Pei Zhou | Scholars@Duke

Pei Zhou
Professor of Biochemistry

Protein-protein interactions play a pivotal role in the regulation of various cellular processes. The formation of higher order protein complexes is frequently accompanied by extensive structural remodeling of the individual components, varying from domain re-orientation to induced folding of unstructured elements. Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for macromolecular structure determination in solution. It has the unique advantage of being capable of elucidating the dynamic behavior of proteins during the process of recognition. Recent advances in NMR techniques have enabled the study of significantly larger proteins and protein complexes. These innovations have also led to faster and more accurate structure determination. My research interests focus on the exploration of molecular recognition and conformation variability of protein complexes in crucial biomedical processes using state-of-the-art NMR techniques.

Current Appointments & Affiliations

Professor of Biochemistry, Biochemistry, Basic Science Departments 2015
Member of the Duke Cancer Institute, Duke Cancer Institute, Institutes and Centers 2001

Contact Information

270 Sands Building, Research Drive, Durham, NC 27710
Duke Box 3711, Durham, NC 27710
peizhou@biochem.duke.edu (919) 668-6409

Background
Education, Training, & Certifications
- Post-Doct Fellow, Biological Chemistry, Harvard University 1998 - 2001
- Ph.D., Harvard University 1998
Previous Appointments & Affiliations
- Professor of Chemistry, Chemistry, Trinity College of Arts & Sciences 2015 - 2020
- Associate Professor of Biochemistry, Biochemistry, Basic Science Departments 2008 - 2015
- Associate Professor in the Department of Chemistry, Chemistry, Trinity College of Arts & Sciences 2010 - 2015
- Associate Professor of Chemistry, Chemistry, Trinity College of Arts & Sciences 2008 - 2009
- Assistant Professor of Biochemistry, Biochemistry, Basic Science Departments 2001 - 2008
- Assistant Professor of Chemistry, Chemistry, Trinity College of Arts & Sciences 2007 - 2008
- Assistant Professor of Chemistry, Chemistry, Trinity College of Arts & Sciences 2002 - 2007
- Instructor, Temporary in the Department of Biochemistry, Biochemistry, Basic Science Departments 2001
Research
Selected Grants
- Mechanism of carbon skeleton formation in molybdenum cofactor biosynthesis awarded by National Institutes of Health 2015 - 2024
- Inhibitors of TrkB Signaling awarded by National Institutes of Health 2019 - 2024
- Molecular mechanism of cephalosporin resistance of N. gonorrhoeae conferred by mutated PBP2 awarded by University of South Alabama 2022 - 2023
- The regulation dephosphorylated-CoA-capped RNA and innate immunity by MESH1 awarded by National Institutes of Health 2020 - 2023
- Discovery and validation of broadly effective LpxH inhibitors as novel therapeutics against multi-drug resistant Gram-negative pathogens awarded by National Institutes of Health 2019 - 2023
- Testing D5 compounds in a human version of a published ELISA system awarded by D5 Therapeutics, Inc 2021 - 2022
- Therapeutic targeting of MESH1 in renal cell carcinoma awarded by Department of Defense 2020 - 2022
- Deep Topological Sampling of Protein Structures - non-competing renewal for Year 4 awarded by National Institutes of Health 2017 - 2022
- Biochemical and functional investigation of the novel enzymatic activities of Mesh1 awarded by National Institutes of Health 2018 - 2022
- IND-enabling studies of the potent LpxC inhibitor LPC-233 as a novel antibiotic against Gram-negative pathogens awarded by Valanbio Therapeutics, Inc. 2020 - 2022
- Structure-Function Analysis of Chlamydia Secretion Chaperones awarded by National Institutes of Health 2016 - 2022
- Organization and Function of Cellular Structure awarded by National Institutes of Health 1975 - 2020
- Biochemistry and Structure of Lipid A Enzymes awarded by National Institutes of Health 2016 - 2020
- Molecular targets in peptidoglycan synthesis awarded by Medical University of South Carolina 2016 - 2020
- Discovery and validation of broadly effective LpxH inhibitors as novel therapeutics against multi-drug resistant Gram-negative pathogens awarded by National Institutes of Health 2018 - 2019
- Targeting Rev1-mediated Translesion Synthesis for Cancer Therapy awarded by National Institutes of Health 2015 - 2017
- LpxC inhibitors as a novel class of antibiotics against N. gonorrhoeae awarded by National Institutes of Health 2011 - 2017
- Preliminary Safety Screening of Duke PlxC inhibitors as Novel Antibiotics against Gram-negative Pathogens awarded by North Carolina Biotechnology Center 2015 - 2016
- Structural Biology and Biophysics Training Program awarded by National Institutes of Health 1994 - 2015
- Biosynthesis And Function Of Lipopolysaccharides 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
- Automated detection of protein crystals in high-throughput crystallography experiments awarded by North Carolina Biotechnology Center 2014 - 2015
- New Console and Cold Probe for the Duke 600 MHz NMR Spectrometer System awarded by National Institutes of Health 2013 - 2014
- Structural and Biochemical Studies of LpxC Inhibition awarded by National Institutes of Health 2003 - 2014
- Lipid A Modification Systems in Gram-Negative Bacteria awarded by National Institutes of Health 1995 - 2013
- Automated NMR Assignment and Protein Structure Determination awarded by National Institutes of Health 2006 - 2012
- Structural, Biochemical and Functional Studies of RNAPII CTD Interacting Proteins awarded by National Institutes of Health 2008 - 2012
- Replacement Equipment Components for an 800 MHz NMR Spectrometer awarded by National Institutes of Health 2010 - 2011
- Regulation of Germline Stem Cell Division in Drosophila awarded by National Institutes of Health 1996 - 2006
- Structure and Regulation of hsp90 Chaperones awarded by National Institutes of Health 2005
External Relationships
- D5 Therapeutics
- LVM Biosciences
- Valanbio Therapeutics
Publications & Artistic Works
Selected Publications
- Academic Articles
  - Kumar, Shivesh, Raul Zavaliev, Qinglin Wu, Ye Zhou, Jie Cheng, Lucas Dillard, Jordan Powers, et al. “Structural basis of NPR1 in activating plant immunity.” Nature 605, no. 7910 (May 2022): 561–66. https://doi.org/10.1038/s41586-022-04699-w.
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  - Victor, Joshua, Tristan Jordan, Erica Lamkin, Kanayo Ikeh, Anthony March, Justin Frere, Andrew Crompton, et al. “SARS-CoV-2 hijacks host cell genome instability pathways.” Res Sq, April 14, 2022. https://doi.org/10.21203/rs.3.rs-1556634/v1.
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  - Sun, Tianai, Chien-Kuang Cornelia Ding, Yuning Zhang, Yang Zhang, Chao-Chieh Lin, Jianli Wu, Yasaman Setayeshpour, et al. “MESH1 knockdown triggers proliferation arrest through TAZ repression.” Cell Death Dis 13, no. 3 (March 10, 2022): 221. https://doi.org/10.1038/s41419-022-04663-6.
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  - Wüllner, Dominik, Maren Gesper, Annika Haupt, Xiaofei Liang, Pei Zhou, Pascal Dietze, Franz Narberhaus, and Julia E. Bandow. “Adaptive Responses of Pseudomonas aeruginosa to Treatment with Antibiotics.” Antimicrob Agents Chemother 66, no. 1 (January 18, 2022): e0087821. https://doi.org/10.1128/AAC.00878-21.
