Log in

Relevant bibliographies by topics / Aldehyde Dehydrogenase Inhibition

Contents

Journal articles
Dissertations / Theses
Book chapters
Conference papers

Academic literature on the topic 'Aldehyde Dehydrogenase Inhibition'

Author: Grafiati

Published: 2 June 2025

Last updated: 31 July 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Aldehyde Dehydrogenase Inhibition.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Aldehyde Dehydrogenase Inhibition"

1

Averill-Bates, Diana A., Enzo Agostinelli, Ewa Przybytkowski, and Bruno Mondovi. "Aldehyde dehydrogenase and cytotoxicity of purified bovine serum amine oxidase and spermine in Chinese hamster ovary cells." Biochemistry and Cell Biology 72, no. 1-2 (1994): 36–42. http://dx.doi.org/10.1139/o94-006.

Full text

Abstract:

Bovine serum amine oxidase (EC 1.4.3.6) catalyses the oxidative deamination of polyamines giving rise to the corresponding aldehydes, ammonia, and hydrogen peroxide. It has been suggested that the dialdehyde produced during the oxidation of spermine subsequently undergoes spontaneous β-elimination to form acrolein. Oxidation of the aldehydes by aldehyde dehydrogenase (EC 1.2.1.5) thus eliminates these reactive species and prevents the formation of acrolein. This work studies the role of each of the oxidation products of spermine in cytotoxicity induced by purified bovine serum amine oxidase. T

APA, Harvard, Vancouver, ISO, and other styles

2

Chen, Chao, Jeong Chan Joo, Greg Brown, et al. "Structure-Based Mutational Studies of Substrate Inhibition of Betaine Aldehyde Dehydrogenase BetB from Staphylococcus aureus." Applied and Environmental Microbiology 80, no. 13 (2014): 3992–4002. http://dx.doi.org/10.1128/aem.00215-14.

Full text

Abstract:

ABSTRACTInhibition of enzyme activity by high concentrations of substrate and/or cofactor is a general phenomenon demonstrated in many enzymes, including aldehyde dehydrogenases. Here we show that the uncharacterized protein BetB (SA2613) fromStaphylococcus aureusis a highly specific betaine aldehyde dehydrogenase, which exhibits substrate inhibition at concentrations of betaine aldehyde as low as 0.15 mM. In contrast, the aldehyde dehydrogenase YdcW fromEscherichia coli, which is also active against betaine aldehyde, shows no inhibition by this substrate. Using the crystal structures of BetB

APA, Harvard, Vancouver, ISO, and other styles

3

MODIG, Tobias, Gunnar LIDÉN, and Mohammad J. TAHERZADEH. "Inhibition effects of furfural on alcohol dehydrogenase, aldehyde dehydrogenase and pyruvate dehydrogenase." Biochemical Journal 363, no. 3 (2002): 769–76. http://dx.doi.org/10.1042/bj3630769.

Full text

Abstract:

The kinetics of furfural inhibition of the enzymes alcohol dehydrogenase (ADH; EC 1.1.1.1), aldehyde dehydrogenase (AlDH; EC 1.2.1.5) and the pyruvate dehydrogenase (PDH) complex were studied in vitro. At a concentration of less than 2mM furfural was found to decrease the activity of both PDH and AlDH by more than 90%, whereas the ADH activity decreased by less than 20% at the same concentration. Furfural inhibition of ADH and AlDH activities could be described well by a competitive inhibition model, whereas the inhibition of PDH was best described as non-competitive. The estimated Km value of

APA, Harvard, Vancouver, ISO, and other styles

4

Karamanakos, Petros N., Periklis Pappas, Vassiliki A. Boumba, et al. "Pharmaceutical Agents Known to Produce Disulfiram-Like Reaction: Effects on Hepatic Ethanol Metabolism and Brain Monoamines." International Journal of Toxicology 26, no. 5 (2007): 423–32. http://dx.doi.org/10.1080/10915810701583010.

