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11. Y. Kim, S.H. Eom, J. Wang, D.S. Lee, S.W. Suh, T.A. Steitz (1995). Crystal structure of Thermus aquatics DNA polymerase. Nature, 376, 612-616.

12. S.H. Eom, J. Wang, T.A. Steitz (1996). The structure of Taq polymerase with DNA at the polymerase active site. Nature, 382, 278-281.

13. D.C. Boisvert, J. Wang, Z. Otwinowski, A.L. Horwich, P.B. Sigler (1996). The 2.4Å crystal structure of the bacterial chaperonin GroEL complex with ATPgS. Nature Struct. Biol. 3, 170-177.

14. J. Wang, P. Yu, T.C. Lin, W.H. Konigsberg, T.A. Steitz (1996). Crystal structures of an NH2-terminal fragment of T4 DNA polymerase and its complexes with single-stranded DNA and with divalent metal ions. Biochemistry, 35, 8110-8119.

15. J. Wang, J.A. Hartling, J.M. Flanagan (1997). The structure of ClpP at 2.3Å resolution suggests a model for ATP-dependent proteolysis. Cell, 91, 447-456.

16. J. Wang, A.K.M.A. Satter, C.C. Wang, J.D. Karam, W.H. Konigsberg, T.A. Steitz (1997). Crystal structure of a pol a family replication DNA polymerase from bacteriophage RB69. Cell. 89, 1087-1099.

17. J. Porankiewiz, J. Wang, A.K. Clarke (1998). New insights into the ATP-dependent ClpP protease: E. coli and beyond. Molecular Microbiology, 29, 275-283.

18. J. Wang, J.A. Harting, J.M. Flanagan (1998). Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask. J. Struct. Biol. 124, 151-163.

19. L.F. Silvian, J. Wang, T.A. Steitz (1999). Insights into editing from an isoleucyl-tRNA synthetase structure with tRNAile and mupirocin. Science, 285, 1074-1077.

20. F. Li, J. Wang, T.A. Steitz (2000). Induced dimerization of dimeric Suflobus Shibatae CCA-adding enzyme upon the binding of two tRNAs. J. Mol. Biol. 304, 483-492.

21. C.J. Noren, J. Wang, F.B. Perler (2000). Dissecting the Chemistry of Protein Splicing and its Applications. Angew. Chem. Int. Ed. 39, 450-466.

22. J. Wang, J.J. Song, I.S. Seong, M.C. Franklin, S. Kamtekar, S.H. Eom, C.H. Chung (2001). Nucleotide-dependent conformational changes in a protease-associated ATPase HslU. Structure 9, 1107-1116.

23. J. Wang, J.J. Song, M.C. Franklin, S. Kamtekar, Y.J. Im, S.H. Rho, I.S. Seong, C.S. Lee, C.H. Chung, S.H. Eom (2001). Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism. Structure 9, 177-184.

24. M. Hochstrasser, and J. Wang (2001). Unraveling the means to the end in ATP-dependent proteolysis. Nat. Struct. Biol. 8, 294-296.

25. M.C. Franklin, J. Wang, T.A. Steitz (2001). Structure of the replicating complex of a pol alpha family DNA polymerase. Cell 105, 657-667.

26. J. Wang (2001). A corrected quaternary arrangement of the peptidase HslV and ATPase HslU in a cocrystal structure. J. Struct. Biol. 134, 15-24.

27. I.S. Seong, M.S. Kang, M.K. Choi, J.W. Lee, O.J. Koh, J. Wang, S. H. Eom, C.H. Chung (2002). The C-terminal tails of HslU ATPase as a molecular switch for activation of HslV peptidase. J. Biol. Chem. 277, 25976-25982.

28. Y.H. Cheon, H.S. Kim, K.H. Han, A. Abendroth, K. Niefind, D. Schomburg, J. Wang, Y. Kim (2002). Crystal structure of D-hyantoinase from Bacillus stearothermophilus: insight into stereochemistry of enantioselectivity. Biochemistry, 412, 9410-9417.

29. F. Li, Y. Xiong, J. Wang, H.D. Cho, K. Tomita, A.M. Weiner, T.A. Steitz (2002). Crystal structure of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP. Cell 111, 815-824.

30. J. Wang (2003). A second response in correcting the HslV-HslU quaternary structure. J. Struct. Biol. 141, 7-8.

31. S. Szep, J. Wang, P. Moore (2003). The crystal structure of a 26-nucleotide RNA containing a hook-turn. RNA, 9,44-51.

32. J. Wang, D.C. Boisvert (2003). Structural basis for GroEL-assisted protein folding from crystal structure of (GroEL-KMgATP)14 at 2.0Å resolution. J. Mol. Biol. 327, 843-855.

33. J. Wang, L. Chen (2003). Domain motions in GroEL upon binding of an oligopeptide. J. Mol. Biol. 334, 489-499.

34. S. Kamtekar, W.D. Kennedy, J. Wang, C. Stathopoulos, D. Soll, T.A. Steitz (2003). The structural basis of cysteine aminoacylation of tRNApro by prolyl-tRNA synthetases. Proc. Natl. Acad. Sci. USA 100, 1673-1678.

