Yongbin YAN, Ph.D.

Tenure-Track Principle Investigator


1992-1997, Bachelor of Mechanical Engineering, Tsinghua University, Beijing

1997-2001, MS. and Ph.D. of Biology, Tsinghua University, Beijing

2001- present, PI, School of Life Sciences, Tsinghua University

 

 

Research interest


We are studying the structure, components, folding, assembly, physiological and pathological roles of cellular bodies including aggresomes/inclusion bodies and RNA granules via biophysical, biochemical and cellular methods. The present projects are;

1. Protein aggregation in conformational diseases: protein folding, misfolding and aggregation by biospectroscopy, particular of aggregation in inherited eye diseases and pathological conditions;

2. Ribonucleases and mRNA decay: structure and function of ribonucleases and their role in the regulation of mRNA turnover, with a focus on deadenylases. We are also interested in the structural basis of assembly and physiological functions of various RNA granules;

3. Creatine kinase and intracellular energy homeostasis: mechanisms of intracellular energy homeostasis regulated by creatine kinase and its binding partners.

 

 

Courses offered


Introduction of Modern Biology for undergraduate students

Biospectroscopy for graduate students

Frontiers of Biophysics for graduate students

 

Selected publications


(* Corresponding author, # co-first authors)

1      Yan YB*. (2016) Creatine kinase in cell cycle regulation and cancer. Amino Acids doi:10.1007/s00726-016-2217-0. [Epub ahead of print]. (commissioned review)

2      Liu H#, Gao YS#, Chen XJ, Chen Z, Zhou HM, Yan YB*, Gong H*. (2016) A single residue substitution accounts for the significant difference in thermostability between two isoforms of human cytosolic creatine kinase. Sci. Rep. 6: 21191. doi: 10.1038/srep21191.

3      Xi YB#, Chen XJ#, Zhao WJ#Yan YB*. (2015) Congenital cataract-causing mutation G129C in gC-crystallin promotes the accumulation of two distinct unfolding intermediates that form highly toxic aggregates. J. Mol. Biol. 427(17): 2765-2781.

4      Zhao L#, Chen XJ#, Zhu J#, Xi YB#, Yang X#, Hu LD#, Ouyang H, Patel SH, Jin X, Lin D, Wu F, Flagg K, Cai H, Li G, Cao G, Lin Y, Chen D, Wen C, Chung C, Wang Y, Qiu A, Yeh E, Wang W, Hu X, Grob S, Abagyan R, Su Z, Tjondro HC, Zhao XJ, Luo H, Hou R, Perry JJP, Gao W, Kozak I, Granet D, Li Y, Sun X, Wang J, Zhang L*, Liu Y*, Yan YB*, Zhang K*. (2015) Lanosterol reverses protein aggregation in cataract. Nature. 523(7562): 607-611.

5      Zhang LN, Yan YB*. (2015) Depletion of poly(A)-specific ribonuclease (PARN) inhibits proliferation of human gastric cancer cells by blocking cell cycle progression. Biochim. Biophys. Acta – Mol. Cell Res. 1853(2): 522-534.

6      Xi YB, Zhao WJ, Zuo XT, Tjondro HC, Li J, Dai AB, Wang S, Yan YB*. (2014) Cataract-causing mutation R233H affects the stabilities of bB1- and bA3/bB1-crystallins with different pH-dependence. Biochim. Biophys. Acta – Mol. Basis Dis. 1842(11): 2216-2229.

7      Leng XY#, Wang S#, Cao NQ, Qi LB, Yan YB*. (2014) The N-terminal extension of bB1-crystallin chaperones b-crystallin folding and cooperates with aA-crystallin. Biochemistry. 53(15): 2464-2473.

8      Yan YB*. (2014) Deadenylation: enzymes, regulation and functional implications. WIRES RNA. 5(3): 421-443. (commissioned review)

9      Zhang K#, Zhao WJ#, Leng XY#, Wang S, Yao K*, Yan YB*. (2014) The importance of the last strand at the C-terminus in βB2-crystallin stability and assembly. Biochim. Biophys. Acta – Mol. Basis Dis. 1842(1): 44-55.

10   Wang S, Zhao WJ, Liu H, Gong H, Yan YB*. (2013) Increasing bB1-crystallin sensitivity to proteolysis caused by the congenital cataract-microcornea syndrome mutation S129R. Biochim. Biophys. Acta – Mol. Basis Dis. 1832(2): 302-311.

 

Contact information


School of Life Sciences, Tsinghua University, Beijing 100084, China
Tel: +86-10-62783477(O), +86-10-62772246 (L)
Fax: +86-10-62771597
E-mail: ybyan(AT)tsinghua.edu.cn