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  - Victor, Joshua, Jamie Deutsch, Annalis Whitaker, Erica N. Lamkin, Anthony March, Pei Zhou, Jason W. Botten, and Nimrat Chatterjee. “SARS-CoV-2 triggers DNA damage response in Vero E6 cells.” Biochem Biophys Res Commun 579 (November 19, 2021): 141–45. https://doi.org/10.1016/j.bbrc.2021.09.024.
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  - Ikeh, Kanayo E., Erica N. Lamkin, Andrew Crompton, Jamie Deutsch, Kira J. Fisher, Mark Gray, David J. Argyle, et al. “REV1 Inhibition Enhances Radioresistance and Autophagy.” Cancers (Basel) 13, no. 21 (October 21, 2021). https://doi.org/10.3390/cancers13215290.
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  - Fenton, Benjamin A., Joshua Tomberg, Carly A. Sciandra, Robert A. Nicholas, Christopher Davies, and Pei Zhou. “Mutations in PBP2 from ceftriaxone-resistant Neisseria gonorrhoeae alter the dynamics of the β3-β4 loop to favor a low-affinity drug-binding state.” J Biol Chem 297, no. 4 (October 2021): 101188. https://doi.org/10.1016/j.jbc.2021.101188.
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  - Yoo, Chan Yul, Jiangman He, Qing Sang, Yongjian Qiu, Lingyun Long, Ruth Jean-Ae Kim, Emily G. Chong, et al. “Direct photoresponsive inhibition of a p53-like transcription activation domain in PIF3 by Arabidopsis phytochrome B.” Nat Commun 12, no. 1 (September 23, 2021): 5614. https://doi.org/10.1038/s41467-021-25909-5.
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  - Adhikari, Hema, Walaa E. Kattan, Shivesh Kumar, Pei Zhou, John F. Hancock, and Christopher M. Counter. “Oncogenic KRAS is dependent upon an EFR3A-PI4KA signaling axis for potent tumorigenic activity.” Nat Commun 12, no. 1 (September 9, 2021): 5248. https://doi.org/10.1038/s41467-021-25523-5.
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  - Lin, Chao-Chieh, Chien-Kuang Cornelia Ding, Tianai Sun, Jianli Wu, Kai-Yuan Chen, Pei Zhou, and Jen-Tsan Chi. “The regulation of ferroptosis by MESH1 through the activation of the integrative stress response.” Cell Death Dis 12, no. 8 (July 22, 2021): 727. https://doi.org/10.1038/s41419-021-04018-7.
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  - Chin, Chui-Yoke, Jinshi Zhao, Anna C. Llewellyn, Igor Golovliov, Anders Sjöstedt, Pei Zhou, and David S. Weiss. “Francisella FlmX broadly affects lipopolysaccharide modification and virulence.” Cell Rep 35, no. 11 (June 15, 2021): 109247. https://doi.org/10.1016/j.celrep.2021.109247.
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  - Zhou, Pei, and Jiyong Hong. “Structure- and Ligand-Dynamics-Based Design of Novel Antibiotics Targeting Lipid A Enzymes LpxC and LpxH in Gram-Negative Bacteria.” Acc Chem Res 54, no. 7 (April 6, 2021): 1623–34. https://doi.org/10.1021/acs.accounts.0c00880.
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  - Martorana, Alessandra M., Elisabete C. C. M. Moura, Paola Sperandeo, Flavia Di Vincenzo, Xiaofei Liang, Eric Toone, Pei Zhou, and Alessandra Polissi. “Degradation of Components of the Lpt Transenvelope Machinery Reveals LPS-Dependent Lpt Complex Stability in Escherichia coli.” Front Mol Biosci 8 (2021): 758228. https://doi.org/10.3389/fmolb.2021.758228.
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  - Chatterjee, Nimrat, Matthew A. Whitman, Cynthia A. Harris, Sophia M. Min, Oliver Jonas, Evan C. Lien, Alba Luengo, et al. “REV1 inhibitor JH-RE-06 enhances tumor cell response to chemotherapy by triggering senescence hallmarks.” Proc Natl Acad Sci U S A 117, no. 46 (November 17, 2020): 28918–21. https://doi.org/10.1073/pnas.2016064117.
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  - Vassel, Faye-Marie, Ke Bian, Graham C. Walker, and Michael T. Hemann. “Rev7 loss alters cisplatin response and increases drug efficacy in chemotherapy-resistant lung cancer.” Proc Natl Acad Sci U S A 117, no. 46 (November 17, 2020): 28922–24. https://doi.org/10.1073/pnas.2016067117.
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  - Kwak, Seung-Hwa, C Skyler Cochrane, Amanda F. Ennis, Won Young Lim, Caroline G. Webster, Jae Cho, Benjamin A. Fenton, Pei Zhou, and Jiyong Hong. “Synthesis and evaluation of sulfonyl piperazine LpxH inhibitors.” Bioorg Chem 102 (September 2020): 104055. https://doi.org/10.1016/j.bioorg.2020.104055.
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  - Ding, Chien-Kuang Cornelia, Joshua Rose, Tianai Sun, Jianli Wu, Po-Han Chen, Chao-Chieh Lin, Wen-Hsuan Yang, et al. “MESH1 is a cytosolic NADPH phosphatase that regulates ferroptosis.” Nat Metab 2, no. 3 (March 2020): 270–77. https://doi.org/10.1038/s42255-020-0181-1.
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  - Cho, Jae, Minhee Lee, C Skyler Cochrane, Caroline G. Webster, Benjamin A. Fenton, Jinshi Zhao, Jiyong Hong, and Pei Zhou. “Structural basis of the UDP-diacylglucosamine pyrophosphohydrolase LpxH inhibition by sulfonyl piperazine antibiotics.” Proc Natl Acad Sci U S A 117, no. 8 (February 25, 2020): 4109–16. https://doi.org/10.1073/pnas.1912876117.
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  - Ji, Yuhyun, Jinsu An, Dohyeon Hwang, Da Hui Ha, Sang Min Lim, Chankyu Lee, Jinshi Zhao, et al. “Metabolic engineering of Escherichia coli to produce a monophosphoryl lipid A adjuvant.” Metab Eng 57 (January 2020): 193–202. https://doi.org/10.1016/j.ymben.2019.11.009.
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  - Wojtaszek, Jessica L., Nimrat Chatterjee, Javaria Najeeb, Azucena Ramos, Minhee Lee, Ke Bian, Jenny Y. Xue, et al. “A Small Molecule Targeting Mutagenic Translesion Synthesis Improves Chemotherapy.” Cell 178, no. 1 (June 27, 2019): 152-159.e11. https://doi.org/10.1016/j.cell.2019.05.028.
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  - Zhao, Jinshi, Jinsu An, Dohyeon Hwang, Qinglin Wu, Su Wang, Robert A. Gillespie, Eun Gyeong Yang, Ziqiang Guan, Pei Zhou, and Hak Suk Chung. “The Lipid A 1-Phosphatase, LpxE, Functionally Connects Multiple Layers of Bacterial Envelope Biogenesis.” Mbio 10, no. 3 (June 18, 2019). https://doi.org/10.1128/mBio.00886-19.
