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Journal of Molecular Biology|June 10, 1994
Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differencesT D Hurley, W F Bosron, C L Stone, et al.Proceedings of the National Academy of Sciences of the United States of America|September 15, 1991
Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutionsT D Hurley, W F Bosron, J A Hamilton, et al.Biochemical and Biophysical Research Communications|February 28, 1992
Human alcohol dehydrogenase: dependence of secondary alcohol oxidation on the amino acids at positions 93 and 94T D Hurley, W F BosronThe Journal of Biological Chemistry|July 19, 1996
X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme bindingG J Davis, W F Bosron, C L Stone, et al.Biochemistry|May 8, 1999
The pH-dependent binding of NADH and subsequent enzyme isomerization of human liver beta 3 beta 3 alcohol dehydrogenaseC L Stone, M B Jipping, K Owusu-Dekyi, et al.Biochemistry|September 9, 2000
Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenaseP C Sanghani, C L Stone, B D Ray, et al.Alcoholism, Clinical and Experimental Research|June 1, 1994
Catalytic efficiency of human alcohol dehydrogenases for retinol oxidation and retinal reductionZ N Yang, G J Davis, T D Hurley, et al.The Journal of Biological Chemistry|September 25, 1990
Expression and kinetic characterization of variants of human beta 1 beta 1 alcohol dehydrogenase containing substitutions at amino acid 47T D Hurley, H J Edenberg, W F BosronJournal of Molecular Biology|January 24, 1997
Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenaseZ N Yang, W F Bosron, T D HurleyThe Journal of Biological Chemistry|July 5, 1989
Stereospecific oxidation of secondary alcohols by human alcohol dehydrogenasesC L Stone, T K Li, W F BosronPageof 17