His primary scientific interests are in Biochemistry, Enzyme, Alcohol dehydrogenase, Isozyme and Ethanol metabolism. All of his Biochemistry and Carboxylesterase and Isoelectric focusing investigations are sub-components of the entire Biochemistry study. His work deals with themes such as Zinc, Metal and Phosphate, which intersect with Enzyme.
His Alcohol dehydrogenase study incorporates themes from Proteomics, Quantitative proteomics, Branched-chain alpha-keto acid dehydrogenase complex, ADH1B and NAD+ kinase. His Isozyme research focuses on subjects like Gene, which are linked to Hydrolase, Molecular biology and Topoisomerase. His Ethanol metabolism research incorporates themes from ALDH2, Aldehyde dehydrogenase and Acetaldehyde.
William F. Bosron spends much of his time researching Biochemistry, Alcohol dehydrogenase, Ethanol, Enzyme and Isozyme. His Biochemistry study frequently draws connections between related disciplines such as Molecular biology. His Alcohol dehydrogenase research includes elements of Amino acid, NAD+ kinase, Coenzyme binding and Stereochemistry.
He focuses mostly in the field of Ethanol, narrowing it down to matters related to Internal medicine and, in some cases, Enzyme assay. His Enzyme research is multidisciplinary, incorporating perspectives in Alpha, Metal and Magnesium. In his work, Allele is strongly intertwined with Protein subunit, which is a subfield of Isozyme.
Biochemistry, Carboxylesterase, Isozyme, Formaldehyde dehydrogenase and Stereochemistry are his primary areas of study. His Biochemistry study frequently links to adjacent areas such as Hepatic stellate cell. His Carboxylesterase study is related to the wider topic of Enzyme.
His Enzyme research is multidisciplinary, incorporating elements of Metabolite, Prodrug and Hydrolysis. William F. Bosron combines subjects such as Molecular biology, Peptide, Alcohol dehydrogenase and Mass spectrometry with his study of Isozyme. He has included themes like Cofactor and Active site in his Formaldehyde dehydrogenase study.
William F. Bosron focuses on Biochemistry, Isozyme, Carboxylesterase, Enzyme and Gene expression. His research in the fields of Alcohol dehydrogenase, Peptide and Label-free quantification overlaps with other disciplines such as Selected reaction monitoring. His work carried out in the field of Isozyme brings together such families of science as Proteomics and Quantitative proteomics.
His Carboxylesterase research includes themes of Thioester, Metabolite, Prodrug, Hydrolysis and Stereochemistry. His Enzyme research is mostly focused on the topic Enzyme inhibitor. The various areas that William F. Bosron examines in his Gene expression study include Hydrolase, Molecular biology and Topoisomerase.
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Genetic polymorphism of human liver alcohol and aldehyde dehydrogenases, and their relationship to alcohol metabolism and alcoholism.
William F. Bosron;Ting‐Kai Li.
Genotypes for aldehyde dehydrogenase deficiency and alcohol sensitivity. The inactive ALDH2(2) allele is dominant.
D W Crabb;H J Edenberg;W F Bosron;T K Li.
Journal of Clinical Investigation (1989)
Characterization of CPT-11 Hydrolysis by Human Liver Carboxylesterase Isoforms hCE-1 and hCE-2
R. Humerickhouse;K. Lohrbach;Lin Li;W. F. Bosron.
Cancer Research (2000)
Current progress on esterases: from molecular structure to function.
Tetsuo Satoh;Palmer Taylor;William F. Bosron;Sonal P. Sanghani.
Drug Metabolism and Disposition (2002)
Research advances in ethanol metabolism.
V.A Ramchandani;W.F Bosron;T.K Li.
Pathologie Biologie (2001)
Human liver cocaine esterases: ethanol-mediated formation of ethylcocaine.
R A Dean;C D Christian;R H Sample;W F Bosron.
The FASEB Journal (1991)
Genetic factors in alcohol metabolism and alcoholism.
W. F. Bosron;T. Ehrig;T.-K. Li.
Seminars in Liver Disease (1993)
Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin.
Evgenia V. Pindel;Natalia Y. Kedishvili;Trent L. Abraham;Monica R. Brzezinski.
Journal of Biological Chemistry (1997)
Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification.
Yiling Xu;Lucinda G. Carr;William F. Bosron;Ting Kai Li.
Methylphenidate Is Stereoselectively Hydrolyzed by Human Carboxylesterase CES1A1
Zejin Sun;Daryl J. Murry;Sonal P. Sanghani;Wilhelmina I. Davis.
Journal of Pharmacology and Experimental Therapeutics (2004)
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