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Jing-Yuan Liu, PhD

Assistant Research Professor

Research Interest

My research focuses on drug discovery by understanding the interactions between proteins and their partners.

 

Education

1991-1995

B.Sc. Biochemistry | Shangdong University | China

1995-1998

M.Sc. Molecular Genetics | Institute of Genetics, Chinese Academy of Sciences | China

1998-2004

Ph.D. Biochemistry | Indiana University | Indianapolis, Indiana

Professional Service

2011-present

Int. J. Biochem Bol Biol | Associate Editorial Board Member

2013-present

Current Cancer Drug Target | Advisory Board Member

Honors

2004

10th SCBA Meeting Travel Award

2002

Outstanding Poster Presentation Award, Department of Biochemistry and Molecular Biology | Indiana University School of Medicine

1994

Annual Excellent Student Award
Shandong University | China



Protein-protein interactions are required for biological functions and alterations in protein-protein interactions can cause diseases such as cancer and diabetes. In addition, small molecules that interact with proteins can alter, regulate or trigger their function and thus may be valuable research and therapeutic tool.  However, protein recognition of exogenous or endogenous partners and formation of stable complexes are not fully understood. The assembly of protein complexes is a dynamic process and can be studied computationally by Molecular Dynamics (MD) simulations. Computational observance can be validated experimentally by time-resolved X-Ray Crystallography, Small Angle Scattering, NMR, and other techniques. Validated computational methods and bioinformatics approaches can then be applied to study multiple protein systems. Our goal is to understand the physics and chemistry that governs the assembly and the interactions between proteins and their partners. Using in silico screening we also can discover and develop small molecule drugs that can inhibit or enhance protein function. 


                                       Search Dr. Liu on PubMed

(*co-corresponding authors).

  • Timm, D.E.; Liu, J.Y.; Baker, L.J.; Harris, R.A. Crystal structure of thiamin pyrophosphokinase. J Mol Biol 310(1): 195-204; 2001.
  • Liu, J.Y.; Timm, D.E.; Harris, R.A.; Hurley, T.D. Studies in the structure and function of thiamin pyrophosphokinase. In: Patel MS, Jordan F, editors. Thiamine: Catalytic mechanism and role in normal and disease states. New York: Marcel Dekker. 2002.
  • Liu, J.Y.; Timm, D.E.; Hurley, T.D. Pyrithiamine as a substrate for thiamine pyrophosphokinase. J Biol Chem 281(10): 6601-6607; 2006
  • Li, Z.; Liu, J.Y.; Zhang, J.T. 14-3-3σ, the double-edged sword of human cancers. Am. J. Transl. Res. 1:312-324; 2009.
  • Liu, J.Y.; Mooney, S.D. Characterization of Ligand Type of Estrogen Receptor by MD Simulation and mm-PBSA Free Energy Analysis. Int J Biochem Mol Biol 2(2):190-198; 2011.
  • Liu, H.; Liu, J.Y.; Wu, X.; Zhang, J.T. Biochemistry, molecular biology, and pharmacology of fatty acid synthase, an emerging therapeutic target and diagnosis/prognosis marker. Int. J. Biochem. Mol. Biol. 1:69-89; 2010.
  • Neher, TM.; Shuck, SC.; Liu, J.Y.; Zhang, J.T.; Turchi, J.J. Identification of novel small molecule inhibitors of the XPA protein using in silico based screening. ACS Chem. Biol. 15:953-965; 2010.
  • Liu, J.Y.; Hurley, T.D. A new crystal form of mouse thiamin pyrophosphokinase. Int J Biochem Mol Biol 2:111-118; 2011.
  • Liu, J.Y.*; Li, Z.; Li, H.; Zhang, J.T.* A critical residue that promotes protein dimerization: a story of partially exposed Phe25 in 14-3-3σ. J. Chem. Inf. Model. 51:2612-25; 2011.
  • Mo, W.; Liu, J.Y.; Zhang, J.T. Biochemistry and pharmacology of human ABCC1/MRP1 and its role in detoxification and in multidrug resistance of cancer chemotherapy. Recent Advances of Cancer Research and Therapy (ed X.Y. Liu; S. Pestka; Y. Shi). Elsvier pp371-404; 2012
  • Li, Z.; Peng, H.; Qin, L.; Qi, J.; Zuo, X.; Liu, J.Y.*; Zhang, J.T*. Determinants of 14-3-3σ dimerization and function in drug resistance. J Biol Chem.  2013 Nov 1;288(44):31447-57.
  • Hu, G.; Liu, J.Y.*; and Wang, J.* Insight into conformational change for 14-3-3σ protein by molecular dynamics simulation. Int. J. Mol. Sci. 2014, 15(2), 2794-2810
  • Huang, W.; Dong, Z.; Wang, F.; Peng, H.; Liu, J.Y.*; and Zhang, J.T.* A small molecule inhibitor targeting the “undruggable” DNA-binding site of human STAT3 inhibits cancer cell proliferation, migration, and invasion. ACS Chem. Biol. (in press)

 


Department of Pharmacology and Toxicology | 635 Barnhill Drive, MS A401 | Indianapolis, IN 46202