Drug Discovery Patents
1-substituted diazen-1-ium-1,2-diolates and O2-substituted
Early Publications (1978-1999)
1. “An example of the combined use of Chinese traditional medicine and western medicine,” X. Ji, Tongliao Science and Technology, 1, 14-16 (1978).
2. “Acupuncture to biliary ascariasis,” X. Ji, Tongliao Science and Technology, 1, 17-19 (1978).
3. “How to improve your English pronunciation,” X. Ji, Journal of National Teachers’ College of Inner Mongolia, 1, 127-130 (1985).
4. “The structures of different diastereomers of bicyclo[2.2.1] hept-5-en-2-yl phenyl sulfoxide,” X. Ji, D. van der Helm, R.V. Williams, and W.J. Ebey, Acta Crystallogr. B45, 93-99 (1989).
5. “Structure of methyl (E)-p[3,3,3-trifluoro-2-(2,2,4,4-tetramethyl-6-thiochromanyl)-1-propenyl]benzoate,” X. Ji, D. van der Helm, K.D. Berlin, and L.W. Spruce, Acta Crystallogr. C45, 750-754 (1989).
6. “Sclerophytin C-F: Isolation and structures of four new diterpenes from the soft coral Sclerophytum capitalis,” M. Alam, P. Sharma, A.S. Zektzer, G.E. Martin, X. Ji and D. van der Helm, J. Org. Chem. 54, 1896-1900 (1989).
7. “Acid-catalyzed rearrangement of arenerol,” V. Lakshmi, S.P. Gunasekera, F.J. Schmitz, X. Ji, and D. van der Helm, J. Org. Chem. 55, 4709-4711 (1990).
8. “Heteroarotinoids: Analytical criteria for the rapid identification of E and Z isomers of these novel retinoids via NMR, UV, and X-ray analyses of selected examples,” J.B. Gale, S.N. Rajadhyaksha, L.W. Spruce, K.D. Berlin, X. Ji, A. Slagle, and D. van der Helm, J. Org. Chem. 55, 3984 - 3991 (1990).
9. “Electrochemical oxidation of xanthosine. Isolation and structure elucidation of a new dimeric xanthine nucleoside,” X. Ji, P. Subramanian, D. van der Helm, and G. Dryhurst, J. Org. Chem. 55, 1291-1296 (1990).
10. “Molecular mechanics and/or X-ray crystallographic studies of: I. Three diastereomers of phenyl norbornenyl sulfoxide, II. Cyclized arenerol and 3-(8-xanthosyl)xanthine, III. Sclerophytin C, and IV. Five novel heteroarotinoids,” X. Ji, Ph.D. Dissertation, University of Oklahoma (1990).
11. “Organometallic compounds of the lanthanides. 64. Synthesis and X-ray crystal structures of dimethylgermyl bis(tetramethylcyclopentadienyl) halide and alkyl derivatives of the lanthanides,” H. Schumann, L. Esser, J. Loebel, A. Dietrich, D. van der Helm, and X. Ji, Organometallics 10, 2585-2592 (1991).
12. “The crystal and molecular structures of two 4-alkenyl-substituted bicyclohexylnitriles,” X. Ji, W. Richter, B.M. Fung, D. van der Helm, and M. Schadt, Mol. Cryst. Liquid Cryst. 201, 29-40 (1991).
13. “Novel heteroarotinoids: Synthesis and biological activity,” L.W. Spruce, J.B. Gale, K.D. Berlin, A.K. Verma, T.R. Breitman, X. Ji, and D. van der Helm, J. Med. Chem. 34, 430-439 (1991).
14. “Structure of 1,1-dichloro-2-(4-methoxyphenyl)-2,3-diphenylcyclopropane,” D. Li, M.B. Hossain, X. Ji, D. van der Helm, R.A. Magarian, and B.W. Day, Acta Crystallogr. C48, 887-891 (1992).
15. “Structure of asperketal B,” X. Ji, D. van der Helm, J. Shin, and W. Fenical, Acta Crystallogr. C48, 891-894 (1992).
16. “Structure of lansamide-2, a product from Clausena lansium,” X. Ji, D. van der Helm, V. Lakshmi, S.K. Agarwal, and R.S. Kapil, Acta Crystallogr. C48, 1082-1085 (1992).
17. “Structure and intramolecular hydrogen bond of 1-phenazinecarboxylic acid,” X. Ji, D. van der Helm, B. Hemming, and B.L. Haymore, Acta Crystallogr. C48, 109-111 (1992).
18. “Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase,” S. Liu, P. Zhang, X. Ji, W.W. Johnson, G.L. Gilliland, and R.N. Armstrong, J. Biol. Chem. 267, 4296-4299 (1992).
19. “Modular mutagenesis of exons 1, 2 and 8 of a glutathione S-transferase from the mu Class. Mechanistic and structural consequences for chimeras of isoenzyme 3-3,” P. Zhang, S. Liu, S.-O. Shan, X. Ji, G.L. Gilliland, and R.N. Armstrong, Biochemistry 31, 10185-10193 (1992).
