (January 1, 1992): 100–108. https://doi.org/10.1016/0959-440X(92)90184-9.
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    • Carr, D. W., R. E. Stofko-Hahn, I. D. Fraser, S. M. Bishop, T. S. Acott, R. G. Brennan, and J. D. Scott. “Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif.” J Biol Chem 266, no. 22 (August 5, 1991): 14188–92.
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    • Dixon, M. M., R. G. Brennan, and B. W. Matthews. “Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that gamma-chymotrypsin is a covalent acyl-enzyme adduct at low pH.” Int J Biol Macromol 13, no. 2 (April 1991): 89–96. https://doi.org/10.1016/0141-8130(91)90054-x.
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    • Brennan, R. G. “Interactions of the helix-turn-helix binding domain. Current opinion in structural biology 1991, 1:80-88.” Current Opinion in Structural Biology 1, no. 1 (January 1, 1991): 80–88. https://doi.org/10.1016/0959-440X(91)90015-L.
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    • Brennan, R. G. “Interactions of the helix-turn-helix binding domain.” Current Opinion in Structural Biology 1, no. 1 (1991): 80–88.
    • Brennan, R. G., S. L. Roderick, Y. Takeda, and B. W. Matthews. “Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex.” Proc Natl Acad Sci U S A 87, no. 20 (October 1990): 8165–69. https://doi.org/10.1073/pnas.87.20.8165.
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    • Brennan, R. G., and B. W. Matthews. “Structural basis of DNA-protein recognition.” Trends Biochem Sci 14, no. 7 (July 1989): 286–90. https://doi.org/10.1016/0968-0004(89)90066-2.
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    • Brennan, R. G., and B. W. Matthews. “The helix-turn-helix DNA binding motif.” J Biol Chem 264, no. 4 (February 5, 1989): 1903–6.
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    • Brennan, R. G., S. Vasu, B. W. Matthews, and A. J. Otsuka. “Crystallization of the bifunctional biotin operon repressor.” J Biol Chem 264, no. 1 (January 5, 1989): 5.
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    • Brennan, R. G., J. Wozniak, R. Faber, and B. W. Matthews. “Crystallization of mutant lysozymes from bacteriophage T4.” Journal of Crystal Growth 90, no. 1–3 (July 2, 1988): 160–67. https://doi.org/10.1016/0022-0248(88)90311-9.
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    • Brennan, R. G., J. Kim, Y. Takeda, W. F. Anderson, and B. W. Matthews. “Studies on the crystallization of the cro protein-pseudo OR3 complex.” Journal of Crystal Growth 76, no. 3 (August 2, 1986): 715–18. https://doi.org/10.1016/0022-0248(86)90189-2.
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    • Brennan, R. G., D. Pyzalska, W. J. Blonski, F. E. Hruska, and M. Sundaralingam. “Crystal structure of the promutagen O4-methylthymidine: importance of the anti conformation of the O(4) methoxy group and possible mispairing of O4-methylthymidine with guanine.” Biochemistry 25, no. 5 (March 11, 1986): 1181–85. https://doi.org/10.1021/bi00353a036.
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    • Brennan, R. G., Y. Takeda, J. Kim, W. F. Anderson, and B. W. Matthews. “Crystallization of a complex of cro repressor with a 17 base-pair operator.” J Mol Biol 188, no. 1 (March 5, 1986): 115–18. https://doi.org/10.1016/0022-2836(86)90488-2.
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    • Brennan, R. G., E. Westhof, and M. Sundaralingam. “Structure of a Z-DNA with two different backbone chain conformations. Stabilization of the decadeoxyoligonucleotide d(CGTACGTACG) by [Co(NH3)6]3+ binding to the guanine.” J Biomol Struct Dyn 3, no. 4 (February 1986): 649–65. https://doi.org/10.1080/07391102.1986.10508453.
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    • Brennan, R. G., and M. Sundaralingam. “Crystallization and preliminary crystallographic studies of the decadeoxyoligonucleotide d(CpGpTpApCpGpTpApCpG).” J Mol Biol 181, no. 4 (February 20, 1985): 561–63. https://doi.org/10.1016/0022-2836(85)90429-2.