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  - Yang, Emily J., Chan Yul Yoo, Jiangxin Liu, He Wang, Jun Cao, Fay-Wei Li, Kathleen M. Pryer, et al. “NCP activates chloroplast transcription by controlling phytochrome-dependent dual nuclear and plastidial switches.” Nat Commun 10, no. 1 (June 14, 2019): 2630. https://doi.org/10.1038/s41467-019-10517-1.
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  - Lee, Minhee, Jinshi Zhao, Seung-Hwa Kwak, Jae Cho, Myungju Lee, Robert A. Gillespie, Do-Yeon Kwon, et al. “Structure-Activity Relationship of Sulfonyl Piperazine LpxH Inhibitors Analyzed by an LpxE-Coupled Malachite Green Assay.” Acs Infect Dis 5, no. 4 (April 12, 2019): 641–51. https://doi.org/10.1021/acsinfecdis.8b00364.
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  - Cristillo, Anthony D., Claire C. Bristow, Elizabeth Torrone, Jo-Anne Dillon, Robert D. Kirkcaldy, Huan Dong, Yonatan H. Grad, et al. “Antimicrobial Resistance in Neisseria gonorrhoeae: Proceedings of the STAR Sexually Transmitted Infection-Clinical Trial Group Programmatic Meeting.” Sex Transm Dis 46, no. 3 (March 2019): e18–25. https://doi.org/10.1097/OLQ.0000000000000929.
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  - Yang, E. J., C. Y. Yoo, J. Liu, H. Wang, J. Cao, F. Li, K. M. Pryer, T. Sun, D. Weigel, and P. Zhou. “NCP activates chloroplast transcription by controlling phytochrome-dependent dual nuclear and plastidial switches.” Nature Communications 10, no. 1 (2019): 1–13.
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  - Wang, Tao, Yonghui Yu, Xiaofei Liang, Shengdong Luo, Zemin He, Zhihui Sun, Yongqiang Jiang, Anders Omsland, Pei Zhou, and Lihua Song. “Lipid A Has Significance for Optimal Growth of Coxiella burnetii in Macrophage-Like THP-1 Cells and to a Lesser Extent in Axenic Media and Non-phagocytic Cells.” Front Cell Infect Microbiol 8 (2018): 192. https://doi.org/10.3389/fcimb.2018.00192.
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  - Liu, Yixiang, Joshua Rose, Shaojia Huang, Yangbo Hu, Qiong Wu, Dan Wang, Conggang Li, Maili Liu, Pei Zhou, and Ling Jiang. “A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases.” Nat Commun 8, no. 1 (December 13, 2017): 2104. https://doi.org/10.1038/s41467-017-02310-9.
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  - Zhou, Pei, and Jinshi Zhao. “Structure, inhibition, and regulation of essential lipid A enzymes.” Biochim Biophys Acta Mol Cell Biol Lipids 1862, no. 11 (November 2017): 1424–38. https://doi.org/10.1016/j.bbalip.2016.11.014.
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  - Wu, Qinglin, Benjamin A. Fenton, Jessica L. Wojtaszek, and Pei Zhou. “Probing the excited-state chemical shifts and exchange parameters by nitrogen-decoupled amide proton chemical exchange saturation transfer (HNdec-CEST).” Chem Commun (Camb) 53, no. 61 (July 27, 2017): 8541–44. https://doi.org/10.1039/c7cc05021f.
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  - Lemaître, Nadine, Xiaofei Liang, Javaria Najeeb, Chul-Jin Lee, Marie Titecat, Emmanuelle Leteurtre, Michel Simonet, Eric J. Toone, Pei Zhou, and Florent Sebbane. “Curative Treatment of Severe Gram-Negative Bacterial Infections by a New Class of Antibiotics Targeting LpxC.” Mbio 8, no. 4 (July 25, 2017). https://doi.org/10.1128/mBio.00674-17.
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  - Zentella, Rodolfo, Ning Sui, Benjamin Barnhill, Wen-Ping Hsieh, Jianhong Hu, Jeffrey Shabanowitz, Michael Boyce, et al. “The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth repressor DELLA.” Nat Chem Biol 13, no. 5 (May 2017): 479–85. https://doi.org/10.1038/nchembio.2320.
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  - Titecat, Marie, Xiaofei Liang, Chul-Jin Lee, Audrey Charlet, Didier Hocquet, Thierry Lambert, Jean-Marie Pagès, et al. “High susceptibility of MDR and XDR Gram-negative pathogens to biphenyl-diacetylene-based difluoromethyl-allo-threonyl-hydroxamate LpxC inhibitors.” J Antimicrob Chemother 71, no. 10 (October 2016): 2874–82. https://doi.org/10.1093/jac/dkw210.
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  - Cho, Jae, Chul-Jin Lee, Jinshi Zhao, Hayley E. Young, and Pei Zhou. “Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis.” Nat Microbiol 1, no. 11 (August 15, 2016): 16154. https://doi.org/10.1038/nmicrobiol.2016.154.
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  - Wu, Qinglin, Brian E. Coggins, and Pei Zhou. “Unbiased measurements of reconstruction fidelity of sparsely sampled magnetic resonance spectra.” Nat Commun 7 (July 27, 2016): 12281. https://doi.org/10.1038/ncomms12281.
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  - Liang, Xiaofei, Ramesh Gopalaswamy, Frank Navas, Eric J. Toone, and Pei Zhou. “A Scalable Synthesis of the Difluoromethyl-allo-threonyl Hydroxamate-Based LpxC Inhibitor LPC-058.” J Org Chem 81, no. 10 (May 20, 2016): 4393–98. https://doi.org/10.1021/acs.joc.6b00589.
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  - Young, Hayley E., Jinshi Zhao, Jeffrey R. Barker, Ziqiang Guan, Raphael H. Valdivia, and Pei Zhou. “Discovery of the Elusive UDP-Diacylglucosamine Hydrolase in the Lipid A Biosynthetic Pathway in Chlamydia trachomatis.” Mbio 7, no. 2 (March 22, 2016): e00090. https://doi.org/10.1128/mBio.00090-16.
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  - Lee, Chul-Jin, Xiaofei Liang, Qinglin Wu, Javaria Najeeb, Jinshi Zhao, Ramesh Gopalaswamy, Marie Titecat, et al. “Drug design from the cryptic inhibitor envelope.” Nat Commun 7 (February 25, 2016): 10638. https://doi.org/10.1038/ncomms10638.
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  - Deis, Lindsay N., Qinglin Wu, You Wang, Yang Qi, Kyle G. Daniels, Pei Zhou, and Terrence G. Oas. “Suppression of conformational heterogeneity at a protein-protein interface.” Proc Natl Acad Sci U S A 112, no. 29 (July 21, 2015): 9028–33. https://doi.org/10.1073/pnas.1424724112.
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  - Martin, Jeffrey W., Pei Zhou, and Bruce R. Donald. “Systematic solution to homo-oligomeric structures determined by NMR.” Proteins 83, no. 4 (April 2015): 651–61. https://doi.org/10.1002/prot.24768.
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  - Wojtaszek, Jessica L., Su Wang, Hyungjin Kim, Qinglin Wu, Alan D. D’Andrea, and Pei Zhou. “Ubiquitin recognition by FAAP20 expands the complex interface beyond the canonical UBZ domain.” Nucleic Acids Res 42, no. 22 (December 16, 2014): 13997–5. https://doi.org/10.1093/nar/gku1153.
