Über den Autor
Henry Weiner is a professor of Biochemistry at Purdue University. Dr Weiner obtained his Ph.D. from Purdue University in 1963. His area of study currently includes protein trafficking and the enzymology of aldehyde dehydrogenasess.
Aldehyde Dehydrogenases-The 1992 Perspective.- Metabolic Role of Aldehyde Dehydrogenase.- Effects of Aldehyde Products of Lipid Peroxidation on the Activity of Aldehyde Metabolizing Enzymes in Hepatomas.- Metabolic Interactions of 4-Hydroxynonenal, Acetaldehyde and Glutathione in Isolated Liver Mitochondria.- Biological Role of Human Cytosolic Aldehyde Dehydrogenase 1: Hormonal Response, Retinal Oxidation and Implication in Testicular Feminization.- Human Cytosolic Aldehyde Dehydrogenase in Androgen Insensitivity Syndrome.- The Use of Immortalized Mouse L1210/OAP Cells Established in Culture to Study the Major Class 1 Aldehyde Dehydrogenase-Catalyzed Oxidation of Aldehydes in Intact Cells.- Enhanced Transcription of the Cytosolic ALDH Gene in Cyclophosphamide Resistant Human Carcinoma Cells.- Attempts to Increase the Expression of Rat Liver Mitochondrial Aldehyde Dehydrogenase in E. coli by Altering the mRNA.- Preliminary Characterization of the Rat Class 3 Aldehyde Dehydrogenase Gene.- Human High-Km Aldehyde Dehydrogenase (ALDH3): Molecular, Kinetic, and Structural Features.- Overexpression or Polycyclic Aromatic Hydrocarbon-Mediated Induction of an Apparently Novel Class 3 Aldehyde Dehydrogenase in Human Breast Adenocarcinoma Cells and Its Relationship to Oxazaphosphorine-Specific Acquired Resistance.- Tumor-Associated Aldehyde Dehydrogenase (ALDH3): Expression in Different Human Tumor Cell Lines with and without Treatment with 3-Methylcholanthrene.- Sexual Differentiation in the Induction of the Class 3 Aldehyde Dehydrogenase.- Mouse Class 3 Aldehyde Dehydrogenases: Positive and Negative Regulation of Gene Expression.- Human Stomach Aldehyde Dehydrogenase, ALDH3.- Bovine Corneal Aldehyde Dehydrogenases: Evidence for Multiple Gene Products (ALDH3 and ALDHX).- Carbonyl-Metabolizing Enzymes and Their Relatives Recruited as Structural Proteins in the Eye Lens.- Members of the ALDH Gene Family are Lens and Corneal Crystalline.- Retinoic Acid Synthesis in the Developing Retina.- Human Liver High Km Aldehyde Dehydrogenase (ALDH4): Properties and Structural Relationship to the Yeast Glutamic ?-Semialdhyde Dehydrogenase.- Effect of Some Compounds Related to Disulfiram on Mitochondrial Aldehyde Dehydrogenase in Vitro and in Vivo.- Photoaffinity Labeling of Aldehyde Dehydrogenase from Horse Liver by P1-N6-(4-Azidophenylethyl) Adenosine-P2[4-(3-Azidopyridinio)Butyl] Diphosphate.- Aldehyde Dehydrogenase: Aldehyde Dehydrogenation and Ester Hydrolysis.- Is the Single Site Binding Model for Aldehyde Dehydrogenase an Oversimplification? The One-Site, Two-Site Debate Revisited.- Crystallization and Preliminary X-Ray Analysis of Bovine Mitochondrial Aldehyde Dehydrogenase and Human Glutathione-Dependent Formaldehyde Dehydrogenase.- Aldo-Keto Reductases: An Overview.- Location of an Essential Arginne Residue in the Primary Structure of Pig Aldose Reductase.- Cys298 Is Responsible for Reversible Thiol-Induced Variation in Aldose Reductase Activity.- Substrate Specificity of Reduced and Oxidized Forms of Human Aldose Reductase.- Kinetic Alteration of Human Aldose Reductase by Mutagenesis of Cysteine Residues.- Inhibition of Aldose Reductase by (2, 6-Dimethylphenylsulphonyl) Nitromethane: Possible Implications for the Nature of an Inhibitor Binding Site and a Cause of Biphasic Kinetics.- Sepiapterin Reductase and ALR2 ("Aldose Reductase") from Bovine Brain.- Polymorphisms of the Aldose Reductase Locus (ALR2) and Suseptibility to Diabetic Microvascular Complications.- Polycyclic Aromatic Hydrocarbons and Phenolic Antioxidants do not Significantly Induce Carbonyl Reductase in Human Cell Lines.- The Purification and Properties of a Novel Carbonyl Reducing Enzyme from Mouse Liver Microsomes.