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    • Brennan, R. G., N. S. Kondo, and M. Sundaralingam. “X-ray structure of cytidine-5'-O-dimethylphosphate. Novel stacking between the ribosyl O(2') hydroxyl oxygen atom and the base.” Nucleic Acids Res 12, no. 17 (September 11, 1984): 6813–25. https://doi.org/10.1093/nar/12.17.6813.
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    • Brennan, R. G., M. Sundaralingam, and N. S. Kondo. “Crystal Structure and Conformation of the Phosphotriester Adenosine 5’-O-(Diethyl phosphate). Possible Steric and Conformational Mechanisms for the Biochemical and Biological Effects Arising from Phosphate Alkylation.” Journal of the American Chemical Society 106, no. 19 (September 1, 1984): 5671–76. https://doi.org/10.1021/ja00331a043.
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    • Brennan, R. G., G. G. Privé, W. J. Blonski, F. E. Hruska, and M. Sundaralingam. “Crystal structure of O4-methyl uridine: stacking induced changes in the geometry of the pyrimidine ring and its mutagenic role.” J Biomol Struct Dyn 1, no. 4 (December 1983): 939–45. https://doi.org/10.1080/07391102.1983.10507495.
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    • Brennan, R. G., M. Sundaralingam, G. G. Privé, W. J. P. Blonski, and F. E. Hruska. “Molecular and Crystal Structure of O⁴-Methyluridine. Reaction Coordinates for an Incipient Nucleophilic Attack Seen by Short Intermolecular Sugar-Base Interactions.” Journal of the American Chemical Society 105, no. 26 (December 1, 1983): 7737–42. https://doi.org/10.1021/ja00364a046.
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    • Wells, R. D., R. Brennan, K. A. Chapman, T. C. Goodman, P. A. Hart, W. Hillen, D. R. Kellogg, et al. “Left-handed DNA helices, supercoiling, and the B-Z junction.” Cold Spring Harb Symp Quant Biol 47 Pt 1 (1983): 77–84. https://doi.org/10.1101/sqb.1983.047.01.010.
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    • Sundaralingam, M., R. G. Brennan, P. Swaminathan, T. P. Haromy, W. B. Dredel, J. N. BeMiller, M. Chmielewski, and D. Pat Cerretti. “Occurrence of the unusual 2C5(1C4) chair conformation in two carbohydrates and the reverse anomeric effect. x-ray structures of 3, 4, 5, 7-tetra-o-acetyl-2, 6-anhydro-d-glycero-d-ido-heptonamide (1) AND 3, 4, 5, 7-tetra-o-acetyl-2, 6- anhydro-d-glyceroL-gluco-heptonamide (2).” Journal of Carbohydrate Chemistry 1, no. 1 (January 1, 1982): 85–103. https://doi.org/10.1080/07328308208085080.
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    • Wells, R. D., R. Brennan, K. A. Chapman, T. C. Goodman, P. A. Hart, W. Hillen, D. R. Kellogg, et al. “Left-handed DNA helices, supercoiling, and the B-Z junction.” Cold Spring Harbor Symposia on Quantitative Biology 47, no. 1 (1982): 77–84.
    • Holtz, A., R. G. Brennan, D. Battista, and C. Terner. “Androgen control of an inhibitory modulator of phosphodiesterase in rat epididymis and prostate.” Endocrinology 108, no. 4 (April 1981): 1538–44. https://doi.org/10.1210/endo-108-4-1538.
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    • Terner, C., A. Holtz, R. G. Brennan, and D. Battista. “Androgen control of phosphodiesterase modulator in epididymis and prostate of rat.” Federation Proceedings 39, no. 3 II (January 1, 1980): 3765.

  • Conference Papers

    • Birukou, Ivan, Glenn W. Kaatz, and Richard G. Brennan. “Crystal Structure of a MepR-DNA Complex Reveals the Mechanism of Transcription Repression of S. Aureus Multidrug Efflux Pump mepA.” In Biophysical Journal, 104:256a-256a. Elsevier BV, 2013. https://doi.org/10.1016/j.bpj.2012.11.1436.
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• Teaching & Mentoring
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  Recent Courses

  • BIOCHEM 393: Research Independent Study 2020
  • BIOCHEM 593: Research Independent Study 2020
  • BIOCHEM 745S: Biochemistry Seminar 2020
  • BIOCHEM 746S: Biochemistry Seminar 2020
  • BIOCHEM 393: Research Independent Study 2019
  • BIOCHEM 593: Research Independent Study 2019
  • BIOCHEM 745S: Biochemistry Seminar 2019
  • BIOCHEM 746S: Biochemistry Seminar 2019
  • BIOCHEM 393: Research Independent Study 2018
  • BIOCHEM 593: Research Independent Study 2018
  • BIOCHEM 745S: Biochemistry Seminar 2018
  • BIOCHEM 746S: Biochemistry Seminar 2018

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