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  - Emptage, Ryan P., Nam K. Tonthat, John D. York, Maria A. Schumacher, and Pei Zhou. “Structural basis of lipid binding for the membrane-embedded tetraacyldisaccharide-1-phosphate 4'-kinase LpxK.” J Biol Chem 289, no. 35 (August 29, 2014): 24059–68. https://doi.org/10.1074/jbc.M114.589986.
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  - Sampson, Timothy R., Brooke A. Napier, Max R. Schroeder, Rogier Louwen, Jinshi Zhao, Chui-Yoke Chin, Hannah K. Ratner, et al. “A CRISPR-Cas system enhances envelope integrity mediating antibiotic resistance and inflammasome evasion.” Proc Natl Acad Sci U S A 111, no. 30 (July 29, 2014): 11163–68. https://doi.org/10.1073/pnas.1323025111.
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  - Wang, Su, and Pei Zhou. “Sparsely-sampled, high-resolution 4-D omit spectra for detection and assignment of intermolecular NOEs of protein complexes.” J Biomol Nmr 59, no. 2 (June 2014): 51–56. https://doi.org/10.1007/s10858-014-9834-2.
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  - Lee, Chul-Jin, Xiaofei Liang, Ramesh Gopalaswamy, Javaria Najeeb, Eugene D. Ark, Eric J. Toone, and Pei Zhou. “Structural basis of the promiscuous inhibitor susceptibility of Escherichia coli LpxC.” Acs Chem Biol 9, no. 1 (January 17, 2014): 237–46. https://doi.org/10.1021/cb400067g.
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  - Masoudi, Ali, Christian R. H. Raetz, Pei Zhou, and Charles W. Pemble. “Chasing acyl carrier protein through a catalytic cycle of lipid A production.” Nature 505, no. 7483 (January 16, 2014): 422–26. https://doi.org/10.1038/nature12679.
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  - Masoudi, A., C. R. H. Raetz, P. Zhou, and C. W. Pemble IV. “Chasing acyl carrier protein through a catalytic cycle of lipid A production.” Nature 505, no. 7483 (January 1, 2014): 422–26. https://doi.org/10.1038/nature12679.
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  - Young, Hayley E., Matthew P. Donohue, Tatyana I. Smirnova, Alex I. Smirnov, and Pei Zhou. “The UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis utilizes Mn2+ cluster for catalysis.” J Biol Chem 288, no. 38 (September 20, 2013): 26987–1. https://doi.org/10.1074/jbc.M113.497636.
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  - Liang, Xiaofei, Chul-Jin Lee, Jinshi Zhao, Eric J. Toone, and Pei Zhou. “Synthesis, structure, and antibiotic activity of aryl-substituted LpxC inhibitors.” J Med Chem 56, no. 17 (September 12, 2013): 6954–66. https://doi.org/10.1021/jm4007774.
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  - Chung, Ben C., Jinshi Zhao, Robert A. Gillespie, Do-Yeon Kwon, Ziqiang Guan, Jiyong Hong, Pei Zhou, and Seok-Yong Lee. “Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis.” Science 341, no. 6149 (August 30, 2013): 1012–16. https://doi.org/10.1126/science.1236501.
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  - Feng, Yesu, Thomas Theis, Xiaofei Liang, Qiu Wang, Pei Zhou, and Warren S. Warren. “Storage of hydrogen spin polarization in long-lived 13C2 singlet order and implications for hyperpolarized magnetic resonance imaging.” J Am Chem Soc 135, no. 26 (July 3, 2013): 9632–35. https://doi.org/10.1021/ja404936p.
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  - Liu, Jiangxin, Shilong Fan, Chul-Jin Lee, Arno L. Greenleaf, and Pei Zhou. “Specific interaction of the transcription elongation regulator TCERG1 with RNA polymerase II requires simultaneous phosphorylation at Ser2, Ser5, and Ser7 within the carboxyl-terminal domain repeat.” J Biol Chem 288, no. 15 (April 12, 2013): 10890–901. https://doi.org/10.1074/jbc.M113.460238.
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  - Tripathy, C., A. K. Yan, P. Zhou, and B. R. Donald. “Extracting structural information from residual chemical shift anisotropy: Analytic solutions for peptide plane orientations and applications to determine protein structure.” Lecture Notes in Computer Science (Including Subseries Lecture Notes in Artificial Intelligence and Lecture Notes in Bioinformatics) 7821 LNBI (April 3, 2013): 271–84. https://doi.org/10.1007/978-3-642-37195-0_25.
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  - Emptage, Ryan P., Charles W. Pemble, John D. York, Christian R. H. Raetz, and Pei Zhou. “Mechanistic characterization of the tetraacyldisaccharide-1-phosphate 4'-kinase LpxK involved in lipid A biosynthesis.” Biochemistry 52, no. 13 (April 2, 2013): 2280–90. https://doi.org/10.1021/bi400097z.
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  - Zeng, Daina, Jinshi Zhao, Hak Suk Chung, Ziqiang Guan, Christian R. H. Raetz, and Pei Zhou. “Mutants resistant to LpxC inhibitors by rebalancing cellular homeostasis.” J Biol Chem 288, no. 8 (February 22, 2013): 5475–86. https://doi.org/10.1074/jbc.M112.447607.
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  - Chung, B. C., J. Zhao, R. A. Gillespie, D. Y. Kwon, Z. Guan, J. Hong, P. Zhou, and S. Y. Lee. “Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis.” Science 341, no. 6149 (2013): 1012–16. https://doi.org/10.1126/science.1240985.
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  - Zeng, Jianyang, Pei Zhou, and Bruce Randall Donald. “HASH: a program to accurately predict protein Hα shifts from neighboring backbone shifts.” J Biomol Nmr 55, no. 1 (January 2013): 105–18. https://doi.org/10.1007/s10858-012-9693-7.
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  - Coggins, Brian E., Jonathan W. Werner-Allen, Anthony Yan, and Pei Zhou. “Rapid protein global fold determination using ultrasparse sampling, high-dynamic range artifact suppression, and time-shared NOESY.” J Am Chem Soc 134, no. 45 (November 14, 2012): 18619–30. https://doi.org/10.1021/ja307445y.
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  - Wojtaszek, Jessica, Chul-Jin Lee, Sanjay D’Souza, Brenda Minesinger, Hyungjin Kim, Alan D. D’Andrea, Graham C. Walker, and Pei Zhou. “Structural basis of Rev1-mediated assembly of a quaternary vertebrate translesion polymerase complex consisting of Rev1, heterodimeric polymerase (Pol) ζ, and Pol κ.” J Biol Chem 287, no. 40 (September 28, 2012): 33836–46. https://doi.org/10.1074/jbc.M112.394841.
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  - Wojtaszek, Jessica, Jiangxin Liu, Sanjay D’Souza, Su Wang, Yaohua Xue, Graham C. Walker, and Pei Zhou. “Multifaceted recognition of vertebrate Rev1 by translesion polymerases ζ and κ.” J Biol Chem 287, no. 31 (July 27, 2012): 26400–408. https://doi.org/10.1074/jbc.M112.380998.
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  - Wen, Jie, Pei Zhou, and Jihui Wu. “Efficient acquisition of high-resolution 4-D diagonal-suppressed methyl-methyl NOESY for large proteins.” J Magn Reson 218 (May 2012): 128–32. https://doi.org/10.1016/j.jmr.2012.02.021.
