Year |
Citation |
Score |
2014 |
Edenberg HJ, Bosron WF. Alcohol Dehydrogenases Reference Module in Biomedical Research. DOI: 10.1016/B978-0-12-801238-3.01962-0 |
0.393 |
|
2009 |
Sanghani SP, Sanghani PC, Schiel MA, Bosron WF. Human carboxylesterases: an update on CES1, CES2 and CES3. Protein and Peptide Letters. 16: 1207-14. PMID 19508181 DOI: 10.2174/092986609789071324 |
0.767 |
|
2007 |
Janecki DJ, Bemis KG, Tegeler TJ, Sanghani PC, Zhai L, Hurley TD, Bosron WF, Wang M. A multiple reaction monitoring method for absolute quantification of the human liver alcohol dehydrogenase ADH1C1 isoenzyme. Analytical Biochemistry. 369: 18-26. PMID 17692277 DOI: 10.1016/J.Ab.2007.06.043 |
0.629 |
|
2007 |
Schiel MA, Green SL, Davis WI, Sanghani PC, Bosron WF, Sanghani SP. Expression and characterization of a human carboxylesterase 2 splice variant. The Journal of Pharmacology and Experimental Therapeutics. 323: 94-101. PMID 17636009 DOI: 10.1124/Jpet.107.127027 |
0.744 |
|
2005 |
Quinney SK, Sanghani SP, Davis WI, Hurley TD, Sun Z, Murry DJ, Bosron WF. Hydrolysis of capecitabine to 5'-deoxy-5-fluorocytidine by human carboxylesterases and inhibition by loperamide. The Journal of Pharmacology and Experimental Therapeutics. 313: 1011-6. PMID 15687373 DOI: 10.1124/Jpet.104.081265 |
0.695 |
|
2004 |
Sanghani SP, Quinney SK, Fredenburg TB, Davis WI, Murry DJ, Bosron WF. Hydrolysis of irinotecan and its oxidative metabolites, 7-ethyl-10-[4-N-(5-aminopentanoic acid)-1-piperidino] carbonyloxycamptothecin and 7-ethyl-10-[4-(1-piperidino)-1-amino]-carbonyloxycamptothecin, by human carboxylesterases CES1A1, CES2, and a newly expressed carboxylesterase isoenzyme, CES3. Drug Metabolism and Disposition: the Biological Fate of Chemicals. 32: 505-11. PMID 15100172 DOI: 10.1124/Dmd.32.5.505 |
0.417 |
|
2004 |
Sun Z, Murry DJ, Sanghani SP, Davis WI, Kedishvili NY, Zou Q, Hurley TD, Bosron WF. Methylphenidate is stereoselectively hydrolyzed by human carboxylesterase CES1A1. The Journal of Pharmacology and Experimental Therapeutics. 310: 469-76. PMID 15082749 DOI: 10.1124/Jpet.104.067116 |
0.696 |
|
2003 |
Sanghani SP, Quinney SK, Fredenburg TB, Sun Z, Davis WI, Murry DJ, Cummings OW, Seitz DE, Bosron WF. Carboxylesterases expressed in human colon tumor tissue and their role in CPT-11 hydrolysis. Clinical Cancer Research : An Official Journal of the American Association For Cancer Research. 9: 4983-91. PMID 14581373 |
0.477 |
|
2003 |
Sanghani PC, Robinson H, Bennett-Lovsey R, Hurley TD, Bosron WF. Structure-function relationships in human Class III alcohol dehydrogenase (formaldehyde dehydrogenase). Chemico-Biological Interactions. 143: 195-200. PMID 12604204 DOI: 10.1016/S0009-2797(02)00203-X |
0.691 |
|
2002 |
Sanghani PC, Bosron WF, Hurley TD. Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation. Biochemistry. 41: 15189-94. PMID 12484756 DOI: 10.1021/Bi026705Q |
0.668 |
|
2002 |
Sanghani SP, Davis WI, Dumaual NG, Mahrenholz A, Bosron WF. Identification of microsomal rat liver carboxylesterases and their activity with retinyl palmitate. European Journal of Biochemistry / Febs. 269: 4387-98. PMID 12230550 DOI: 10.1046/J.1432-1033.2002.03121.X |
0.362 |
|
2002 |
Sanghani PC, Robinson H, Bosron WF, Hurley TD. Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes. Biochemistry. 41: 10778-86. PMID 12196016 DOI: 10.1021/Bi0257639 |