Full text

Abstract:

Several pharmaceutical agents produce ethanol intolerance, which is often depicted as disulfiram-like reaction. As in the case with disulfiram, the underlying mechanism is believed to be the accumulation of acetaldehyde in the blood, due to inhibition of the hepatic aldehyde dehydrogenases. In the present study, chloramphenicol, furazolidone, metronidazole, and quinacrine, which are reported to produce a disulfiram-like reaction, as well as disulfiram, were administered to Wistar rats and the hepatic activities of alcohol and aldehyde dehydrogenases (1A1 and 2) were determined. The expression

APA, Harvard, Vancouver, ISO, and other styles

5

Panoutsopoulos, Georgios I., and Christine Beedham. "Enzymatic oxidation of phthalazine with guinea pig liver aldehyde oxidase and liver slices: inhibition by isovanillin." Acta Biochimica Polonica 51, no. 4 (2004): 943–51. https://doi.org/10.18388/abp.2004_3527.

Full text

Abstract:

The enzymes aldehyde oxidase and xanthine oxidase catalyze the oxidation of a wide range of N-heterocycles and aldehydes. These enzymes are widely known for their role in the metabolism of N-heterocyclic xenobiotics where they provide a protective barrier by aiding in the detoxification of ingested nitrogen-containing heterocycles. Isovanillin has been shown to inhibit the metabolism of aromatic aldehydes by aldehyde oxidase, but its inhibition towards the heterocyclic compounds has not been studied. The present investigation examines the oxidation of phthalazine in the absence and in the pres

APA, Harvard, Vancouver, ISO, and other styles

6

Dicker, E., and A. I. Cederbaum. "Inhibition of the low-Km mitochondrial aldehyde dehydrogenase by diethyl maleate and phorone in vivo and in vitro Implications for formaldehyde metabolism." Biochemical Journal 240, no. 3 (1986): 821–27. http://dx.doi.org/10.1042/bj2400821.

Full text

Abstract:

Formaldehyde can be oxidized primarily by two different enzymes, the low-Km mitochondrial aldehyde dehydrogenase and the cytosolic GSH-dependent formaldehyde dehydrogenase. Experiments were carried out to evaluate the effects of diethyl maleate or phorone, agents that deplete GSH from the liver, on the oxidation of formaldehyde. The addition of diethyl maleate or phorone to intact mitochondria or to disrupted mitochondrial fractions produced inhibition of formaldehyde oxidation. The kinetics of inhibition of the low-Km mitochondrial aldehyde dehydrogenase were mixed. Mitochondria isolated from

APA, Harvard, Vancouver, ISO, and other styles

7

Paulová, Hana, Jan Kovář, Jiří Plocek, and Jiří Slavík. "Inhibition of aldehyde reductase I by some isoquinoline alkaloids." Collection of Czechoslovak Chemical Communications 52, no. 9 (1987): 2338–46. http://dx.doi.org/10.1135/cccc19872338.

Full text

Abstract:

Aldehyde reductase I has been found to be inhibited by certain isoquinoline alkaloids (protoberberines, protopines, benzylisoquinolines, benzyltetrahydroisoquinolines, phthalideisoquinolines, pavinanes) and narceine imide. The sensitivity of this enzyme to the compounds tested was compared with that of alcohol dehydrogenase and/or aldehyde reductase II to them; alcohol dehydrogenase proved more selective in binding the alkaloids. The kinetics of the inhibitory action of berberine and other results suggest that the binding site of aldehyde reductase I for alkaloids is relatively large, has a hy

APA, Harvard, Vancouver, ISO, and other styles

8

Yusuf, Rushdia Zareen, Borja Saez, Azeem Sharda, et al. "Aldehyde dehydrogenase 3a2 protects AML cells from oxidative death and the synthetic lethality of ferroptosis inducers." Blood 136, no. 11 (2020): 1303–16. http://dx.doi.org/10.1182/blood.2019001808.