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  - Werner-Allen, Jon W., and Pei Zhou. “¹H, ¹³C and ¹⁵N backbone and side-chain resonance assignments of Drosophila melanogaster Ssu72.” Biomol Nmr Assign 6, no. 1 (April 2012): 57–61. https://doi.org/10.1007/s12104-011-9325-2.
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  - Young, Hayley E., Louis E. Metzger, John K. Lee, Robert M. Stroud, Pei Zhou, and Christian R. H. Raetz. “Enzymatic and structural studies of UDP-2,3-diacylglucosamine hydrolysis in lipid A biosynthesis.” Faseb Journal 26 (April 1, 2012).
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  - Tripathy, Chittaranjan, Jianyang Zeng, Pei Zhou, and Bruce Randall Donald. “Protein loop closure using orientational restraints from NMR data.” Proteins 80, no. 2 (February 2012): 433–53. https://doi.org/10.1002/prot.23207.
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  - Moss, Marcia L., Gary Powell, Miles A. Miller, Lori Edwards, Bin Qi, Qing-Xiang Amy Sang, Bart De Strooper, et al. “ADAM9 inhibition increases membrane activity of ADAM10 and controls α-secretase processing of amyloid precursor protein.” J Biol Chem 286, no. 47 (November 25, 2011): 40443–51. https://doi.org/10.1074/jbc.M111.280495.
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  - Martin, Jeffrey W., Anthony K. Yan, Chris Bailey-Kellogg, Pei Zhou, and Bruce R. Donald. “A geometric arrangement algorithm for structure determination of symmetric protein homo-oligomers from NOEs and RDCs.” J Comput Biol 18, no. 11 (November 2011): 1507–23. https://doi.org/10.1089/cmb.2011.0173.
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  - Zeng, Jianyang, Kyle E. Roberts, Pei Zhou, and Bruce Randall Donald. “A Bayesian approach for determining protein side-chain rotamer conformations using unassigned NOE data.” J Comput Biol 18, no. 11 (November 2011): 1661–79. https://doi.org/10.1089/cmb.2011.0172.
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  - Zeng, Jianyang, Pei Zhou, and Bruce Randall Donald. “Protein side-chain resonance assignment and NOE assignment using RDC-defined backbones without TOCSY data.” J Biomol Nmr 50, no. 4 (August 2011): 371–95. https://doi.org/10.1007/s10858-011-9522-4.
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  - Nguyen, Bidong D., Doreen Cunningham, Xiaofei Liang, Xin Chen, Eric J. Toone, Christian R. H. Raetz, Pei Zhou, and Raphael H. Valdivia. “Lipooligosaccharide is required for the generation of infectious elementary bodies in Chlamydia trachomatis.” Proc Natl Acad Sci U S A 108, no. 25 (June 21, 2011): 10284–89. https://doi.org/10.1073/pnas.1107478108.
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  - Martin, Jeffrey W., Anthony K. Yan, Chris Bailey-Kellogg, Pei Zhou, and Bruce R. Donald. “A graphical method for analyzing distance restraints using residual dipolar couplings for structure determination of symmetric protein homo-oligomers.” Protein Sci 20, no. 6 (June 2011): 970–85. https://doi.org/10.1002/pro.620.
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  - Chen, J., Q. Li, C. C. Liu, P. Zhou, G. Bu, and J. Wang. “Erratum to: NMR structure note: Solution structure of the core domain of MESD that is essential for proper folding of LRP5/6 (Journal of Biomolecular NMR (2010) 47 (283-288) DOI:10.1007/s10858-010-9426-8).” Journal of Biomolecular Nmr 50, no. 1 (May 1, 2011): 101. https://doi.org/10.1007/s10858-011-9476-6.
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  - Wen, Jie, Jihui Wu, and Pei Zhou. “Sparsely sampled high-resolution 4-D experiments for efficient backbone resonance assignment of disordered proteins.” J Magn Reson 209, no. 1 (March 2011): 94–100. https://doi.org/10.1016/j.jmr.2010.12.012.
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  - Werner-Allen, Jon W., Chul-Jin Lee, Pengda Liu, Nathan I. Nicely, Su Wang, Arno L. Greenleaf, and Pei Zhou. “cis-Proline-mediated Ser(P)5 dephosphorylation by the RNA polymerase II C-terminal domain phosphatase Ssu72.” J Biol Chem 286, no. 7 (February 18, 2011): 5717–26. https://doi.org/10.1074/jbc.M110.197129.
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  - Lee, Chul-Jin, Xiaofei Liang, Xin Chen, Daina Zeng, Sang Hoon Joo, Hak Suk Chung, Adam W. Barb, et al. “Species-specific and inhibitor-dependent conformations of LpxC: implications for antibiotic design.” Chem Biol 18, no. 1 (January 28, 2011): 38–47. https://doi.org/10.1016/j.chembiol.2010.11.011.
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  - Liang, Xiaofei, Chul-Jin Lee, Xin Chen, Hak Suk Chung, Daina Zeng, Christian R. H. Raetz, Yaoxian Li, Pei Zhou, and Eric J. Toone. “Syntheses, structures and antibiotic activities of LpxC inhibitors based on the diacetylene scaffold.” Bioorg Med Chem 19, no. 2 (January 15, 2011): 852–60. https://doi.org/10.1016/j.bmc.2010.12.017.
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  - Martin, J. W., A. K. Yan, C. Bailey-Kellogg, P. Zhou, and B. R. Donald. “A Geometric Arrangement Algorithm for Structure Determination of Symmetric Protein Homo-oligomers from NOEs and RDCs.” Lecture Notes in Computer Science (Including Subseries Lecture Notes in Artificial Intelligence and Lecture Notes in Bioinformatics) 6577 LNBI (January 1, 2011): 222–37. https://doi.org/10.1007/978-3-642-20036-6_21.
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  - Tripathy, C., J. Zeng, P. Zhou, and B. R. Donald. “Protein Loop Closure Using Orientational Restraints from NMR Data.” Lecture Notes in Computer Science (Including Subseries Lecture Notes in Artificial Intelligence and Lecture Notes in Bioinformatics) 6577 LNBI (January 1, 2011): 483–98. https://doi.org/10.1007/978-3-642-20036-6_43.
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  - Zeng, J., K. E. Roberts, P. Zhou, and B. R. Donald. “A Bayesian Approach for Determining Protein Side-Chain Rotamer Conformations Using Unassigned NOE Data.” Lecture Notes in Computer Science (Including Subseries Lecture Notes in Artificial Intelligence and Lecture Notes in Bioinformatics) 6577 LNBI (January 1, 2011): 563–78. https://doi.org/10.1007/978-3-642-20036-6_49.
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  - Zeng, J., P. Zhou, and B. R. Donald. “A Markov random field framework for protein side-chain resonance assignment.” Lecture Notes in Computer Science (Including Subseries Lecture Notes in Artificial Intelligence and Lecture Notes in Bioinformatics) 6044 LNBI (December 23, 2010): 550–70. https://doi.org/10.1007/978-3-642-12683-3_36.
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  - Hard, Ryan L., Jiangxin Liu, Juan Shen, Pei Zhou, and Dehua Pei. “HDAC6 and Ubp-M BUZ domains recognize specific C-terminal sequences of proteins.” Biochemistry 49, no. 50 (December 21, 2010): 10737–46. https://doi.org/10.1021/bi101014s.