0.699 |
|
2002 |
Satoh T, Taylor P, Bosron WF, Sanghani SP, Hosokawa M, La Du BN. Current progress on esterases: from molecular structure to function. Drug Metabolism and Disposition: the Biological Fate of Chemicals. 30: 488-93. PMID 11950776 DOI: 10.1124/Dmd.30.5.488 |
0.311 |
|
2002 |
Bosron WF, Hurley TD. Lessons from a bacterial cocaine esterase. Nature Structural Biology. 9: 4-5. PMID 11753424 DOI: 10.1038/Nsb0102-4 |
0.557 |
|
2001 |
Ramchandani VA, Bosron WF, Li TK. Research advances in ethanol metabolism Pathologie Biologie. 49: 676-682. PMID 11762128 DOI: 10.1016/S0369-8114(01)00232-2 |
0.447 |
|
2001 |
Crabb DW, Pinairs J, Hasanadka R, Fang M, Leo MA, Lieber CS, Tsukamoto H, Motomura K, Miyahara T, Ohata M, Bosron W, Sanghani S, Kedishvili N, Shiraishi H, Yokoyama H, et al. Alcohol and Retinoids Alcoholism: Clinical and Experimental Research. 25: 207S-217S. DOI: 10.1111/J.1530-0277.2001.Tb02398.X |
0.401 |
|
2000 |
Sanghani PC, Stone CL, Ray BD, Pindel EV, Hurley TD, Bosron WF. Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase Biochemistry. 39: 10720-10729. PMID 10978156 DOI: 10.1021/Bi9929711 |
0.671 |
|
2000 |
Humerickhouse R, Lohrbach K, Li L, Bosron WF, Dolan ME. Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms hCE-1 and hCE-2 Cancer Research. 60: 1189-1192. PMID 10728672 |
0.314 |
|
1999 |
Zhang J, Burnell JC, Dumaual N, Bosron WF. Binding and hydrolysis of meperidine by human liver carboxylesterase hCE-1. The Journal of Pharmacology and Experimental Therapeutics. 290: 314-8. PMID 10381793 |
0.379 |
|
1999 |
Stone CL, Jipping MB, Owusu-Dekyi K, Hurley TD, Li TK, Bosron WF. The pH-dependent binding of NADH and subsequent enzyme isomerization of human liver β3β3 alcohol dehydrogenase Biochemistry. 38: 5829-5835. PMID 10231534 DOI: 10.1021/Bi982944V |
0.655 |
|
1998 |
Kedishvili NY, Gough WH, Davis WI, Parsons S, Li TK, Bosron WF. Effect of cellular retinol-binding protein on retinol oxidation by human class IV retinol/alcohol dehydrogenase and inhibition by ethanol Biochemical and Biophysical Research Communications. 249: 191-196. PMID 9705855 DOI: 10.1006/Bbrc.1998.9105 |
0.431 |
|
1997 |
Xie P, Parsons SH, Speckhard DC, Bosron WF, Hurley TD. X-ray structure of human class IV σσ alcohol dehydrogenase. Structural basis for substrate specificity Journal of Biological Chemistry. 272: 18558-18563. PMID 9228021 DOI: 10.1074/Jbc.272.30.18558 |
0.695 |
|
1997 |
Pindel EV, Kedishvili NY, Abraham TL, Brzezinski MR, Zhang J, Dean RA, Bosron WF. Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin Journal of Biological Chemistry. 272: 14769-14775. PMID 9169443 DOI: 10.1074/Jbc.272.23.14769 |
0.415 |
|
1997 |
Kedishvili NY, Gough WH, Chernoff EA, Hurley TD, Stone CL, Bowman KD, Popov KM, Bosron WF, Li TK. cDNA sequence and catalytic properties of a chick embryo alcohol dehydrogenase that oxidizes retinol and 3beta,5alpha-hydroxysteroids. The Journal of Biological Chemistry. 272: 7494-500. PMID 9054452 DOI: 10.1074/Jbc.272.11.7494 |
0.697 |
|
1997 |
Yang ZN, Bosron WF, Hurley TD. Structure of human χχ alcohol dehydrogenase: A glutathione-dependent formaldehyde dehydrogenase Journal of Molecular Biology. 265: 330-343. PMID 9018047 DOI: 10.1006/Jmbi.1996.0731 |
0.692 |
|
1996 |