20. “The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structure analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution,” X. Ji, P. Zhang, R.N. Armstrong, and G.L. Gilliland, Biochemistry 31, 10169-10184 (1992).
21. “Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase,” W.W. Johnson, S. Liu, X. Ji, G.L. Gilliland, and R.N. Armstrong, J. Biol. Chem. 268, 11508-11511 (1993).
22. “Second-sphere electrostatic effects in the active site of glutathione S-transferase. Observation of an on-face hydrogen bond between the side chain of threonine 13 and the p-cloud of tyrosine 6 and its influence on catalysis,” S. Liu, X. Ji, G.L. Gilliland, W.J. Stevens, and R.N. Armstrong, J. Am. Chem. Soc. 115, 7910-7911 (1993).
23. “Structure determination and refinement of human alpha class glutathione transferase A1-1,” I. Sinning, G.J. Kleywegt, S.W. Cowan, P. Reinemer, H.W. Dirr, R. Huber, G.L. Gilliland, R.N. Armstrong, X. Ji, P.G. Board, B. Olin, B. Mannervik, and T.A. Jones, J. Mol. Biol. 232, 192-212 (1993).
24. “Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase,” X. Ji, R.N. Armstrong, and G.L. Gilliland, Biochemistry (Accelerated Publications) 32, 12949-12954 (1993).
25. “Crystallographic and mechanistic studies of class mu glutathione S-transferases,” R.N. Armstrong, G.L. Gilliland, X. Ji, W.W. Johnson, and Suxing Liu, in Structure and Function of Glutathione Transferases, K.D. Tew, C.B. Pickett, T.J. Mantle, B. Mannervik, and J.D. Hayes eds., CRC Press, pp. 87-97 (1993).
26. “Fusion proteins as alternate crystallization paths to difficult structure problems,” D.C. Carter, F. Ruker, J.X. Ho, K. Lim, K. Keeling, G.L. Gilliland, and X. Ji, Protein Peptide Lett. 1, 175-178 (1994).
27. “Three-dimensional structure of Schistosoma jaonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV,” K. Lim, J.X. Ho, K. Keeling, G.L. Gilliland, X. Ji, F. Rüker, and D.C. Carter, Protein Sci. 3, 2233-2244 (1994).
28. “Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene,” X. Ji, W.W. Johnson, M.A. Sesay, L. Dickert, S.M. Prassad, H.L. Ammon, R.N. Armstrong, and G.L. Gilliland, Biochemistry 33, 1043-1052 (1994).
29. “The crystal structure of the 3-3 isozyme of glutathione S-transferase from the mu gene class: An example of a difficult MIR structure determination,” G.L. Gilliland, X. Ji, and R.N. Armstrong, in Isomorphous Replacement Methods in Macromolecular Crystallography, American Crystallographic Association, pp. 1-28 (1994).
30. “Three-dimensional structure, catalytic properties and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods,” X. Ji, E.C. von Rosenvinge, W.W. Johnson, S.I. Tomarev, J. Piatigorsky, R.N. Armstrong, and G.L. Gilliland, Biochemistry 34, 5317-5328 (1995).
31. “Crystallographic, molecular modeling and biophysical characterization of the valine beta 67 (E11) → threonine variant of hemoglobin,” I. Pechik, X. Ji, K. Fidelis, M. Karavitis, J. Moult, W.S. Brinigar, C. Fronticelli, and G.L. Gilliland, Biochemistry 35, 1935-1945 (1996).
32. “Positive and negative cooperativities at subsequent steps of oxygenation regulate the allosteric behavior of multistate sebacylhemoglobin,” E. Bucci, A. Razynska, H. Kwansa, Z. Gryczynski, J.H. Collins, C. Fronticelli, R. Unger, M. Braxenthaler, J. Moult, X. Ji, and G.L. Gilliland, Biochemistry 35, 3418-3425 (1996).
33. “First-sphere and second-sphere electrostatic effects in the active site of a class mu glutathione transferase,” G. Xiao, S. Liu, X. Ji, W.W. Johnson, J. Chen, J.F. Parsons, W.W. Stevens, G.L. Gilliland, and R.N. Armstrong, Biochemistry 35, 4753-4765 (1996).
34. “Location of a potential transport binding site in a sigma class glutathione transferase by X-ray crystallography,” X. Ji, E.C. von Rosenvinge, W.W. Johnson, R.N. Armstrong, and G.L. Gilliland, Proc. Natl. Acad. Sci. USA 93, 8208-8213 (1996).
35. “Structure, mechanism and evolution of class mu and sigma glutathione transferases,” R.N. Armstrong, J. Chen, W.W. Johnson, J. Parsons, X. Ji, G.L. Gilliland, S.I. Tomarev, and J. Piatigorsky, in Structure, Function and Clinical Implications of Glutathione Transferases, N.P.E. Vermeulen, G.J. Mulder, H. Nieuwenhuyse, W.H.M. Peters, and P.J. van Bladeren, eds., CRC Press, pp. 13-22 (1996).