Full text

Abstract:

Abstract Metabolic alterations in cancer represent convergent effects of oncogenic mutations. We hypothesized that a metabolism-restricted genetic screen, comparing normal primary mouse hematopoietic cells and their malignant counterparts in an ex vivo system mimicking the bone marrow microenvironment, would define distinctive vulnerabilities in acute myeloid leukemia (AML). Leukemic cells, but not their normal myeloid counterparts, depended on the aldehyde dehydrogenase 3a2 (Aldh3a2) enzyme that oxidizes long-chain aliphatic aldehydes to prevent cellular oxidative damage. Aldehydes are by-pro

APA, Harvard, Vancouver, ISO, and other styles

9

Keller, Markus A., Katrin Watschinger, Georg Golderer, Gabriele Werner-Felmayer, and Ernst R. Werner. "Fatty aldehyde dehydrogenase, the enzyme downstream of tetrahydrobiopterin-dependent alkylglycerol monooxygenase." Pteridines 24, no. 1 (2013): 105–9. http://dx.doi.org/10.1515/pterid-2013-0004.

Full text

Abstract:

AbstractThe tetrahydrobiopterin-dependent degradation of ether lipids by alkylglycerol monooxygenase (AGMO) produces fatty aldehydes, which are toxic to cells. Therefore, it is of great physiological importance that these harmful compounds are converted into their corresponding, less toxic fatty acids by fatty aldehyde dehydrogenase (FALDH). Dysfunction of this enzyme causes Sjögren-Larsson syndrome. This severe inherited disorder is accompanied by symptoms such as ichthyosis, mental retardation and spasticity. Surprisingly, fatty alcohols and not fatty aldehydes were found to accumulate in fi

APA, Harvard, Vancouver, ISO, and other styles

10

VELASCO-GARCÍA, Roberto, Lilian GONZÁLEZ-SEGURA, and Rosario A. MUÑOZ-CLARES. "Steady-state kinetic mechanism of the NADP+- and NAD+-dependent reactions catalysed by betaine aldehyde dehydrogenase from Pseudomonas aeruginosa." Biochemical Journal 352, no. 3 (2000): 675–83. http://dx.doi.org/10.1042/bj3520675.

Full text

Abstract:

Betaine aldehyde dehydrogenase (BADH) catalyses the irreversible oxidation of betaine aldehyde to glycine betaine with the concomitant reduction of NAD(P)+ to NADP(H). In Pseudomonas aeruginosa this reaction is a compulsory step in the assimilation of carbon and nitrogen when bacteria are growing in choline or choline precursors. The kinetic mechanisms of the NAD+- and NADP+-dependent reactions were examined by steady-state kinetic methods and by dinucleotide binding experiments. The double-reciprocal patterns obtained for initial velocity with NAD(P)+ and for product and dead-end inhibition e

APA, Harvard, Vancouver, ISO, and other styles

More sources

Dissertations / Theses on the topic "Aldehyde Dehydrogenase Inhibition"

1

Koch, Maximilian [Verfasser], Stephan A. [Akademischer Betreuer] Sieber, and Wolfgang [Akademischer Betreuer] Eisenreich. "Functional analysis of selective aldehyde dehydrogenase 1A1 inhibition by cytotoxic duocarmycin analogs and LC-MS-based metabolomic profiling of polar metabolites in bacteria / Maximilian Koch. Betreuer: Stephan A. Sieber. Gutachter: Wolfgang Eisenreich ; Stephan A. Sieber." München : Universitätsbibliothek der TU München, 2015. http://d-nb.info/1079324054/34.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Ibrahim, Ali I. M. "Design, Synthesis and Biological Evaluation of Chemical Probes Incorporating Aldehyde Dehydrogenase (ALDH) Recognition Motifs and Fluorescent Properties. An Investigation Towards the Development of ALDH-Affinic Fluorophores for Hypoxia Cell Tracking." Thesis, University of Bradford, 2017. http://hdl.handle.net/10454/18179.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Venton, Geoffroy. "Approches thérapeutiques métaboliques et immunologiques des leucémies aiguës myéloïdes." Thesis, Aix-Marseille, 2016. http://www.theses.fr/2016AIXM5031/document.

