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1. Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH)
: the quintessential moonlighting protein in normal cell function and in human disease
by Sirover, Michael A
2017, ISBN 9780128098523
Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH): The Quintessential Moonlighting Protein in Normal Cell Function and in Human Disease examines the biochemical... 
Glycolysis | Aldehyde dehydrogenase
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2. Full Text Mapping Aldehyde Dehydrogenase 1A1 Activity using an [18F]Substrate‐Based Approach
by Pereira, Raul and Gendron, Thibault and Sanghera, Chandan and Greenwood, Hannah E and Newcombe, Joseph and McCormick, Patrick N and Sander, Kerstin and Topf, Maya and Årstad, Erik and Witney, Timothy H
Chemistry – A European Journal, ISSN 0947-6539, 02/2019, Volume 25, Issue 9, pp. 2345 - 2351
Aldehyde dehydrogenases (ALDHs) catalyze the oxidation of aldehydes to carboxylic acids. Elevated ALDH expression in human cancers is linked to metastases and... 
F]fluorination | cancer | radiolabeling | aldehyde dehydrogenase | radiochemistry | MECHANISM | MARKER | CHEMISTRY, MULTIDISCIPLINARY | CANCER STEM-CELLS | INACTIVATION | METABOLISM | SUBSTRATE | [F-18]fluorination | ALDH1A1 | Niacinamide | Pyridine | Liver | Gastrointestinal diseases | Colorectal cancer | Oxidoreductases | Metastasis | Aldehydes | Organic acids | NADPH | Pyridines | Tumor cells | Positron emission | Benzaldehyde | Fluorine isotopes | Radioactive tracers | Mapping | Selectivity | Urinary tract | Carboxylic acids | Aldehyde dehydrogenase | Substrates | Metastases | Organic chemistry | Lungs | Oxidation | Nicotinamide | Fluorination | Chemical synthesis | Positron emission tomography | Radioactivity | Full Paper | Full Papers | [18F]fluorination
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3. Full Text Activation of aldehyde dehydrogenase 2 (ALDH2) confers cardioprotection in protein kinase C epsilon (PKCɛ) knockout mice
by Budas, Grant R and Disatnik, Marie-Hélène and Chen, Che-Hong and Mochly-Rosen, Daria
Journal of Molecular and Cellular Cardiology, ISSN 0022-2828, 2009, Volume 48, Issue 4, pp. 757 - 764
Abstract Acute administration of ethanol can reduce cardiac ischemia/reperfusion injury. Previous studies demonstrated that the acute cytoprotective effect of... 
Cardiovascular | Aldehyde dehydrogenase 2 | Cardiac ischemia | Signaling | Protein kinase C | Preconditioning | CARDIAC & CARDIOVASCULAR SYSTEMS | LIPID-PEROXIDATION | CONTRACTILE DYSFUNCTION | REPERFUSION INJURY | CARDIAC MYOCYTES | ISCHEMIA | CELL BIOLOGY | SIGNALING PATHWAY | 4-HYDROXYNONENAL-INDUCED APOPTOSIS | ETHANOL | RAT-HEART | RABBIT HEARTS | Signal Transduction | Reperfusion Injury | Aldehyde Dehydrogenase, Mitochondrial | Heart - physiology | Humans | Protein Kinase C-epsilon - genetics | Mice, Knockout | Myocardial Ischemia - pathology | Gene Expression Regulation, Enzymologic | Animals | Ethanol - chemistry | Protein Kinase C - metabolism | Protein Kinase C-epsilon - metabolism | Mice | Enzyme Activation | Mutation | Aldehyde Dehydrogenase - metabolism | Aldehydes | Protein kinases | Index Medicus
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4. Full Text A new NAD+-dependent glyceraldehyde dehydrogenase obtained by rational design of l-lactaldehyde dehydrogenase from Escherichia coli
by Wu, Xing and Xu, Lin and Yan, Ming
Bioscience, Biotechnology, and Biochemistry, ISSN 0916-8451, 12/2016, Volume 80, Issue 12, pp. 2306 - 2310
NAD + -dependent glyceraldehyde dehydrogenases usually had lower activity in the nonphosphorylated Entner-Doudoroff (nED) pathway. In the present study, a new... 
