Full Publication List:

 

1.   Kornacki, J.A., West, A.H. and Firshein, W. (1984). Proteins encoded by the trans‑acting replication and maintenance regions of broad host range plasmid RK2. Plasmid 11: 48-57.

 

2.   Gutowski, J.K., West, A. and Cohen, S. (1985). The regulation of DNA synthesis in quiescent lymphocytes by cytoplasmic inhibitors. Proc. Natl. Acad. Sci. (USA) . 82: 5160-5164.

 

3.   Horwich, A.L., Cheng, M., West, A. and Pollock, R.A. (1991). Mitochondrial protein import. In Current Topics in Microbiology and Immunology, vol. 170. R.W. Compans, ed. Springer-Verlag, Berlin-Heidelberg-New York. pp. 1-42.

 

4.   West, A.H., Clark, D.J., Martin, J., Neupert, W., Hartl, F.-U. and Horwich, A.L. (1992). Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein. J. Biol. Chem. 267: 24625-24633.

 

5.   Stock, A.M., Martinez-Hackert, E., Rasmussen, B.F., West, A.H., Stock, J.B., Ringe, D. and Petsko, G.A. (1993). Structure of the Mg2+-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry 32: 13376-13380.

 

6.   West, A.H., Martinez-Hackert, E. and Stock, A.M. (1994). Structural basis for the mechanism of phosphoryl transfer in bacterial chemotaxis. In Phosphate in Microorganisms. Cellular and Molecular Biology, A. Torriani-Gorini, E. Yagil, and S. Silver, eds., Amer. Soc. Microbiol. Press, Wash., D.C., pp. 309-314.

 

7.   West, A.H., Djordjevic, S., Martinez-Hackert, E. and Stock, A.M. (1995). Purification, crystallization, and preliminary X-ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes. Proteins: Struct., Funct., and Genet. 21: 345-350.

 

8.   West, A.H., Martinez-Hackert, E. and Stock, A.M. (1995). Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB. J. Mol. Biol.  250: 276-290.

 

9.   Djordjevic, S., Goudreau, P.N, Xu, Q., Stock, A.M. and West, A.H. (1998). Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain. Proc. Natl. Acad. Sci. (USA). 95: 1381-1386.

 

10. Xu, Q., Nguyen, V. and West, A.H. (1999). Purification, crystallization, and preliminary X‑ray diffraction analysis of the yeast phosphorelay protein YPD1. Acta Cryst. D55: 291-293.

 

11. Janiak-Spens, F., Sparling, J.M., Gurfinkel, M. and West, A.H. (1999). Differential stabilities of phosphorylated response regulator domains reflect functional roles of the yeast osmoregulatory SLN1 and SSK1 proteins. J. Bacteriol. 181: 411-417.

 

12. Xu, Q. and West, A.H. (1999). Conservation of structure and function among histidine-containing phosphotransfer (HPt) domains as revealed by the crystal structure of YPD1. J. Mol. Biol. 292: 1039-1050.

 

13. Janiak-Spens, F. and West, A.H. (2000). Functional roles of conserved amino acid residues surrounding the phosphorylatable histidine of the yeast phosphorelay protein YPD1. Mol. Microbiol. 37: 136-144.

 

14. Janiak-Spens, F., Sparling, D.P. and West, A.H. (2000). Novel role for an HPt domain in stabilizing the phosphorylated state of a response regulator domain. J. Bacteriol. 182: 6673-6678.

 

15. West, A.H. and Stock, A.M. (2001). Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 26: 369-376.

 

16. Bourret, R.B, Charon, N.W, Stock, A.M. and West, A.H. (2002). Bright lights, abundant operons – fluorescence and genomic technologies advance studies of bacterial locomotion and signal transduction: Review of the BLAST meeting, Cuernavaca, Mexico, 14 to 19 January 2001. J. Bacteriol. 184: 1-17.

 

17. Lee, J., Chen, L., West, A.H. and Richter-Addo, G.B. (2002). Interactions of organic nitroso compounds with metals. Chem. Rev. 102: 1019-1065.

 

18. Stock, A.M. and West, A.H. (2003). Response regulator proteins and their interactions with histidine protein kinases. In Histidine Kinases in Signal Transduction M. Inouye and R. Dutta, eds., Academic Press, San Diego, pp. 237-271.

 

19. Porter, S.W., Xu, Q. and West, A.H. (2003). Ssk1p response regulator binding surface on histidine-containing phosphotransfer protein Ypd1p. Euk. Cell 2: 27-33. 