Davis GJ, Bosron WF, Stone CL, Owusu-Dekyi K, Hurley TD. X-ray structure of human β3β3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding Journal of Biological Chemistry. 271: 17057-17061. PMID 8663387 DOI: 10.1074/Jbc.271.29.17057 |
0.617 |
|
1995 |
Kedishvili NY, Bosron WF, Stone CL, Hurley TD, Peggs CF, Thomasson HR, Popov KM, Carr LG, Edenberg HJ, Li TK. Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase: Active-site amino acid sequence explains substrate specificity compared with liver isozymes Journal of Biological Chemistry. 270: 3625-3630. PMID 7876099 DOI: 10.1074/Jbc.270.8.3625 |
0.714 |
|
1995 |
Stone CL, Hurley TD, Peggs CF, Kedishvili NY, Davis GJ, Thomasson HR, Li TK, Bosron WF. Cimetidine inhibition of human gastric and liver alcohol dehydrogenase isoenzymes: Identification of inhibitor complexes by kinetics and molecular modeling Biochemistry. 34: 4008-4014. PMID 7696266 DOI: 10.1021/Bi00012A019 |
0.678 |
|
1995 |
Kedishvili NY, Bosron WF, Stone CL, Peggs CF, Thomasson HR, Popov KM, Carr LG, Hurley TD, Edenberg HJ, Li TK. Cloning and expression of a human stomach alcohol dehydrogenase isozyme Advances in Experimental Medicine and Biology. 372: 341-347. PMID 7484396 DOI: 10.1007/978-1-4615-1965-2_41 |
0.634 |
|
1995 |
Ma Y, Bosron WF, Mieli-Vergani G, Vergani D. 100 ALCOHOL DEHYDROGENASE Journal of Pediatric Gastroenterology and Nutrition. 20: 470. DOI: 10.1097/00005176-199505000-00110 |
0.31 |
|
1994 |
Davis GJ, Carr LG, Hurley TD, Li TK, Bosron WF. Comparative Roles of Histidine-51 in Human β1β1 and Threonine-51 in ππ Alcohol Dehydrogenases Archives of Biochemistry and Biophysics. 311: 307-312. PMID 8203892 DOI: 10.1006/Abbi.1994.1242 |
0.677 |
|
1994 |
Hurley TD, Bosron WF, Stone CL, Amzel LM. Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences. Journal of Molecular Biology. 239: 415-29. PMID 8201622 DOI: 10.1006/Jmbi.1994.1382 |
0.741 |
|
1994 |
Brzezinski MR, Abraham TL, Stone CL, Dean RA, Bosron WF. Purification and characterization of a human liver cocaine carboxylesterase that catalyzes the production of benzoylecgonine and the formation of cocaethylene from alcohol and cocaine Biochemical Pharmacology. 48: 1747-1755. PMID 7980644 DOI: 10.1016/0006-2952(94)90461-8 |
0.41 |
|
1994 |
Yang ZN, Davis GJ, Hurley TD, Stone CL, Li TK, Bosron WF. Catalytic efficiency of human alcohol dehydrogenases for retinol oxidation and retinal reduction Alcoholism: Clinical and Experimental Research. 18: 587-591. PMID 7943659 DOI: 10.1111/J.1530-0277.1994.Tb00914.X |
0.606 |
|
1993 |
Ehrig T, Muhoberac BB, Brems D, Bosron WF. Monomers of human β1β1 alcohol dehydrogenase exhibit activity that differs from the dimer Journal of Biological Chemistry. 268: 11721-11726. PMID 8505301 |
0.322 |
|
1993 |
Hurley TD, Yang Z, Bosron WF, Weiner H. Crystallization and preliminary X-ray analysis of bovine mitochondrial aldehyde dehydrogenase and human glutathione-dependent formaldehyde dehydrogenase Advances in Experimental Medicine and Biology. 328: 245-250. PMID 8493900 DOI: 10.1007/978-1-4615-2904-0_26 |
0.578 |
|
1993 |
Stone CL, Bosron WF, Dunn MF. Amino acid substitutions at position 47 of human β1β1 and β2β2 alcohol dehydrogenases affect hydride transfer and coenzyme dissociation rate constants Journal of Biological Chemistry. 268: 892-899. PMID 8419368 |
0.305 |
|
1993 |