rational design | site-directed mutagenesis | l-lactaldehyde dehydrogenase | specific activity | glyceraldehyde dehydrogenase | substrate specificity | ALDEHYDE DEHYDROGENASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FOOD SCIENCE & TECHNOLOGY | SATURATION MUTAGENESIS | NAD | SUBSTRATE-SPECIFICITY | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PURIFICATION | CHEMISTRY, APPLIED | REVEALS | Catalytic Domain | Temperature | Escherichia coli - enzymology | Mutagenesis, Site-Directed | Enzyme Stability | Models, Molecular | Aldehyde Oxidoreductases - genetics | Aldehyde Oxidoreductases - metabolism | Sequence Alignment | Aldehyde Oxidoreductases - chemistry | Escherichia coli - genetics | Mutation | Glyceraldehyde - metabolism | NAD - metabolism | Hydrogen-Ion Concentration | Index Medicus
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5. Full Text The ALDH21 gene found in lower plants and some vascular plants codes for a NADP+‐dependent succinic semialdehyde dehydrogenase
by Kopečná, Martina and Vigouroux, Armelle and Vilím, Jan and Končitíková, Radka and Briozzo, Pierre and Hájková, Eva and Jašková, Lenka and Schwartzenberg, Klaus and Šebela, Marek and Moréra, Solange and Kopečný, David
The Plant Journal, ISSN 0960-7412, 10/2017, Volume 92, Issue 2, pp. 229 - 243
Lower plant species including some green algae, non‐vascular plants (bryophytes) as well as the oldest vascular plants (lycopods) and ferns (monilophytes)... 
ALDH | γ‐aminobutyric acid | aldehyde dehydrogenase | succinic semialdehyde | Physcomitrella patens | X‐ray crystallography | site‐directed mutagenesis | structure–function | site-directed mutagenesis | X-ray crystallography | ALDH5 | γ-aminobutyric acid | ALDH21 | ARABIDOPSIS-GLYOXYLATE REDUCTASE | ESCHERICHIA-COLI | structure-function | SUBCELLULAR-LOCALIZATION | gamma-aminobutyric acid | FUNCTIONAL-CHARACTERIZATION | PLANT SCIENCES | STREPTOCOCCUS-PYOGENES | SUBSTRATE-SPECIFICITY | STRUCTURAL BASIS | GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE | ALDEHYDE-DEHYDROGENASE | BACTERIAL EXPRESSION | Bryophyta - genetics | gamma-Aminobutyric Acid - metabolism | Succinate-Semialdehyde Dehydrogenase - genetics | Substrate Specificity | Structure-Activity Relationship | Phylogeny | Genes, Plant - physiology | Ferns - genetics | Ferns - enzymology | Genes, Plant - genetics | Succinic Acid - metabolism | Protein Conformation | Succinate-Semialdehyde Dehydrogenase - metabolism | gamma-Aminobutyric Acid - analogs & derivatives | Bryophyta - enzymology | Genetic research | GABA | Enzymes | Plants | Genes | Phosphates | Salts | Dehydrogenases | Genomes | Dehydration | Aldehydes | Dehydrogenase | Cytosol | Aldehyde dehydrogenase | Mitochondria | γ-Aminobutyric acid | Arginine | Hydrogen bonds | Flowering | NADP | Flowers & plants | Catalysis | Crystal structure | Binding | Algae | Aquatic plants | Mosses | NAD | Ferns | Succinic semialdehyde dehydrogenase | Bryophytes | Index Medicus
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6. Full Text Variant Aldehyde Dehydrogenase 2 (ALDH22) in East Asians Interactively Exacerbates Tobacco Smoking Risk for Coronary Spasm　― Possible Role of Reactive Aldehydes
by Mizuno, Yuji and Hokimoto, Seiji and Harada, Eisaku and Kinoshita, Kenji and Yoshimura, Michihiro and Yasue, Hirofumi
Circulation Journal, ISSN 1346-9843, 2017, Volume 81, Issue 1, pp. 96 - 102
Background:Coronary spastic angina (CSA) is common among East Asians and tobacco smoking (TS) is an established risk factor for CSA. Aldehyde dehydrogenase 2... 