Full text

Abstract:

Le Dimethyl Ampal Thiolester (DIMATE) est un inhibiteur des aldéhydes déshydrogénases (ALDHs) de type 1 et 3. L’intérêt croissant au cours de ces dernières années pour ces enzymes intra cytoplasmiques que sont les ALDHs, s’explique par leurs utilisations comme marqueurs pour distinguer les cellules souches, saines ou cancéreuses, au sein de différents tissus, comme le tissu hématopoïétique. Le traitement des Leucémies Aiguës Myéloïdes demeure une problématique clinique majeure. En effet, malgré un taux de rémission complète moyen d’environ 70% avec les traitements conventionnels, la survie moy

APA, Harvard, Vancouver, ISO, and other styles

4

Fitzmaurice, Arthur Gerald III. "The Role of Pesticide-Induced Aldehyde Dehydrogenase Inhibition in the Pathogenesis of Parkinson’s Disease." Thesis, 2012. https://thesis.library.caltech.edu/7134/2/fitzmauricePhDthesis.pdf.

Full text

Abstract:

<p>Parkinson’s disease (PD) is a neurodegenerative disorder particularly characterized by the loss of dopaminergic neurons in the substantia nigra pars compacta. Its etiology is unknown but likely includes both genetic and environmental factors. Since pesticide use has been associated with PD occurrence, we conducted a screen to identify pesticides that impair the ubiquitin-proteasome system (UPS), a degradative process implicated in PD pathogenesis. Benomyl was identified as a UPS inhibitor in this screen and became the focus of this dissertation.</p> <p>In an epidemiologic study, we used

APA, Harvard, Vancouver, ISO, and other styles

5

Lee, Yung-Pin, and 李永彬. "Inhibition of Human Alcohol Dehydrogenases and Aldehyde Dehydrogenases by Cimetidine and Acetaminophen: Quantitative Simulations for the Inhibition of Ethanol Metabolism by Mechanism-based Kinetic Equations." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/m6v986.

Full text

Abstract:

博士<br>國立中山大學<br>生物科學系研究所<br>102<br>Human alcohol dehydrogenase (ADH) family and aldehyde dehydrogenase (ALDH) isozymes are two principal enzyme systems responsible for alcohol metabolism in humans. Cimetidine, an H2-receptor antagonist for peptic ulcers treatment, and acetaminophen for antipyretic and analgesic medications, are two widely used over-the-counter drugs. It has been reported that cimetidine or acetaminophen can elevate blood ethanol level after ingestion of alcohol and might affect bioavailability of ethanol by inhibiting gastric ADH. The purpose of this dissertation is to (1) cha

APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Aldehyde Dehydrogenase Inhibition"

1

Gessner, Peter K., and Teresa Gessner. "Inhibition of aldehyde dehydrogenase." In Disulfiram and its Metabolite, Diethyldithiocarbamate. Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2328-0_9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Conyers, R. A. J., R. Bais, and A. M. Rofe. "Cimetidine Inhibition of Hepatic Aldehyde Dehydrogenase and Oxalate Production." In Urolithiasis. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4899-0873-5_153.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Nagasawa, H. T., C. H. Kwon, J. A. Elberling, et al. "Rationale for Alcoholism Treatment Based on Inhibition of Aldehyde Dehydrogenase." In Novel Pharmacological Interventions for Alcoholism. Springer New York, 1992. http://dx.doi.org/10.1007/978-1-4612-2878-3_21.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Devaraj, Varadahalli R., Lakshmaiah Sreerama, Melinda J. C. Lee, Herbert T. Nagasawa, and Norman E. Sladek. "Yeast Aldehyde Dehydrogenase Sensitivity to Inhibition by Chlorpropamide Analogues as an Indicator of Human Aldehyde Dehydrogenase Sensitivity to These Agents." In Advances in Experimental Medicine and Biology. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5871-2_18.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Lipsky, James J., Dennis C. Mays, Jennifer L. Holt, et al. "Inhibition of and Interaction with Human Recombinant Mitochondrial Aldehyde Dehydrogenase by Methyl Diethylthiocarbamate Sulfoxide." In Advances in Experimental Medicine and Biology. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5871-2_24.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Russo, James E. "Inhibition of Mouse and Human Class 1 Aldehyde Dehydrogenase by 4-(N,N-Dialkylamino)Benzaldehyde Compounds." In Advances in Experimental Medicine and Biology. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5871-2_25.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Mays, Dennis C., Andy J. Tomlinson, Kenneth L. Johnson, Jennifer Lam, James J. Lipsky, and Stephen Naylor. "Inhibition of Human Mitochondrial Aldehyde Dehydrogenase by Metabolites of Disulfiram and Structural Characterization of the Enzyme Adduct by HPLC-Tandem Mass Spectrometry." In Advances in Experimental Medicine and Biology. Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4735-8_8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Rekha, Ganaganur K., and Norman E. Sladek. "Inhibition of Human Class 3 Aldehyde Dehydrogenase, and Sensitization of Tumor Cells that Express Significant Amounts of this Enzyme to Oxazaphosphorines, by the Naturally Occurring Compound Gossypol." In Advances in Experimental Medicine and Biology. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5871-2_16.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Koivusalo, Martti, and Kai O. Lindros. "Phenethyl Isothiocyanate as an Inhibitor of Aldehyde Dehydrogenases." In Advances in Experimental Medicine and Biology. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5871-2_26.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Havel, Shelby L., and Michael D. Griswold. "Inhibiting Aldehyde Dehydrogenase Function Using WIN 18,446 to Synchronize Spermatogenesis." In Methods in Molecular Biology. Springer US, 2025. https://doi.org/10.1007/978-1-0716-4698-4_6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Aldehyde Dehydrogenase Inhibition"