Stone CL, Hurley TD, Amzel LM, Dunn MF, Bosron WF. Kinetics of a glycine for Arg-47 human alcohol dehydrogenase mutant can be explained by Lys-228 recruitment into the pyrophosphate binding site. Advances in Experimental Medicine and Biology. 328: 429-37. PMID 8388156 DOI: 10.1007/978-1-4615-2904-0_45 |
0.732 |
|
1993 |
Bosron WF, Ehrig T, Li TK. Genetic factors in alcohol metabolism and alcoholism Seminars in Liver Disease. 13: 126-135. PMID 8337601 DOI: 10.1055/S-2007-1007344 |
0.392 |
|
1993 |
Stone CL, Thomasson HR, Bosron WF, Li TK. Purification and partial amino acid sequence of a high-activity human stomach alcohol dehydrogenase Alcoholism: Clinical and Experimental Research. 17: 911-918. PMID 8214434 DOI: 10.1111/J.1530-0277.1993.Tb00863.X |
0.477 |
|
1993 |
Hurley TD, Bosron WF, Mario Amzel L. Human alcohol dehydrogenase: Design of a secondary alcohol dehydrogenase using crystallography and mutagenesis Protein Engineering, Design and Selection. 6: 44. DOI: 10.1093/Protein/6.Supplement.44-A |
0.664 |
|
1992 |
Ehrig T, Muhoberac BB, Hurley TD, Bosron WF. Tryptophan fluorescence quenching by alkaline pH and ternary complex formation in human β1β1 and horse EE alcohol dehydrogenases Febs Letters. 300: 283-285. PMID 1555656 DOI: 10.1016/0014-5793(92)80864-D |
0.62 |
|
1992 |
Hurley TD, Bosron WF. Human alcohol dehydrogenase: Dependence of secondary alcohol oxidation on the amino acids at positions 93 and 94 Biochemical and Biophysical Research Communications. 183: 93-99. PMID 1543513 DOI: 10.1016/0006-291X(92)91613-U |
0.672 |
|
1991 |
Hurley TD, Ehrig T, Edenberg HJ, Bosron WF. Characterization of human alcohol dehydrogenases containing substitutions at amino acids 47 and 51 Advances in Experimental Medicine and Biology. 284: 271-275. PMID 2053482 DOI: 10.1007/978-1-4684-5901-2_29 |
0.694 |
|
1991 |
Ehrig T, Hurley TD, Edenberg HJ, Bosron WF. General Base Catalysis in a Glutamine for Histidine Mutant at Position 51 of Human Liver Alcohol Dehydrogenase Biochemistry. 30: 1062-1068. PMID 1989677 DOI: 10.1021/Bi00218A026 |
0.696 |
|
1991 |
Dean RA, Christian CD, Sample RHB, Bosron WF. Human liver cocaine esterases: Ethanol-mediated formation of ethylcocaine Faseb Journal. 5: 2735-2739. PMID 1916095 DOI: 10.1096/Fasebj.5.12.1916095 |
0.308 |
|
1991 |
Hurley TD, Bosron WF, Hamilton JA, Amzel LM. Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions. Proceedings of the National Academy of Sciences of the United States of America. 88: 8149-53. PMID 1896463 DOI: 10.1073/Pnas.88.18.8149 |
0.745 |
|
1990 |
Hurley TD, Edenberg HJ, Bosron WF. Expression and kinetic characterization of variants of human β1β1 alcohol dehydrogenase containing substitutions at amino acid 47 Journal of Biological Chemistry. 265: 16366-16372. PMID 2398055 |
0.692 |
|
1990 |
Ehrig T, Bosron WF, Li TK. Alcohol and aldehyde dehydrogenase Alcohol and Alcoholism (Oxford, Oxfordshire). 25: 105-116. PMID 2198030 DOI: 10.1093/Oxfordjournals.Alcalc.A044985 |
0.503 |
|
1989 |
Burnell JC, Li TK, Bosron WF. Purification and steady-state kinetic characterization of human liver beta 3 beta 3 alcohol dehydrogenase. Biochemistry. 28: 6810-5. PMID 2819035 DOI: 10.1021/Bi00443A005 |
0.312 |
|
1989 |
Stone CL, Li TK, Bosron WF. Stereospecific oxidation of secondary alcohols by human alcohol dehydrogenases Journal of Biological Chemistry. 264: 11112-11116. PMID 2738060 |
0.377 |
|
1989 |