Aldehyde dehydrogenase 2 | Coronary spastic angina | Reactive aldehydes | East Asians | Tobacco smoking | CARDIAC & CARDIOVASCULAR SYSTEMS | ARTERY SPASM | CIGARETTE SMOKERS | HEART-DISEASE | POLYMORPHISMS | ALCOHOL | GENE | ANGINA | INFLAMMATION | CARDIOVASCULAR-DISEASE | JAPANESE | Smoking - adverse effects | Coronary Vasospasm - blood | Humans | Middle Aged | Aldehyde Dehydrogenase, Mitochondrial - metabolism | Male | Angina Pectoris - etiology | Aldehydes - blood | Coronary Vasospasm - genetics | Female | Uric Acid - blood | Coronary Vasospasm - etiology | Smoking - blood | Japan | Genotype | Smoking - genetics | Aldehyde Dehydrogenase, Mitochondrial - genetics | Coronary Vasospasm - enzymology | Angina Pectoris - blood | Asian Continental Ancestry Group | Angina Pectoris - genetics | Sex Factors | Angina Pectoris - enzymology | Cholesterol, HDL - blood | Aged | Index Medicus
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7. Full Text Possible Interaction of Alcohol Dehydrogenase and Aldehyde Dehydrogenase Genes With the Dopamine D2 Receptor Gene in Anxiety‐Depressive Alcohol Dependence
by Huang, San‐Yuan and Lin, Wei‐Wen and Ko, Huei‐Chen and Lee, Jia‐Fu and Wang, Tso‐Jen and Chou, Yuan‐Hwa and Yin, Shih‐Jiun and Lu, Ru‐Band
Alcoholism: Clinical and Experimental Research, ISSN 0145-6008, 03/2004, Volume 28, Issue 3, pp. 374 - 384
A bstract : Background: The role of the dopamine D2 receptor ( DRD2 ) gene in the development of alcohol abuse or dependence is controversial. The controversy... 
Anxiety‐Depression | Alcohol Dependence | ALDH2 | DRD2 | ADH1B | Anxiety-Depression | AFFECTIVE-DISORDERS | 4 ABORIGINAL GROUPS | SUBSTANCE ABUSE | BINDING CHARACTERISTICS | DIAGNOSTIC INTERVIEW SCHEDULE | anxiety-depression | VENTRAL TEGMENTAL AREA | NO ASSOCIATION | A1 ALLELE | LINKAGE DISEQUILIBRIUM | alcohol dependence | SUBSTANCE DEPENDENCE | DRD2 LOCUS | Humans | Middle Aged | Asian Continental Ancestry Group - genetics | Aldehyde Dehydrogenase - genetics | Genotype | Male | Depression - genetics | Anxiety - enzymology | Depression - enzymology | Receptors, Dopamine D2 - genetics | Haplotypes - genetics | Anxiety - genetics | Alcoholism - enzymology | Alcohol Dehydrogenase - genetics | Anxiety - complications | Adult | Alcoholism - genetics | Depression - complications | Female | Alcoholism - complications | Index Medicus
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8. Full Text Impact of alcohol dehydrogenase‐aldehyde dehydrogenase polymorphism on clinical outcome in patients with hypopharyngeal cancer
by Avinçsal, Mehmet Ozgur and Shinomiya, Hirotaka and Teshima, Masanori and Kubo, Mie and Otsuki, Naoki and Kyota, Naomi and Sasaki, Ryohei and Zen, Yoh and Nibu, Ken‐ichi
Head & Neck, ISSN 1043-3074, 04/2018, Volume 40, Issue 4, pp. 770 - 777
BackgroundThe purpose of this research was to investigate the association between alcohol dehydrogenase 1B (ADH1B) and aldehyde dehydrogenase 2 (ALDH2)... 