- Properties and Stereoselectivity of Carbonyl Reductases Involved in the Ketone Reduction of Warfarin and Analogues.- Activation of Pulmonary Carbonyl Reductase by Aromatic Amines and Pyridine Ring-Containing Compounds.- Unique Dihydrodiol Specific Dehydrogenase of Bovine Liver: Inhibition Studies and Comparison with Aldo/Keto Reductase.- Carbonyl Reduction by 3?-HSD from Comamonas testosteroni- New Properties and Its Relationship to the Scad Family.- Substrate Specificity of Alchohol Dehydrogenases.- The Influence of pH on the Substrate Specificity and Stereoselectivity of Alcohol Dehydrogenase from Horse Liver.- The Catalytic Specificity of Liver Alcohol Dehydrogenase: Vitamin A Alcohol and Vitamin A Aldehyde Activities.- A Synthetic Approach to Analysis of the Structural Zinc Site of Alcohol Dehydrogenase.- Pyrophosphate Binding Site.- Site-Directed Mutagenesis of Mammalian Alcohol and Sorbitol Dehydrogenases Map Functional Differences within the Enzyme Family.- Horse Liver Alcohol Dehydrogenase-S-Isozyme: Confirmation of the Primary Structure by Protein Sequencing and Ion Spray Mass Spectrometry.- Mixed Substrate Experiments with Class III (?) Alcohol Dehydrogenases from Human and Pig Liver and Stomach.- Glutathione-Dependent Formaldehyde Dehydrogenase/ClassIII Alcohol Dehydrogenase: Further Characterization of the Rat Liver Enzyme.- Class IV Alcohol Dehydrogenase: Structure and Function.- The Oxidation of Aldehydes by Horse Liver Alcohol Dehydrogenase.- Effect of Glycation Upon Activity of Liver Alcohol Dehydrogenase.- Kinetically Specific Spin-Label Substrates of Liver Alcohol Dehydrogenase and of Liver Aldehyde Dehydrogenase.- Fluorescence Studies of Ternary Complexes of Liver Alcohol Dehydrogenase.- Evolutionary Relationships of Branched Chain and Non-Specific Alcohol and Aldehyde Dehydrogenases.- Enzyme and Isozyme Developments within the Medium-Chain Alcohol Dehydrogenase Family.- Tissue Distribution of Alcohol and Sorbitol Dehydrogenase mRNAs.- The Role of Alcohol and Aldehyde Dehydrogenases in Alcohol-Related Diseases: Clinical Studies of Molecular Markers.- Regulation of the Human Alcohol Dehydrogenase Genes ADH1, ADH2, and ADH3: Differences in cis-Acting Sequences at CTF/NF-1 Sites.- DNA Elements Mediating Retinoid and Thyroid Hormone Regulation of Alcohol Dehydrogenase Gene Expression.- Modulation of Hepatic and Renal Alcohol Dehydrogenase Activity and mRNA by Steroid Hormones in Vivo.- Alcohol- and Aldehyde-Dehydrogenase: Modulation by Biogenic Amine Metabolites, Neuropeptides and Psychoactive Agents.- Microbial Alcohol, Aldehyde, and Formate Ester Oxidoreductases.- Carbonyl Metabolising Enzymes in Alkane-Grown Microorganisms.
The Sixth International Workshop on the Enzymology and Molecular Biology of Carbonyl Metabolism was held outside of Dublin, Ireland at the end of June, 1992. Prof. Keith Tipton, Chairman of the Biochemistry Department at Trinity College, kindly agreed to host the meeting. On behalf of all of us who attended I wish to extend our sincere thanks to the whole Tipton family for making us feel so welcome in Ireland. It has been a decade since the frrst workshop was held in Bern, Switzerland. The scope of the meetings reflected somewhat the changes that have occurred in biochemistry during the past decade. At the first meeting primarily enzymes and their properties were discussed. At this last meeting many of the talks centered on gene regulation as well as more traditional aspects of enzymology and metabolism. During the past decade site directed mutagenesis to probe for the active site of an enzyme has become part of traditional enzymology; this was virtually unheard of at our frrst meeting. Many of the presenters now used this tool to study some aspect of structure and function of one of the three carbonyl metabolizing enzymes.
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