Stone CL, Burnell JC, Li TK, Bosron WF. Relationships between the kinetics of alcohol or coenzyme oxidoreduction and amino acid sequence of human liver alcohol dehydrogenase isoenzymes. Progress in Clinical and Biological Research. 290: 155-65. PMID 2726815 |
0.357 |
|
1989 |
Crabb DW, Edenberg HJ, Bosron WF, Li TK. Genotypes for aldehyde dehydrogenase deficiency and alcohol sensitivity. The inactive ALDH22 allele is dominant Journal of Clinical Investigation. 83: 314-316. PMID 2562960 DOI: 10.1172/Jci113875 |
0.481 |
|
1988 |
Xu Y, Carr LG, Bosron WF, Li TK, Edenberg HJ. Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification Genomics. 2: 209-214. PMID 3397059 DOI: 10.1016/0888-7543(88)90004-3 |
0.426 |
|
1988 |
Bosron WF, Lumeng L, Li TK. Genetic polymorphism of enzymes of alcohol metabolism and susceptibility to alcoholic liver disease Molecular Aspects of Medicine. 10: 147-158. PMID 3067025 DOI: 10.1016/0098-2997(88)90019-2 |
0.49 |
|
1987 |
Rex DK, Patterson LS, Edenberg HJ, Bosron WF. Structure and expression of mouse liver alcohol dehydrogenase isoenzymes Progress in Clinical and Biological Research. 232: 237-243. PMID 3615423 |
0.345 |
|
1987 |
Rex DK, Bosron WF, Dwulet F, Li TK. Purification and characterization of the Danish (skive) variant of mouse liver alcohol dehydrogenase Biochemical Genetics. 25: 111-121. PMID 3579863 DOI: 10.1007/Bf00498955 |
0.446 |
|
1987 |
Bosron WF, Li TK. Catalytic properties of human liver alcohol dehydrogenase isoenzymes Enzyme. 37: 19-28. PMID 3569190 |
0.376 |
|
1987 |
Johnson CT, Bosron WF, Harden CA, Li TK. Purification of human liver aldehyde dehydrogenase by high-performance liquid chromatography and identification of isoenzymes by immunoblotting Alcoholism: Clinical and Experimental Research. 11: 60-65. PMID 3551665 DOI: 10.1111/J.1530-0277.1987.Tb01264.X |
0.381 |
|
1987 |
Li TK, Bosron WF. Distribution and properties of human alcohol dehydrogenase isoenzymes Annals of the New York Academy of Sciences. 1-10. PMID 3474918 DOI: 10.1111/J.1749-6632.1987.Tb48648.X |
0.433 |
|
1987 |
Zhang K, Bosron WF, Edenberg HJ. Structure of the mouse Adh-1 gene and identification of a deletion in a long alternating purine-pyrimidine sequence in the first intron of strains expressing low alcohol dehydrogenase activity Gene. 57: 27-36. PMID 3428612 DOI: 10.1016/0378-1119(87)90173-9 |
0.332 |
|
1987 |
Patterson LS, Zhang K, Edenberg HJ, Bosron WF. Genetic control of liver alcohol dehydrogenase expression in inbred mice Alcohol and Alcoholism (Oxford, Oxfordshire). 157-159. PMID 3426672 |
0.302 |
|
1986 |
Li TK, Bosron WF. Genetic variability of enzymes of alcohol metabolism in human beings Annals of Emergency Medicine. 15: 997-1004. PMID 3526998 DOI: 10.1016/S0196-0644(86)80118-4 |
0.482 |
|
1986 |
Bosron WF, Li TK. Genetic polymorphism of human liver alcohol and aldehyde dehydrogenases, and their relationship to alcohol metabolism and alcoholism Hepatology. 6: 502-510. PMID 3519419 DOI: 10.1002/Hep.1840060330 |
0.479 |
|
1986 |
Bosron WF. Selective carboxymethylation of cysteine-174 of the β2β2 and β1β1 human liver alcohol dehydrogenase isoenzymes by lodoacetate1 Biochemistry. 25: 1876-1881. PMID 2939875 DOI: 10.1021/Bi00356A006 |
0.521 |
|
1986 |