 

20. Chooback, L. and West, A.H. (2003). Co-crystallization of the yeast phosphorelay protein YPD1 with the SLN1 response regulator domain and preliminary X-ray diffraction analysis. Acta Cryst. D59: 927-929.

 

21. Janiak-Spens, F. and West, A.H. (2003). Histidine kinases. In Handbook of Cell Signaling. R.A. Bradshaw and E.A. Dennis, eds., Academic Press, San Diego, pp. 563-566.

 

22. Copeland, D. M., West, A.H. and Richter-Addo, G.B. (2003). Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane. Proteins: Str., Funct. Genet., 53: 182-192.

 

23. Xu, Q., Porter, S.W. and West, A.H. (2003). The yeast YPD1/SLN1 complex: Insights into molecular recognition in two-component signaling systems. Structure 11: 1569-1581.

 

24. Andi, B., West, A.H. and Cook, P.F. (2004). Stabilization and characterization of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae. Arch. Biochem. Biophys. 421: 243-254.

 

25. Perez, E., West, A.H., Stock, A.M. and Djordjevic, S. (2004). Discrimination between different methylation states of chemotaxis receptor Tar by receptor methyltransferase CheR. Biochemistry 43: 953-961.

 

26. Andi, B., West, A.H. and Cook, P.F. (2004). Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae. Biochemistry 43: 11790-11795.

 

27. Janiak-Spens, Cook, P.F. and West, A.H. (2005). Kinetic analysis of YPD1-dependent phosphotransfer reactions in the yeast osmoregulatory phosphorelay system. Biochemistry, Biochemistry 44: 377-386.

 

28. Porter, S.W. and West, A.H. (2005). A common docking site for response regulators on the yeast phosphorelay protein YPD1. Biochim. Biophys. Acta 1748: 138-145.

 

29. Andi, B., West, A.H. and Cook, P.F. (2005). Regulatory mechanism of histidine-tagged homocitrate synthase from S. cerevisiae: I. Kinetic studies. J. Biol. Chem. 280: 31624-31632.

 

30. Andi, B., Cook, P.F. and West, A.H. (2006). Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-Å resolution. Cell Biochem. Biophys. 46: 17-26.

31. Xu, H., Andi, B., Qian, J., West, A.H. and Cook, P.F. (2006). The a-aminoadipate pathway for lysine biosynthesis in fungi. Cell Biochem. Biophys. 46: 43-64.

 

32. Copeland, D.M., Soares, A.S., West, A.H. and Richter-Addo, G.B. (2006). Crystal structures of nitrite and nitric oxide complexes of horse heart myoglobin. J. Inorg. Biochem. 100: 1413-1425.

 

33. Qian, J., West, A.H. and Cook, P.F. (2006). Acid-base chemical mechanism of homocitrate synthase from Saccharomyces cerevisiae. Biochemistry 45: 12136-12143.

 

34. Xu, H., West, A.H. and Cook, P.F. (2006). Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry 45: 12156-12166.

 

35. Menon, V., Li, D., Chauhan, N., Rajnarayanan, R., Dubrovska, A., West, A.H. and Calderone, R. (2006). Functional studies of the Ssk1p response regulator protein of Candida albicans as determined by phenotypic analysis of receiver domain point mutants. Mol. Microbiol. 62: 997-1013.

 

36. Xu, H., Alguindigue, S., West, A.H. and Cook, P.F. (2007). A proposed proton shuttle mechanism for saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry 46: 871-882.

 

37. Lin, Y., Alguindigue, S., Volkman, J., Nicholas, K.M., West, A.H. and Cook, P.F. (2007). Complete kinetic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry 46: 890-898.

 

38. Xu, H., West, A.H. and Cook, P.F. (2007). Determinants of substrate specificity for saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry 46: 7625-7636.

 

39. Tan, H., Janiak-Spens, F. and West, A.H. (2007). Functional characterization of the phosphorelay protein Mpr1p from Schizosaccharomyces pombe. FEMS Yeast Res. 7: 912-921.

 

40. Zahran, Z.N., Chooback, L., Copeland, D.M., West, A.H. and Richter-Addo, G.B. (2007). Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations. J. Inorg. Biochem. In press, published on-line: doi:10.1016/j.jinorgbio.2007.08.002

 

41. Andi, B., Cook, P.F. and West, A.H. (2007). Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae.  Biochemistry, In press.