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  - Yershova, A., C. Tripathy, P. Zhou, and B. R. Donald. “Algorithms and analytic solutions using sparse residual dipolar couplings for high-resolution automated protein backbone structure determination by NMR.” Springer Tracts in Advanced Robotics 68, no. STAR (December 20, 2010): 355–72. https://doi.org/10.1007/978-3-642-17452-0_21.
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  - Woodruff, Rachel V., Martha G. Bomar, Sanjay D’Souza, Pei Zhou, and Graham C. Walker. “The unusual UBZ domain of Saccharomyces cerevisiae polymerase η.” Dna Repair (Amst) 9, no. 11 (November 10, 2010): 1130–41. https://doi.org/10.1016/j.dnarep.2010.08.001.
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  - Coggins, Brian E., Ronald A. Venters, and Pei Zhou. “Radial sampling for fast NMR: Concepts and practices over three decades.” Prog Nucl Magn Reson Spectrosc 57, no. 4 (November 2010): 381–419. https://doi.org/10.1016/j.pnmrs.2010.07.001.
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  - Chen, Jianglei, Qianqian Li, Chia-Chen Liu, Pei Zhou, Guojun Bu, and Jianjun Wang. “NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.” J Biomol Nmr 47, no. 4 (August 2010): 283–88. https://doi.org/10.1007/s10858-010-9426-8.
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  - Werner-Allen, Jon W., Brian E. Coggins, and Pei Zhou. “Fast acquisition of high resolution 4-D amide-amide NOESY with diagonal suppression, sparse sampling and FFT-CLEAN.” J Magn Reson 204, no. 1 (May 2010): 173–78. https://doi.org/10.1016/j.jmr.2010.02.017.
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  - Barb, Adam W., Ling Jiang, Christian R. H. Raetz, and Pei Zhou. “Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240.” Biomol Nmr Assign 4, no. 1 (April 2010): 37–40. https://doi.org/10.1007/s12104-009-9201-5.
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  - Lee, Chul-Jin, Xiaofei Liang, Eugene Park, Daina Zeng, Shauna Swanson, Xin Chen, Robert A. Nicholas, Christian R. H. Raetz, Eric J. Toone, and Pei Zhou. “Structure-activity relationships of diacetylene-based LpxC inhibitors.” Faseb Journal 24 (April 2010).
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  - Zeng, Daina, Pei Zhou, and Christian R. H. Raetz. “Characterization of E. coli mutants resistant to LpxC inhibitors.” Faseb Journal 24 (April 2010).
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  - Bomar, Martha G., Sanjay D’Souza, Marzena Bienko, Ivan Dikic, Graham C. Walker, and Pei Zhou. “Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y family DNA polymerases iota and Rev1.” Mol Cell 37, no. 3 (February 12, 2010): 408–17. https://doi.org/10.1016/j.molcel.2009.12.038.
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  - Zhou, Pei, and Gerhard Wagner. “Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies.” J Biomol Nmr 46, no. 1 (January 2010): 23–31. https://doi.org/10.1007/s10858-009-9371-6.
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  - Zeng, Jianyang, Jeffrey Boyles, Chittaranjan Tripathy, Lincong Wang, Anthony Yan, Pei Zhou, and Bruce Randall Donald. “High-resolution protein structure determination starting with a global fold calculated from exact solutions to the RDC equations.” J Biomol Nmr 45, no. 3 (November 2009): 265–81. https://doi.org/10.1007/s10858-009-9366-3.
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  - Barb, A. W., T. M. Leavy, L. I. Robins, Z. Guan, D. A. Six, P. Zhou, M. J. Hangauer, C. R. Bertozzi, and C. Raetz. “Correction to uridine-based inhibitors as new leads for antibiotics targeting Escherichia coli LpxC (Biochemistry (2009) 48, (3068) DOI: 10.1021/bi900167q).” Biochemistry 48, no. 32 (August 18, 2009): 7776. https://doi.org/10.1021/bi9012066.
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  - Barb, Adam W., Tanya M. Leavy, Lori I. Robins, Ziqiang Guan, David A. Six, Pei Zhou, Matthew J. Hangauer, Carolyn R. Bertozzi, and Christian R. H. Raetz. “Uridine-based inhibitors as new leads for antibiotics targeting Escherichia coli LpxC.” Biochemistry 48, no. 14 (April 14, 2009): 3068–77. https://doi.org/10.1021/bi900167q.
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  - Coggins, Brian E., and Pei Zhou. “High resolution 4-D spectroscopy with sparse concentric shell sampling and FFT-CLEAN.” J Biomol Nmr 42, no. 4 (December 2008): 225–39. https://doi.org/10.1007/s10858-008-9275-x.
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  - Barb, Adam W., and Pei Zhou. “Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase of bacterial lipid A synthesis.” Curr Pharm Biotechnol 9, no. 1 (February 2008): 9–15. https://doi.org/10.2174/138920108783497668.
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  - Zeng, Jianyang Michael, Chittaranjan Tripathy, Pei Zhou, and Bruce R. Donald. “A HAUSDORFF-BASED NOE ASSIGNMENT ALGORITHM USING PROTEIN BACKBONE DETERMINED FROM RESIDUAL DIPOLAR COUPLINGS AND ROTAMER PATTERNS.” Comput Syst Bioinformatics Conf 2008 (2008): 169–81.
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  - Zeng, Jianyang, Chittaranjan Tripathy, Pei Zhou, and Bruce R. Donald. “A Hausdorff-based NOE assignment algorithm using protein backbone determined from residual dipolar couplings and rotamer patterns.” Comput Syst Bioinformatics Conf 7 (2008): 169–81.
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  - Barb, A. W., L. Jiang, C. R. H. Raetz, and P. Zhou. “Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: Time-dependent inhibition and specificity in ligand binding (Proceedings of National Academy of Sciences of the United States of America (November 20, 2007) 104, 47, (18433-18438) DOI:10.1073/pnas0709412104)).” Proceedings of the National Academy of Sciences of the United States of America 104, no. 52 (December 26, 2007): 21020. https://doi.org/10.1073/pnas.0711056105.
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  - Moss, Marcia L., Martha Bomar, Qian Liu, Harvey Sage, Peter Dempsey, Patricia M. Lenhart, Patricia A. Gillispie, et al. “The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events.” J Biol Chem 282, no. 49 (December 7, 2007): 35712–21. https://doi.org/10.1074/jbc.M703231200.
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  - Barb, Adam W., Ling Jiang, Christian R. H. Raetz, and Pei Zhou. “Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: Time-dependent inhibition and specificity in ligand binding.” Proc Natl Acad Sci U S A 104, no. 47 (November 20, 2007): 18433–38. https://doi.org/10.1073/pnas.0709412104.
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  - Brower-Toland, Brent, Seth D. Findley, Ling Jiang, Li Liu, Hang Yin, Monica Dus, Pei Zhou, Sarah C. R. Elgin, and Haifan Lin. “Drosophila PIWI associates with chromatin and interacts directly with HP1a.” Genes Dev 21, no. 18 (September 15, 2007): 2300–2311. https://doi.org/10.1101/gad.1564307.
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  - Pai, Ming-Tao, Shiou-Ru Tzeng, Jeffrey J. Kovacs, Mignon A. Keaton, Shawn S-C Li, Tso-Pang Yao, and Pei Zhou. “Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin.” J Mol Biol 370, no. 2 (July 6, 2007): 290–302. https://doi.org/10.1016/j.jmb.2007.04.015.
