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Research Professors/Scientist


Qi Zhang, PhD

Qi Zhang

Research Assistant Professor
Tulane University School of Medicine
Department of Biochemistry and Molecular Biology
1430 Tulane Avenue, #8543
New Orleans, LA 70112
(504) 988-4218
E-mail:  qzhang10@tulane.edu

» Lu Lab Website

Research Interests:  Targeting the p53-pathway for the treatment of cancer; Study of p53 regulators by a combination of biochemical and structural analyses.

Summary:  Tumor suppressor p53 plays a central role in preventing tumorigenesis. Its mutation or inactivation is highly related to all human cancers. During my postdoctoral studies, I have focused on the discovery of anticancer small molecule candidates to restore normal p53 function and understanding the structure-function relationship between important p53 regulators, ribosomal proteins and MDM2. These studies will potentially provide new insights into human cancer development and lead to the discovery of novel agents for cancer chemotherapy. Through my research, I developed a protocol to screen and identify compounds that inhibit MDM2/MDMX and activate p53. I have identified a novel p53 activator, Inauzhin, which can inhibit and kill tumor cells. Currently, I play a major role in working with a multidisciplinary team for the optimization of the lead drug Inauhzin and testing different combination strategies for cancer treatment. Together with my collaborators, I not only unveiled the key chemical features for anti-cancer activity of Inauhzin, but also developed the newly synthesized Inauhzin analogs as improved small molecule inhibitors for further development of anti-cancer therapy. Additionally, my studies on the structure and function relationship of p53 regulators, MDM2 and RPL11 and RPL5, have unveiled important amino acid residues in these protein regulators for the p53 regulation. As a major player of the research team in this project, I have been responsible for coordinating with members at the center of structure biology at Indiana University and Tulane University on solving the crystal structure of the MDM2/ribosomal protein complex. I have been developing an elegant and sophisticated multigene expression system to co-express and co-purify the novel protein complex in order to explore the structures and functions of the p53 regulators MDM2 and the ribosomal proteins. I have obtained extensive experience in the screening for therapeutic candidates and the biochemical characterization of drug targets as a postdoctoral researcher at Indiana University School of Medicine. I have collaborated efficiently with scientists from various areas, such as molecular biology, cellular biology, biochemistry, computer-aided drug design, combinatorial chemistry, clinical pharmacology, drug analysis and high-throughput screening, facilitating the progression of drug discovery projects. My research will be complementary to the mission of Tulane School of Medicine and Tulane Cancer Center in discovering cures for cancer diseases and building the essential bridge between basic research and clinical research to accomplish this objective.

Publications

  1. Zhang Q, Zeng SX and Lu H. (2012). Targeting the p53-MDM2-MDMX-loop for cancer therapy. p53 mutations, MDM2 and cancer. First edition, Springer Science and Humana Press. Book Chapter. In preparation.
  2. Zhang Y, Zhang Q, Zeng SX, Hao Q and Lu H. (2012) Inauhzin Sensitizes p53-dependent cytotoxicity and tumor suppression of chemotherapeutic agents. Neoplasia. Accepted.
  3. Zhang Q*, Ding DR, Zeng SX, Ye QZ, and Lu H. (2012) Structure and activity studies of Inauhzin derivatives as novel antitumor compounds that induced p53 expression and acetylation. PLoS ONE. 7(10), e46294. * Co-first author.
  4. Zhang Q and Lu H. (2013) Identification of small molecules affecting p53-MDM2/MDMX interaction by fluorescence polarization. Methodology Mol Biol. Second Edition, 962:95-111. P53 Protocols,  Springer Protocols and Humana Press.
  5. Zhang Y, Zhang Q, Zeng SX, Zhang Y, Mayo L and Lu H. (2012) Inauhzin and Nutlin3 synergistically activate p53 and suppress tumor growth. Cancer Biology & Therapy, 13(10): 915-924.
  6. Zhang Q, Zeng SX, Zhang Y, Zhang Y, Ding DR, Ye QZ, Meroueh SO and Lu H. (2012) A small molecule Inauzhin inhibits SIRT1 activity and suppresses tumor growth via activation of p53. Embo Molecular Medicine, 4(4):298-312 (Recommended in Lead Discovery's Daily Updates, 2012).
  7. Zhou X, Hao Q, Liao JM, Zhang Q and Lu H. (2012) Ribosomal protein S14 unties the MDM2-p53 loop upon ribosomal stress. Oncogene, 1-9.
  8. Lee JH, Zhang Q, Jo S, Chai SC, Oh M, Im W, Lu H, Lim HS. (2011) Novel pyrrolopyrimidine-based α-helix mimetics: cell permeable inhibitors of protein-protein interactions. J Am Chem Soc, 133 (4), 676-679. (Recommended in Faculty of 1000 Biology, 2011; Highlighted in SciBX: Science-Business eXchange, 2011, 4[3]). 
  9. Zhang Q, Xiao H, Chai SC, Hoang QQ, and Lu H. (2011) Hydrophilic residues are crucial for RPL11 interaction with the zinc finger domain of MDM2 and p53 activation. J Bio Chem, 4; 286(44):38264-74.
  10. Zhang Q and Lu H. (2010) Nutlin-3’s two roads to apoptosis. Cancer Biology & Therapy. 10(6):579-81. Review Commentary.

 

 

Tulane University, New Orleans, LA 70118 504-865-5000 website@tulane.edu