hypopharyngeal cancers | alcohol dehydrogenase‐aldehyde dehydrogenase (ADH‐ALDH) polymorphism | head and neck cancers | prognosis | alcohol dehydrogenase-aldehyde dehydrogenase (ADH-ALDH) polymorphism | SURGERY | HEAD | DRINKING | RISK | SMOKING | ESOPHAGEAL | NECK-CANCER | LESIONS | OTORHINOLARYNGOLOGY | SQUAMOUS-CELL CARCINOMA | JAPANESE | Hypopharyngeal Neoplasms - surgery | Hypopharyngeal Neoplasms - genetics | Prognosis | Carcinoma, Squamous Cell - genetics | Carcinoma, Squamous Cell - pathology | Humans | Middle Aged | Gene Expression Regulation, Neoplastic | Carcinoma, Squamous Cell - surgery | Male | Hypopharyngeal Neoplasms - mortality | Carcinoma, Squamous Cell - mortality | Adult | Retrospective Studies | Risk Assessment | Japan | Kaplan-Meier Estimate | Proportional Hazards Models | Aldehyde Dehydrogenase - genetics | Alcohol Drinking - adverse effects | Disease-Free Survival | Hypopharyngeal Neoplasms - pathology | Alcohol Dehydrogenase - genetics | Alleles | Survival Analysis | Aged | Polymorphism, Single Nucleotide | Cohort Studies | Cancer patients | Care and treatment | Squamous cell carcinoma | Patient outcomes | Genetic aspects | Single nucleotide polymorphisms | Aldehydes | Statistical analysis | Dehydrogenases | Cell survival | Alcohol | Single-nucleotide polymorphism | Alcohol dehydrogenase | Multivariate analysis | Gene polymorphism | Aldehyde dehydrogenase | Risk factors
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9. Full Text Complete oxidation of methanol in biobattery devices using a hydrogel created from three modified dehydrogenases
by Kim, Yang Hee and Campbell, Elliot and Yu, Jiang and Minteer, Shelley D and Banta, Scott
Angewandte Chemie - International Edition, ISSN 1433-7851, 01/2013, Volume 52, Issue 5, pp. 1437 - 1440
  Enzyme catalysis: Three dehydrogenases have been engineered to self-assemble into a hydrogel that supports a synthetic metabolic network. The new catalytic... 
biofuel cells | self-assembly | enzyme catalysis | protein engineering | electrochemistry | PROTEIN | SPECIFICITY | BUILDING-BLOCKS | ALDEHYDE DEHYDROGENASES | CHEMISTRY, MULTIDISCIPLINARY | ENZYMES | BIOMATERIALS | AGGREGATION | INTEIN | Alcohol Dehydrogenase - metabolism | Carbon Dioxide - chemistry | Biocatalysis | Carbon Dioxide - metabolism | Hydrogel, Polyethylene Glycol Dimethacrylate - chemistry | Oxidation-Reduction | Oxidoreductases - metabolism | Oxidoreductases - genetics | Bioelectric Energy Sources | Aldehyde Dehydrogenase - genetics | Formate Dehydrogenases - metabolism | Aldehyde Dehydrogenase - chemistry | Formate Dehydrogenases - genetics | Oxidoreductases - chemistry | Methanol - metabolism | Formate Dehydrogenases - chemistry | Alcohol Dehydrogenase - genetics | Protein Engineering | Kinetics | Methanol - chemistry | Aldehyde Dehydrogenase - metabolism | Alcohol Dehydrogenase - chemistry | Electrochemical reactions | Biomass energy | Electrochemistry | Oxidoreductases | Chemical properties | Catalysis | Cells | Methanol | Index Medicus | Surgical implants | Biomedical materials | Hydrogels | Anodizing | Methyl alcohol | Carbon dioxide | Oxidation
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10. Full Text Strong Association of the Alcohol Dehydrogenase 1B Gene ( ADH1B ) with Alcohol Dependence and Alcohol-Induced Medical Diseases
by Li, Dawei and Zhao, Hongyu and Gelernter, Joel
Biological Psychiatry, ISSN 0006-3223, 2011, Volume 70, Issue 6, pp. 504 - 512
Background The alcohol dehydrogenase 1B gene ( ADH1B ) is hypothesized to affect predisposition to alcohol dependence (AD) and abuse. A variant of the ADH1B... 