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  - Lemieux, George A., Fernando Blumenkron, Nolan Yeung, Pei Zhou, Jason Williams, Amrie C. Grammer, Robert Petrovich, Peter E. Lipsky, Marcia L. Moss, and Zena Werb. “The low affinity IgE receptor (CD23) is cleaved by the metalloproteinase ADAM10.” J Biol Chem 282, no. 20 (May 18, 2007): 14836–44. https://doi.org/10.1074/jbc.M608414200.
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  - Barb, Adam W., Amanda L. McClerren, Karnem Snehelatha, C Michael Reynolds, Pei Zhou, and Christian R. H. Raetz. “Inhibition of lipid A biosynthesis as the primary mechanism of CHIR-090 antibiotic activity in Escherichia coli.” Biochemistry 46, no. 12 (March 27, 2007): 3793–3802. https://doi.org/10.1021/bi6025165.
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  - Bomar, Martha G., Ming-Tao Pai, Shiou-Ru Tzeng, Shawn Shun-Cheng Li, and Pei Zhou. “Structure of the ubiquitin-binding zinc finger domain of human DNA Y-polymerase eta.” Embo Rep 8, no. 3 (March 2007): 247–51. https://doi.org/10.1038/sj.embor.7400901.
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  - Coggins, Brian E., and Pei Zhou. “Sampling of the NMR time domain along concentric rings.” J Magn Reson 184, no. 2 (February 2007): 207–21. https://doi.org/10.1016/j.jmr.2006.10.002.
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  - Coggins, Brian E., and Pei Zhou. “Polar Fourier transforms of radially sampled NMR data.” J Magn Reson 182, no. 1 (September 2006): 84–95. https://doi.org/10.1016/j.jmr.2006.06.016.
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  - Werner-Allen, Jon W., Ling Jiang, and Pei Zhou. “A 'just-in-time' HN(CA)CO experiment for the backbone assignment of large proteins with high sensitivity.” J Magn Reson 181, no. 1 (July 2006): 177–80. https://doi.org/10.1016/j.jmr.2006.04.001.
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  - Ban, Yih-En Andrew, Johannes Rudolph, Pei Zhou, and Herbert Edelsbrunner. “Evaluating the quality of NMR structures by local density of protons.” Proteins 62, no. 4 (March 1, 2006): 852–64. https://doi.org/10.1002/prot.20811.
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  - Coggins, Brian E., and Pei Zhou. “PR-CALC: a program for the reconstruction of NMR spectra from projections.” J Biomol Nmr 34, no. 3 (March 2006): 179–95. https://doi.org/10.1007/s10858-006-0020-z.
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  - Li, Ming, Hemali P. Phatnani, Arno L. Greenleaf, and Pei Zhou. “NMR assignment of the SRI domain of human Set2/HYPB.” J Biomol Nmr 36 Suppl 1 (2006): 5. https://doi.org/10.1007/s10858-005-4690-8.
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  - Li, Ming, Hemali P. Phatnani, Ziqiang Guan, Harvey Sage, Arno L. Greenleaf, and Pei Zhou. “Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1.” Proc Natl Acad Sci U S A 102, no. 49 (December 6, 2005): 17636–41. https://doi.org/10.1073/pnas.0506350102.
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  - He, Chuan, Jean-Christophe Hus, Li Jing Sun, Pei Zhou, Derek P. G. Norman, Volker Dötsch, Hua Wei, et al. “A methylation-dependent electrostatic switch controls DNA repair and transcriptional activation by E. coli ada.” Mol Cell 20, no. 1 (October 7, 2005): 117–29. https://doi.org/10.1016/j.molcel.2005.08.013.
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  - Coggins, Brian E., Ronald A. Venters, and Pei Zhou. “Filtered backprojection for the reconstruction of a high-resolution (4,2)D CH3-NH NOESY spectrum on a 29 kDa protein.” J Am Chem Soc 127, no. 33 (August 24, 2005): 11562–63. https://doi.org/10.1021/ja053110k.
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  - Jiang, Ling, Brian E. Coggins, and Pei Zhou. “Rapid assignment of protein side chain resonances using projection-reconstruction of (4,3)D HC(CCO)NH and intra-HC(C)NH experiments.” J Magn Reson 175, no. 1 (July 2005): 170–76. https://doi.org/10.1016/j.jmr.2005.03.014.
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  - Venters, Ronald A., Brian E. Coggins, Doug Kojetin, John Cavanagh, and Pei Zhou. “(4,2)D Projection--reconstruction experiments for protein backbone assignment: application to human carbonic anhydrase II and calbindin D(28K).” J Am Chem Soc 127, no. 24 (June 22, 2005): 8785–95. https://doi.org/10.1021/ja0509580.
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  - Coggins, Brian E., Amanda L. McClerren, Ling Jiang, Xuechen Li, Johannes Rudolph, Ole Hindsgaul, Christian R. H. Raetz, and Pei Zhou. “Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design.” Biochemistry 44, no. 4 (February 1, 2005): 1114–26. https://doi.org/10.1021/bi047820z.
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  - McClerren, Amanda L., Pei Zhou, Ziqiang Guan, Christian R. H. Raetz, and Johannes Rudolph. “Kinetic analysis of the zinc-dependent deacetylase in the lipid A biosynthetic pathway.” Biochemistry 44, no. 4 (February 1, 2005): 1106–13. https://doi.org/10.1021/bi048001h.
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  - Coggins, Brian E., Ronald A. Venters, and Pei Zhou. “Generalized reconstruction of n-D NMR spectra from multiple projections: application to the 5-D HACACONH spectrum of protein G B1 domain.” J Am Chem Soc 126, no. 4 (February 4, 2004): 1000–1001. https://doi.org/10.1021/ja039430q.
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  - Coggins, Brian E., Xuechen Li, Ole Hindsgaul, Christian R. H. Raetz, and Pei Zhou. “Assignment of the 1H, 13C and 15N resonances of the LpxC deacetylase from Aquifex aeolicus in complex with the substrate-analog inhibitor TU-514.” J Biomol Nmr 28, no. 2 (February 2004): 201–2. https://doi.org/10.1023/B:JNMR.0000013817.29493.87.
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  - Coggins, Brian E., Xuechen Li, Amanda L. McClerren, Ole Hindsgaul, Christian R. H. Raetz, and Pei Zhou. “Structure of the LpxC deacetylase with a bound substrate-analog inhibitor.” Nat Struct Biol 10, no. 8 (August 2003): 645–51. https://doi.org/10.1038/nsb948.
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  - Coggins, Brian E., and Pei Zhou. “PACES: Protein sequential assignment by computer-assisted exhaustive search.” J Biomol Nmr 26, no. 2 (June 2003): 93–111. https://doi.org/10.1023/a:1023589029301.
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  - Blackshear, Perry J., Wi S. Lai, Elizabeth A. Kennington, Gary Brewer, Gerald M. Wilson, Xiaoju Guan, and Pei Zhou. “Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates.” J Biol Chem 278, no. 22 (May 30, 2003): 19947–55. https://doi.org/10.1074/jbc.M301290200.
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  - Lugovskoy, Alexey A., Alexei I. Degterev, Amr F. Fahmy, Pei Zhou, John D. Gross, Junying Yuan, and Gerhard Wagner. “A novel approach for characterizing protein ligand complexes: molecular basis for specificity of small-molecule Bcl-2 inhibitors.” J Am Chem Soc 124, no. 7 (February 20, 2002): 1234–40. https://doi.org/10.1021/ja011239y.
