Cardiovascular System: “Cholesterol and lipoprotein metabolism”

Renal System: “Acid-base disorders” & “Uric acid metabolism”

MCBM: “Acid-base balance”; “O2 metabolism & toxicity” & “Ketone body metabolism”

Postdoctoral Fellowship, Cancer Research Institute, New York (1995 –1998)
Klein Fellowship, Brandeis University (1991-1992)
Samuel Goldwyn Fellowship, Brandeis University (1989 - 1991)

1. Ren, H., Dou, S.-X., Zhang, X.-D., Liu, J.-L., Wang, P.-Y., and Hu, J.-S., and Xi, X. G.(2008) Modulation of double-stranded DNA unwinding and single-stranded DNA annealing of human RECQ5 helicase by a RecQ-specific motif. Biochem. J. (in press).

2. Zhang, X. D., Dou, S. X., Xie, P., Hu, J.-S., Wang, P.Y., and Xi, X.G. (2006) Escherichia coli RecQ is a rapid, efficient, and monomeric helicase. J. Biol. Chem., 281, 12655-12663.

3. Sun, J.-Z., Julin, D. and Hu, J.-S. (2006) The nuclease domain of the Escherichia ColiRecBCD enzyme catalyzes degradation of linear and circular single-stranded and double-stranded DNA. Biochemistry, 45, 131-140.

4. Lee, J. W., Kusumoto, R., Doherty, K. M., Lin, G.-X., Zeng, W., Cheng, W.-H., von Kobbe, C., Brosh Jr., R. M., Hu, J.-S., and Bohr, V. A. (2005) Modulation of Werner syndrome protein function by a single mutation in the conserved RecQ domain. J Biol. Chem., 280, 39627-39636.

5. Hu, J.-S., Feng, H.-Q., Zeng, W.-Y., Lin, G.-X., and Xi, X. G. (2005) Solution structure of a multifunctional DNA- and protein-binding domain of human Werner syndrome protein. Proc. Natl. Acad. Sci. USA, 102, 18379-18384.

6. Hu, J.-S., Plaksin, D., Margulies, D. (2005) Backbone and side chain resonance assignments of a TRAV14-3 mouse T cell receptor domain. J. Biomol. NMR. 31, 271-272.

7. Sun, J.-Z., Feng, H.-Q., Lin, G.-X., Zeng, W.-Y. and Hu, J.-S. (2005)NMR assignments of the winged-helix domain of human Werner syndrome protein. J. Biomol. NMR., 32, 261-261.

8. Koenig, B., Hu, J.-S., Hendler, R. and Bax, A. (1999) NMR measurement of dipolar couplings in Protein aligned by transient binding to purple membrane fragments. J. Am. Chem. Soc. 121, 1385-1386.

9. Cornilescu, G., Hu, J.-S. and Bax, A. (1999) Identification of the hydrogen bonding network in a protein by scalar couplings. J. Am. Chem. Soc. 121, 2949-2950.

10. Hu, J.-S. and Bax, A. (1998) Measurement of three-bond ¹³C'-¹³C^b J couplings in human ubiquitin by a triple resonance, E. COSY-type NMR technique. J. Biomol. NMR, 11, 199-203.

11. Hu, J.-S., and Bax, A. (1997) Determination of fand c₁ angles in proteins from ¹³C-¹³C three-bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond? J. Am. Chem. Soc. 119, 6360-6368.

12. Grzesiek, S., Bax, A., Hu, J.-S., Kaufman, J., Palmer, I., Stahl, S. J., Tjandra, N. and Wingfield, P. T. (1997) Refined solution structure and backbone dynamics of HIV-1 Nef. Prot. Sci. 6, 1248-1263.

13. Hu, J.-S. and Bax, A. (1997) c₁ Angle information from a simple two-dimensional NMR experiment which identifies trans ³J_NCg couplings in isotopically enriched proteins. J. Biomol. NMR 9, 323-328.

14. Hu, J.-S., Grzesiek, S. and Bax, A. (1997) Two-dimensional NMR methods for determining c₁ angles of aromatic residues in proteins from three-bond J_C'Cg and J_NCg couplings. J. Am. Chem. Soc. 119, 1803-1804.

15. Hu, J.-S., and Redfield, A. G. (1997) Conformational and dynamic differences between human N-ras p21 bound to GTPgS and to GMPPNP as studied by NMR. Biochemistry 36, 5045-5052.

16. Hu, J.-S., and Bax, A. (1996) Measurement of three-bond ¹³C-¹³C J couplings between carbonyl and carbonyl/carboxyl carbons in isotopically enriched proteins. J. Am. Chem. Soc. 118, 8170-8171.

17. Grzesiek, S., Bax, A., Clore, G. M., Gronenborn, A. M., Hu, J.-S., Kaufman, J., Palmer, I., Stahl, S. J. and Wingfield, P. T. (1996) The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein Kinase. Nature Struct. Biol. 3, 340-345.

Research Interests

Multidimensional NMR methods and their application in structural biology;

Structures and functions of the DNA repair and tumor suppressor proteins;

Molecular mechanism of the RecQ helicases function in DNA metabolism and in maintaining genome integrity.

Active Research Grants

American Cancer Society (PI): “Structural Studies of DNA Repair Nucleases: RecB and WRN”, $631,479.

American Heart Association (PI): “Structural Studies of the Werner Syndrome Protein and its Interaction with DNA”, $260,000.