36. “Active site architecture of polymorphic forms of human glutathione S-transferase P1-1 accounts for their enantioselectivity and disparate activity in the glutathione conjugation of 7beta,8alpha-dihydroxy-9alpha,10alpha-oxy-7,8,9,10-tetrahydrobenzo(a)pyrene,” X. Hu, R. O’Donnell, S.K. Srivastava, H. Xia, P. Zimniak, B. Nanduri, R.J. Bleicher, S. Awasthi, Y.C. Awasthi, X. Ji, and S.V. Singh, Biochem. Biophys. Res. Comm. 235, 424-428 (1997).
37. “Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase,” X. Ji, M. Tordova, R. O’Donnell, J.F. Parsons, J.B. Hayden, G.L. Gilliland, and P. Zimniak, Biochemistry 36, 9690-9702 (1997).
38. “Mechanism of differential catalytic efficiency of two polymorphic forms of human glutathione S-transferase P1-1 in the glutathione conjugation of carcinogenic diol epoxide of chrysene,” X. Hu, X. Ji, S.K. Srivastava, H. Xia, S. Awasthi, B. Nanduri, Y.C. Awasthi, P. Zimniak, and S.V. Singh, Archi. Biochem. Biophys. 345, 32-38 (1997).
39. “Activity of four allelic forms of glutathione S-transferase hGSTP1-1 for diol epoxides of polycyclic aromatic hydrocarbons,” X. Hu, H. Xia, S.K. Srivastava, C. Herzog, Y.C. Awasthi, X. Ji, P. Zimniak, and S.V. Singh, Biochem. Biophys. Res. Comm. 238, 397-402 (1997).
40. “Alpha-Subunit oxidation in T-state crystals of a sebacyl crosslinked human hemoglobin with unusual autoxidation properties,” X. Ji, M. Karavitis, A. Razynska, H. Kwansa, G.B. Vásquez, C. Fronticelli, E. Bucci, and G.L. Gilliland, Biophys. Chem. 70, 21-34 (1998).
41. “Conformation of the sebacyl beta1Lys82-beta2Lys82 crosslink in T-state human hemoglobin,” X. Ji, M. Braxenthaler, J. Moult, C. Fronticelli, E. Bucci, and G.L. Gilliland, PROTEINS: Struct. Funct. Genet. 30, 309-320 (1998).
42. “Human carboxyhemoglobin at 2.2 Å resolution: Structure and solvent comparisons of R-state, R2-state, and T-state hemoglobins,” G.B. Vásquez, X. Ji, C. Fronticelli, and G.L. Gilliland, Acta Crystallogr. D54, 355-366 (1998).
43. “Crystal structure of apo-cellular retinoic acid-binding protein type II (R111M) suggests a mechanism of ligand entry,” X. Chen, M. Tordova, G.L. Gilliland, L. Wang, Y. Li, H. Yan, and X. Ji, J. Mol. Biol. 278, 641-653 (1998).
44. “Cysteines beta93 and beta112 as probes of conformational and functional events at the human hemoglobin subunit interfaces,” G.B. Vásquez, M. Karavitis, X. Ji, I. Pechik, W.S. Brinigar, G.L. Gilliland, and C. Fronticelli, Biophys. J. 76, 88-97 (1999).
45. “Purification, characterization and crystallization of ERA, an essential GTPase from Escherichia coli,” X. Chen, S.-M. Chen, B.S. Powell, D.L. Court, and X. Ji, FEBS Lett. 445, 425-430 (1999).
46. “Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents,” B. Xiao, G. Shi, X. Chen, H. Yan, and X. Ji, Structure Fold. Des. 7, 489-496 (1999).
47. “Oxygen binding to alpha-subunits in high-salt crystals of T-state hemoglobin,” G.B. Vásques, X. Ji, I. Pechik, C. Fronticelli, and G.L. Gilliland, Proteins Peptide Lett. 6, 59-66 (1999).
48. “Crystal structure of ERA: A GTPase-dependent cell cycle regulator containing an RNA-binding motif,” X. Chen, D.L. Court, and X. Ji, Proc. Natl. Acad. Sci. USA 96, 8396-8401 (1999).
49. “Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1,” X. Ji, J. Blaszczyk, B. Xiao, R. O’Donnell, X. Hu, C. Herzog, S.V. Singh, and P. Zimniak, Biochemistry 38, 10231-10238 (1999).
50. “Amino acid substitutions at positions 207 and 221 constitute to catalytic differences between murine glutathione S-transferase A1-1 and A2-2 toward (+)-anti-7,8-dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene,” H. Xia, Y. Gu, S.-S. Pan, X. Ji, and S.V. Singh, Biochemistry 38, 9824-9830 (1999).
51. “Crystal structure of a murine glutathione S-transferase in complex with glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: Evidence of signaling across the dimer interface,” B. Xiao, S.P. Singh, Y.C. Awasthi, P. Zimniak, and X. Ji, Biochemistry 38, 11887-11894 (1999).
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