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  - Zhou, P., A. A. Lugovskoy, J. S. McCarty, P. Li, and G. Wagner. “Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45.” Proc Natl Acad Sci U S A 98, no. 11 (May 22, 2001): 6051–55. https://doi.org/10.1073/pnas.111145098.
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  - Zhou, P., A. A. Lugovskoy, and G. Wagner. “A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins.” J Biomol Nmr 20, no. 1 (May 2001): 11–14. https://doi.org/10.1023/a:1011258906244.
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  - Lugovskoy, A. A., P. Zhou, J. J. Chou, J. S. McCarty, P. Li, and G. Wagner. “Solution structure of the CIDE-N domain of CIDE-B and a model for CIDE-N/CIDE-N interactions in the DNA fragmentation pathway of apoptosis.” Cell 99, no. 7 (December 23, 1999): 747–55. https://doi.org/10.1016/s0092-8674(00)81672-4.
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  - Zhou, P., J. Chou, R. S. Olea, J. Yuan, and G. Wagner. “Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: a structural basis for specific adaptor/caspase interaction.” Proc Natl Acad Sci U S A 96, no. 20 (September 28, 1999): 11265–70. https://doi.org/10.1073/pnas.96.20.11265.
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  - Zhou, P., L. J. Sun, V. Dötsch, G. Wagner, and G. L. Verdine. “Solution structure of the core NFATC1/DNA complex.” Cell 92, no. 5 (March 6, 1998): 687–96. https://doi.org/10.1016/s0092-8674(00)81136-8.
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  - Wolfe, S. A., P. Zhou, V. Dötsch, L. Chen, A. You, S. N. Ho, G. R. Crabtree, G. Wagner, and G. L. Verdine. “Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc.” Nature 385, no. 6612 (January 9, 1997): 172–76. https://doi.org/10.1038/385172a0.
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  - Ikeh, Kanayo, Erica Lamkin, Andrew Crompton, Jamie Deutsch, Kira Fisher, Mark E. Gray, David Argyle, et al. “REV1 Inhibition Enhances Radioresistance and Autophagy,” n.d. https://doi.org/10.20944/preprints202109.0202.v1.
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- Book Sections
  - Coggins, B. E., and P. Zhou. “CLEAN.” In New Developments in NMR, 2017-January:169–219, 2017. https://doi.org/10.1039/9781782628361-00169.
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  - Coggins, B. E., and P. Zhou. “Backprojection and Related Methods.” In New Developments in NMR, 2017-January:119–68, 2017. https://doi.org/10.1039/9781782628361-00119.
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- Conference Papers
  - An, Jinsu, Jinshi Zhao, Dohyeon Hwang, Robert A. Gillespie, Eun Gyeong Yang, Pei Zhou, and Hak Suk Chung. “The lipid A 1-phosphatase, LpxE, play multiple roles in bacteria envelope biogenesis.” In Faseb Journal, Vol. 32. FEDERATION AMER SOC EXP BIOL, 2018.
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  - Lee, Minhee, Jinshi Zhao, Jae Cho, Do-Yeon Kwon, Pei Zhou, and Jiyong Hong. “Synthesis and biological evaluation of sulfonyl piperazine derivatives for LpxH inhibition.” In Abstracts of Papers of the American Chemical Society, Vol. 253. AMER CHEMICAL SOC, 2017.
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  - Chung, Ben C., Jinshi Zhao, Robert Gillespie, Do Yeon Kwon, Ziqiang Guan, Jiyong Hong, Pei Zhou, and Seok-Yong Lee. “Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis.” In Biophysical Journal, 106:14a-14a. Elsevier BV, 2014. https://doi.org/10.1016/j.bpj.2013.11.131.
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  - Liu, Jiangxin, Shilong Fan, Chul-Jin Lee, Arno L. Greenleaf, and Pei Zhou. “Specific interaction of the TCERG1 FF4-6 tandem repeat domains with RNA polymerase II requires simultaneous phosphorylation at Ser2, Ser5 and Ser7 of the CTD.” In Faseb Journal, Vol. 27. FEDERATION AMER SOC EXP BIOL, 2013.
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  - Masoudi, Ali, Charles W. Pemble, Christian R. H. Raetz, and Pei Zhou. “Structural Basis for Acyl-substrate Delivery and Product Release by ACP in the Biosynthesis of Lipid A.” In Faseb Journal, Vol. 27. FEDERATION AMER SOC EXP BIOL, 2013.
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  - Lee, Chul-Jin, Xiaofei Liang, Eugene Park, Daina Zeng, Shauna Swanson, Xin Chen, Robert A. Nicholas, Christian R. H. Raetz, Eric J. Toone, and Pei Zhou. “Structure-activity relationships of diacetylene-based LpxC inhibitors.” In Faseb Journal, Vol. 26. FEDERATION AMER SOC EXP BIOL, 2012.
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  - Young, Hayley E., Louis E. Metzger, John K. Lee, Robert M. Stroud, Pei Zhou, and Christian R. H. Raetz. “Enzymatic and structural studies of UDP-2,3-diacylglucosamine hydrolysis in lipid A biosynthesis.” In Faseb Journal, Vol. 26, 2012.
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  - Zeng, Daina, Pei Zhou, and Christian R. H. Raetz. “Characterization of E. coli mutants resistant to LpxC inhibitors.” In Faseb Journal, Vol. 26. FEDERATION AMER SOC EXP BIOL, 2012.
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  - Greenleaf, A. L., H. P. Phatnani, M. Li, and P. Zhou. “Structure and CTD phosphorylation pattern-binding specificity of the SRI domain of Set2.” In Faseb Journal, 20:A467–A467. FEDERATION AMER SOC EXP BIOL, 2006.
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  - McClerren, A., J. Rudolph, P. Zhou, and C. R. H. Raetz. “Mechanistic studies of the deacetylase LpxC, a novel target for drug design in gram-negative bacteria.” In Faseb Journal, 18:C54–C54. FEDERATION AMER SOC EXP BIOL, 2004.
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Teaching & Mentoring
Recent Courses
- BIOCHEM 393: Research Independent Study 2022
- BIOCHEM 593: Research Independent Study 2022
- BIOCHEM 659: Structural Biochemistry II 2022
- CBB 659: Structural Biochemistry II 2022
- CELLBIO 659: Structural Biochemistry II 2022
- SBB 659: Structural Biochemistry II 2022
- UPGEN 659: Structural Biochemistry II 2022
- BIOCHEM 393: Research Independent Study 2021
- BIOCHEM 593: Research Independent Study 2021
- BIOCHEM 659: Structural Biochemistry II 2021
- CBB 659: Structural Biochemistry II 2021
- CELLBIO 659: Structural Biochemistry II 2021
- SBB 659: Structural Biochemistry II 2021
- UPGEN 659: Structural Biochemistry II 2021
- BIOCHEM 393: Research Independent Study 2020
- BIOCHEM 593: Research Independent Study 2020
- BIOCHEM 659: Structural Biochemistry II 2020
- CBB 659: Structural Biochemistry II 2020
- CELLBIO 659: Structural Biochemistry II 2020
- SBB 659: Structural Biochemistry II 2020
- UPGEN 659: Structural Biochemistry II 2020

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