35. Z.S. Juo, G.A. Kassavetis, J. Wang, E.P. Geiduschek, P. B. Sigler. (2003). Crystal structure of a Pol III Transcription Assembly: a yeast Brf1-TBP-DNA ternary complex. Nature, 422, 534-539.

36. J. Yoon, B. Oh, K. Kim, J.E. Park, J. Wang, H.K. Kim, Y. Kim (2003). Modifying the oligomeric state of cyclic amidase and its effect on enzymatic catalysis. Biochem. Biophys. Res. Commun. 310, 651-659.

37. Y. Xiong, F. Li, J. Wang, A.M. Weiner, T.A. Steitz (2003). Crystal structure of an archaeal class I CCA-adding enzyme and its nucleotide complexes. Mol. Cell 12, 1165-1172.

38. C.X. Wang, E. Zakharova, J. Li, C.M. Joyce, J. Wang, W. Konigsberg (2004). Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiphosphoryl linkages on the 3'-5' exonuclease activity. Biochemistry 43, 3853-3861.

39. E. Zakharova, J. Wang, W. Konigsberg. (2004). The activity of selected RB69 DNA polymerase mutants can be restored by manganese ions: the existence of alternative metal ion ligands used during the polymerase cycle. Biochemistry 43, 6587-6595.

40. H.J. Merianos, J. Wang, P.B. Moore (2004). The structure of a ribosomal S8/spc operon mRNA complex. RNA 10, 954-964.

41. P.L. Adams, M.R. Stahley, A.B. Kosek, J. Wang, S.A. Strobel (2004). Crystal structure of a self-splicing group I intron with both exons. Nature 430, 45-50.

42. J. Wang (2004). Nucleotide-dependent domain motions with rings of the RecA/AAA+ superfamily. J. Struct. Biol. 148, 259-267.

43. R. Pattanayek, J. Wang, T. Mori, Y. Xu., C.H. Johnson, M. Egli (2004). Visualizing a circadian clock protein: crystal structure of KaiC and functional insights. Mol. Cell 15, 375-388.

44. S. Kamtekar, A.J. Berman, J. Wang, J.M. Lazaro, M. deVega, L. Blanco, M. Salas, T.A. Steitz (2004). Insights into strand displacement and processivity from the crystal structure of the protein-primed DNA polymerase of bacteriophage phi29. Mol. Cell 16, 609-618.

45. P.L. Adams, M.R. Stahley, M.L. Gill, A.B. Kosek, J. Wang, S.A. Strobel (2004). Crystal structure of a group I intron splicing intermediate. RNA 10, 1867-1887.

46. S.A. Strobel, P.L. Adams, M.R. Stahley, J. Wang (2004). RNA kink turns to the left and to the right. RNA 10, 1852-1854.

47. J. Wang, S. Kamtaker, A.J. Berman, T.A. Steitz (2005). Correction of X-ray intensities from single crystals containing lattice-translocation defects. Acta Cryst. D. 61, 67-74.

48. G. Yang, J. Wang, W. Konigsberg (2005). Base selectivity is impaired by mutants that perturb hydrogen bonding networks in the RB69 DNA polymerase active site. Biochemistry 44, 3338-3346.

49. J. Wang (2005). Recent cyanobacterial Kai protein structures suggest a rotary clock. Structure 13, 735-741.

50. J. Wang, S.H. Rho, H.H. Park, S.H. Eom (2005). Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects. Acta Cryst. D61, 932-941 .

51. I. Rodriguez, J. Lazaro, L. Blanco, S. Kamtekar, A. Berman, J. Wang, T.A. Steitz, M. Salas, M. deVega, (2005) A specific subdomain of f29 DNA polymerase confers both processivity and strand dispacement capacity. Proc. Natl. Acad. Sci. USA 102, 6407-6412.

52. E. Park, Y.M. Rho, O. Koh, S.W. Ahn, I.S. Seong, J.J. Song, O. Bang, J.H. Seol, J. Wang, S.H. Eom, C.H. Chung, (2005) Role of the GYVG pore moitif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase. J. Biol. Chem. 280, 25976-25982

53. J. Wang, S. Gulich, C. Bradford, M.Ramirez-Alvarado, L. Regan, (2005). A twisted four-sheeted model for an amyloid fibril. Structure 13, 1279-1288.

54. J. Wang, (2005). Hoogsteen Base-Pairing in DNA replication. Nature 437, E6-E7.

55. M.A. Talavera. E.E. Matthews, W.K. Eliason, I. Sagi, J. Wang, A. Henn, E.M. De La Cruz, (2006). Hydrodynamic Characterization of the DEAD-box RNA Helicase DbpA. J. Mol. Biol. 355, 697-707.

56. H. Zhang, C. Rhee, A. Bebenek, J.W. Drake, J. Wang, W. Konigsberg, (2006). The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Biochemistry, 45, 2211-2220.

57. S. Kamtekar, A.J. Berman, J. Wang, J.M. Lazaro, M. de Vega, L. BLanco, M. Salas, T.A. Steitz (2006). The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition. EMBO J. 25, 1335-1343.