1

Choi, Seung A., Jung Won Choi, Kyu-Chang Wang, et al. "Abstract 5513: Targeting brain tumor initiating cells in atypical teratoid/rhabdoid tumors: Aldehyde dehydrogenase inhibition with disulfiram." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-5513.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Simpkins, F., K. Hew, D. Azzam, et al. "Abstract POSTER-THER-1431: Combined Src and MEK inhibition decreases ovarian cancer (OVCA) cell growth, tumorigenicity and aldehyde dehydrogenase positive tumor-initiating-cells." In Abstracts: 10th Biennial Ovarian Cancer Research Symposium; September 8-9, 2014; Seattle, WA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1557-3265.ovcasymp14-poster-ther-1431.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Awad, Ola, Jason T. Yustein, Preeti Shah, et al. "Abstract 4274: High aldehyde dehydrogenase activity identifies a chemotherapy-resistant population of ewing's sarcoma cells with a stem cell phenotype that retains sensitivity to EWS-FLI1 inhibition." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4274.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Koh, Hyeon Kang, Soo Yeon Seo, Jin Ho Kim, et al. "Abstract 4872: Disulfiam, a re-positioned aldehyde dehydrogenase inhibitor, enhances radiosensitivity of human glioblastoma cellsin vitro." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4872.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Koh, Hyeon Kang, Soo Yeon Seo, Jin Ho Kim, et al. "Abstract 4872: Disulfiam, a re-positioned aldehyde dehydrogenase inhibitor, enhances radiosensitivity of human glioblastoma cellsin vitro." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4872.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Bobustuc, George C., Alisher Holmuhamedov, Kalkunte S. Srivenugopal, Jacob C. Frick, JAMES L. WEESE, and Santhi D. Konduri. "Abstract 3493: Disulfiram a dual mgmt and aldehyde dehydrogenase inhibitor sensitizes pancreatic cancer to gemcitabine and abraxane." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-3493.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Parise, Robert A., Jan Beumer, Dana Clausen, Merrill Egorin, Joseph Covey, and Julie Eiseman. "Abstract 5465: Modulation of DMS612 (BEN) pharmacokinetics and metabolism in mice by disulfiram, and aldehyde dehydrogenase inhibitor." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-5465.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Bobustuc, George C., Deborah Donohoe, Alisher Holmuhamedov, Srivenugopal Kalkunte, and Santhi D. Konduri. "Abstract 285: Disulfiram, a dual MGMT and aldehyde dehydrogenase inhibitor, sensitizes ER-positive breast cancer cells to temozolomide and cyclophosphamide." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-285.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!