Jialing Lin

Contact Information:
Jialing Lin



 

Lin, Jialing (HSC)
Associate Professor

Department of:

College Of Medicine/Biochemistry & Molec Biology -Associate Professor

Center of:

Education:

Washington (St. Louis)   Ph.D.   1991

Professional Interest/Expertise/Specializations:
Bcl-2 family proteins regulated cell death and its relationship to development and treatment of cancer; Biosynthesis and functional structure of membrane proteins.

Websites:

Peggy and Charles Stephenson Oklahoma Cancer Center

Research Projects:

Structure-Function of Bcl-2 Related Apoptosis Regulators in Membranes-The goals of this project is to determine (1) the structural basis for tBid-activated oligomerization of pro-apoptotic Bax in the mitochondrial outer membrane; and (2) the structural basis for inhibition of tBid-activated Bax by Bcl-XL in the mitochondrial outer membrane.
The goals of this project is to determine (1) the structural basis for tBid-activated oligomerization of pro-apoptotic Bax in the mitochondrial outer membrane; and (2) the structural basis for inhibition of tBid-activated Bax by Bcl-XL in the mitochondrial outer membrane-The specific aims of this project are (1) to identify the Bax binding protein; and (2) to characterize the role of the Bax bindi

Selected Publications:

A natural compound elevates expression of Bim that interacts with Bcl-2 converting the anti-apoptotic protein to a pro-apoptotic Bax-like molecule
2011    Lixia Zhao#, Feng He#, Haiyang Liu#, Xiaojiang Hao*, Jialing Lin* and Quan Chen*
J. Biol. Chem.
Bax forms an oligomer via separate, yet interdependent, surfaces. J. Biol. Chem.
2010    Zhang, Z., Zhu, W., Lapolla, S.M., Miao, Y., Shao, Y., Falcone, M., Boreham, D., McFarlane, N., Ding, J., Johnson, A.E., Zhang, X.C., Andrews, D.W. and Lin, J.
J. Biol. Chem.
http://www.ncbi.nlm.nih.gov/pubmed?term=Bax%20forms%20an%20oligomer%20via%20separate%2C%20yet%20interdependent%2C%20surfaces
Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes
   Leber, B., Lin, J., and Andrews, D.W.
Apoptosis
tBid elicits a conformational alteration in the membrane-bound Bcl-2 such that it inhibits Bax pore formation.
   Peng, J.^, Tan, C.^, Roberts, G.J., Nikolaeva, O.^, Zhang, Z., Lapolla, S.M., Primorac, S., Andrews, D.W., and Lin, J.*
J. Biol. Chem.
Bcl-2 and Bax interact via the BH1-3 groove:BH3 motif interface and a novel interface involving the BH4 motif.
   Ding, J.^, Zhang, Z., Roberts, G.J., Falcone, M., Miao, Y., Shao, Y., Zhang, X.C., Andrews, D.W., and Lin, J.
J. Biol. Chem.
Keywords, Tags:
apoptosis, mitochondria,