Crabb DW, Bosron WF, Ting-Kai Li. Role of the pituitary and neonatal androgenic imprinting in the hormonal regulation of liver alcohol dehydrogenase activity Biochemical Pharmacology. 35: 1527-1532. PMID 2939837 DOI: 10.1016/0006-2952(86)90120-6 |
0.425 |
|
1985 |
Bosron WF, Gaither JW, Magnes LJ. Kinetic characterization of two classes of dog liver alcohol dehydrogenase isoenzymes Alcoholism: Clinical and Experimental Research. 9: 228-234. PMID 3893194 DOI: 10.1111/J.1530-0277.1985.Tb05740.X |
0.461 |
|
1985 |
Rex DK, Bosron WF, Smialek JE, Li TK. Alcohol and aldehyde dehydrogenase isoenzymes in North American Indians Alcoholism: Clinical and Experimental Research. 9: 147-152. PMID 3159308 |
0.302 |
|
1985 |
Edenberg HJ, Zhang K, Fong K, Bosron WF, Li TK. Cloning and sequencing of cDNA encoding the complete mouse liver alcohol dehydrogenase Proceedings of the National Academy of Sciences of the United States of America. 82: 2262-2266. PMID 3157987 DOI: 10.1073/Pnas.82.8.2262 |
0.438 |
|
1984 |
Bosron WF, Crabb DW, Housinger TA, Li TK. Effect of fasting on the activity and turnover of rat liver alcohol dehydrogenase Alcoholism: Clinical and Experimental Research. 8: 196-200. PMID 6375431 DOI: 10.1111/J.1530-0277.1984.Tb05837.X |
0.426 |
|
1984 |
Yin SJ, Bosron WF, Li TK, Ohnishi K, Okuda K, Ishii H, Tsuchiya M. Polymorphism of human liver alcohol dehydrogenase: Identification of ADH2 2-1 and ADH2 2-2 phenotypes in the Japanese by isoelectric focusing Biochemical Genetics. 22: 169-180. PMID 6370230 DOI: 10.1007/Bf00499296 |
0.313 |
|
1984 |
Rex DK, Bosron WF, Li TK. Purification and characterization of mouse alcohol dehydrogenase from two inbred strains that differ in total liver enzyme activity Biochemical Genetics. 22: 115-124. PMID 6370228 DOI: 10.1007/Bf00499291 |
0.416 |
|
1984 |
Bosron WF, Yin SJ, Li TK. Inactivation of the human liver alcohol dehydrogenase β2β2 and β1β1 isoenzymes by iodacetate Federation Proceedings. 43: no. 751. |
0.363 |
|
1984 |
Yin SJ, Bosron WF, Magnes LJ, Li TK. Purification and kinetic characterization of human liver alcohol dehydrogenase isoenzymes containing β2 subunits Federation Proceedings. 43: no. 2669. |
0.37 |
|
1983 |
Bosron WF, Crabb DW, Ting-Kai Li. Relationship between kinetics of liver alcohol dehydrogenase and alcohol metabolism Pharmacology, Biochemistry and Behavior. 18: 223-227. PMID 6356161 DOI: 10.1016/0091-3057(83)90175-2 |
0.404 |
|
1983 |
Bosron WF, Magnes LJ, Li TK. Human liver alcohol dehydrogenase: ADHIndianapolis results from genetic polymorphism at the ADH2 gene locus Biochemical Genetics. 21: 735-744. PMID 6354175 DOI: 10.1007/Bf00498920 |
0.45 |
|
1983 |
Crabb DW, Bosron WF, Li TK. Steady-state kinetic properties of purified rat liver alcohol dehydrogenase: Application to predicting alcohol elimination rates in vivo Archives of Biochemistry and Biophysics. 224: 299-309. PMID 6347067 DOI: 10.1016/0003-9861(83)90213-8 |
0.457 |
|
1983 |
Bosron WF, Magnes LJ, Li TK. Kinetic and electrophoretic properties of native and recombined isoenzymes of human liver alcohol dehydrogenase Biochemistry. 22: 1852-1857. PMID 6342668 DOI: 10.1021/Bi00277A017 |
0.42 |
|
1981 |
Bosron WF, Li TK. Genetic determinants of alcohol and aldehyde dehydrogenases and alcohol metabolism Seminars in Liver Disease. 1: 179-188. PMID 7051301 DOI: 10.1055/S-2008-1041746 |
0.412 |
|
1981 |