Psychiatry | meta-analysis | ethanol metabolism | drinking | Addiction | liver disease | METABOLIZING ENZYME GENES | ALDEHYDE DEHYDROGENASE | PSYCHIATRY | LIVER-DISEASE | FRAGMENT-LENGTH-POLYMORPHISM | NEUROSCIENCES | ALDH2 GENE | ADH2-ASTERISK-2 ALLELE | CHRONIC-PANCREATITIS | OPIOID-RECEPTOR GENE | MEXICAN-AMERICAN MEN | GENOME-WIDE ASSOCIATION | Genetic Predisposition to Disease - genetics | Ethnic Groups - genetics | Genetic Association Studies - statistics & numerical data | Humans | Alcohol Dehydrogenase - genetics | Alcoholism - genetics | Alcoholism - complications | Alcohol-Induced Disorders - genetics | Alcohol-Induced Disorders - complications | Alcoholic beverages | Alcoholism | Index Medicus | Drinking | Liver Disease | Meta-analysis | Ethanol Metabolism
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11. Full Text An Alcohol Dehydrogenase from the Short‐Chain Dehydrogenase/Reductase Family of Enzymes for the Lactonization of Hexane‐1,6‐diol
by Dithugoe, Choaro D and van Marwijk, Jacqueline and Smit, Martha S and Opperman, Diederik J
ChemBioChem, ISSN 1439-4227, 01/2019, Volume 20, Issue 1, pp. 96 - 102
Biocatalytic production of lactones, and in particular ϵ‐caprolactone (CL), have gained increasing interest as a greener route to polymer building blocks,... 
caprolactone | lactones | diols | alcohol dehydrogenases | short-chain dehydrogenases/reductases | ORGANIC-SYNTHESIS | CHEMISTRY, MEDICINAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | BAEYER-VILLIGER MONOOXYGENASES | YEAST | ENZYMATIC CONVERGENT CASCADE | EPSILON-CAPROLACTONE SYNTHESIS | RING-OPENING POLYMERIZATION | CATALYZED OXIDATIONS | CHIRAL LACTONES | EXPRESSION | Enzymes | Dehydrogenases | Liver | Alcohol | Selectivity | Alcohol dehydrogenase | Aldehydes | Dehydrogenase | Aliphatic compounds | Substrates | NADH oxidase | Lactones | Intermediates | Regeneration | NADH | Acids | Dehydrogenation | Nicotinamide adenine dinucleotide | Oxidation | Histocompatibility antigen HLA | Adipic acid | Buffers | Diols | Reductase
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12. Full Text Selective inactivation of α-ketoglutarate dehydrogenase and pyruvate dehydrogenase: Reaction of lipoic acid with 4-hydroxy-2-nonenal
by Humphries, Kenneth M and Szweda, Luke I
Biochemistry, ISSN 0006-2960, 11/1998, Volume 37, Issue 45, pp. 15835 - 15841
Previous research has established that 4-hydroxy-2-nonenal (HNE), a highly toxic product of lipid peroxidation, is a potent inhibitor of mitochondrial... 
OXIDATIVE STRESS | LIPID-PEROXIDATION | ALZHEIMERS-DISEASE | MITOCHONDRIAL NADH | BIOCHEMISTRY & MOLECULAR BIOLOGY | ISCHEMIA | MULTIENZYME COMPLEXES | RAT-HEART | RADICALS | RABBIT HEARTS | PARKINSONS-DISEASE | Pyruvate Dehydrogenase Complex - metabolism | Pyruvate Dehydrogenase Complex - isolation & purification | Mitochondria, Heart - enzymology | Rats | Thioctic Acid - immunology | Ketoglutarate Dehydrogenase Complex - metabolism | Aldehydes - metabolism | Enzyme Activation - drug effects | Rats, Sprague-Dawley | Blotting, Western | Ketoglutarate Dehydrogenase Complex - antagonists & inhibitors | Thioctic Acid - metabolism | Pyruvate Dehydrogenase Complex - antagonists & inhibitors | Animals | Immune Sera - metabolism | Aldehydes - pharmacology | Binding Sites, Antibody | Ketoglutarate Dehydrogenase Complex - isolation & purification | Sulfhydryl Reagents - metabolism | Proteins | Mitochondria | Research | Respiration | Index Medicus
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