Dafeldecker WP, Parés X, Vallee BL, Bosron WF, Li TK. Simian liver alcohol dehydrogenase: Isolation and characterization of isoenzymes from Saimiri sciureus Biochemistry. 20: 856-861. PMID 7011375 DOI: 10.1021/Bi00507A031 |
0.636 |
|
1980 |
Lumeng L, Bosron WF, Li TK. Rate-determining factors for ethanol metabolism in vivo during fasting Advances in Experimental Medicine and Biology. 132: 489-496. PMID 7424728 DOI: 10.1007/978-1-4757-1419-7_50 |
0.314 |
|
1980 |
Bosron WF, Li TK, Vallee BL. New molecular forms of human liver alcohol dehydrogenase: Isolation and characterization of ADH(Indianapolis) Proceedings of the National Academy of Sciences of the United States of America. 77: 5784-5788. PMID 7003596 DOI: 10.1073/Pnas.77.10.5784 |
0.612 |
|
1979 |
Bosron WF, Li TK, Vallee BL. Heterogeneity and new molecular forms of human liver alcohol dehydrogenase Biochemical and Biophysical Research Communications. 91: 1549-1555. PMID 526323 DOI: 10.1016/0006-291X(79)91241-5 |
0.63 |
|
1979 |
Lumeng L, Bosron WF, Ting-Kai L. Quantitative correlation of ethanol elimination rates in vivo with liver alcohol dehydrogenase activities in fed, fasted and food-restricted rats Biochemical Pharmacology. 28: 1547-1551. PMID 475866 DOI: 10.1016/0376-8716(79)90055-3 |
0.349 |
|
1979 |
Bosron WF, Li TK, Dafeldecker WP, Vallee BL. Human liver π-alcohol dehydrogenase: Kinetic and molecular properties Biochemistry. 18: 1101-1105. PMID 427099 DOI: 10.1021/Bi00573A026 |
0.63 |
|
1977 |
Bosron WF, Li TK, Lange LG, Dafeldecker WP, Vallee BL. Isolation and characterization of an anodic form of human liver alcohol dehydrogenase Biochemical and Biophysical Research Communications. 74: 85-91. PMID 836289 DOI: 10.1016/0006-291X(77)91378-X |
0.631 |
|
1977 |
Li TK, Bosron WF, Dafeldecker WP. Isolation of II-alcohol dehydrogenase of human liver: is it a determinant of alcoholism? Proceedings of the National Academy of Sciences of the United States of America. 74: 4378-4381. PMID 270680 DOI: 10.1073/Pnas.74.10.4378 |
0.504 |
|
1977 |
Bosron WF, Anderson RA, Falk MC, Kennedy FS, Vallee BL. Effect of magnesium on the properties of zinc alkaline phosphatase. Biochemistry. 16: 610-4. PMID 13822 DOI: 10.1021/Bi00623A009 |
0.538 |
|
1975 |
Anderson RA, Bosron WF, Kennedy FS, Vallee BL. Role of magnesium in Escherichia coli alkaline phosphatase. Proceedings of the National Academy of Sciences of the United States of America. 72: 2989-93. PMID 1103131 DOI: 10.1073/Pnas.72.8.2989 |
0.503 |
|
1975 |
Bosron WF, Vallee BL. Effect of phosphate on multiple forms of Escherechia coli alkaline phosphatase Biochemical and Biophysical Research Communications. 66: 809-813. PMID 1101892 DOI: 10.1016/0006-291X(75)90581-1 |
0.467 |
|
1975 |
Bosron WF, Kennedy FS, Vallee BL. Zinc and magnesium content of alkaline phosphatase from Escherichia coli. Biochemistry. 14: 2275-82. PMID 238559 DOI: 10.1021/Bi00681A036 |
0.495 |
|
1973 |
Bosron WF, Prairie RL. Reduced triphosphopyridine-linked aldehyde reductase II. Species and tissue distribution Archives of Biochemistry and Biophysics. 154: 166-172. PMID 4144052 DOI: 10.1016/0003-9861(73)90045-3 |
0.767 |
|
1972 |
Bosron WF, Prairie RL. Triphosphopyridine nucleotide-linked aldehyde reductase. I. Purification and properties of the enzyme from pig kidney cortex Journal of Biological Chemistry. 247: 4480-4485. PMID 4402936 |
0.751 |
|
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