ALDH1A1

This protein belongs to the aldehyde dehydrogenases family of proteins and is a member of the ALDH1 subfamily (including ALDH1A2, ALDH1A3, ALDH1B1, ALDH2). Aldehyde dehydrogenase isozymes are NAD(P)-dependent dehydrogenases that catalyze the oxidation of an aldehyde into the corresponding carboxylic acid while reducing NAD+ or NADP+. ALDH1A1 is the only ALDH1 isozyme known to oxidize 9-cis retinaldehyde into 9-cis retinoic acid{{Cite journal |last1=Labrecque |first1=J |last2=Dumas |first2=F |last3=Lacroix |first3=A |last4=Bhat |first4=P V |date=1995-01-15 |title=A novel isoenzyme of aldehyde dehydrogenase specifically involved in the biosynthesis of 9-cis and all-trans retinoic acid |url=https://portlandpress.com/biochemj/article-abstract/305/2/681/30791/A-novel-isoenzyme-of-aldehyde-dehydrogenase?redirectedFrom=fulltext |journal=Biochemical Journal |volume=305 |issue=2 |pages=681–684 |doi=10.1042/bj3050681 |issn=0264-6021 |pmc=1136415 |pmid=7832787}} and thus serve as the only known activator of the rexinoid nuclear receptor pathway.{{Cite journal |last1=Esposito |first1=Mark |last2=Amory |first2=John K. |last3=Kang |first3=Yibin |date=2024-08-12 |title=The pathogenic role of retinoid nuclear receptor signaling in cancer and metabolic syndromes |url=https://rupress.org/jem/article/221/9/e20240519/276897/The-pathogenic-role-of-retinoid-nuclear-receptor |journal=Journal of Experimental Medicine |volume=221 |issue=9 |pages=e20240519 |doi=10.1084/jem.20240519 |pmid=39133222 |pmc=11318670 |issn=0022-1007}} ALDH1A1 has also been described with activity against other substrates in living systems, including all-trans retinaldehyde{{Cite journal |last1=Topping |first1=Traci |last2=Griswold |first2=Michael D. |date=2022 |title=Global Deletion of ALDH1A1 and ALDH1A2 Genes Does Not Affect Viability but Blocks Spermatogenesis |journal=Frontiers in Endocrinology |volume=13 |pages=871225 |doi=10.3389/fendo.2022.871225 |doi-access=free |issn=1664-2392 |pmc=9097449 |pmid=35574006}} as well as oxazaphosphorine, a cyclophosphamide metabolite.{{Cite journal |last1=Sládek |first1=Norman E. |last2=Kollander |first2=Rahn |last3=Sreerama |first3=Lakshmaiah |last4=Kiang |first4=David T. |date=2002-04-01 |title=Cellular levels of aldehyde dehydrogenases (ALDH1A1 and ALDH3A1) as predictors of therapeutic responses to cyclophosphamide-based chemotherapy of breast cancer: a retrospective study |url=https://link.springer.com/article/10.1007/s00280-001-0412-4 |journal=Cancer Chemotherapy and Pharmacology |language=en |volume=49 |issue=4 |pages=309–321 |doi=10.1007/s00280-001-0412-4 |issn=1432-0843|url-access=subscription }} Unique among the ALDH1 isozymes, ALDH1A1 is known to possess esterase activity in biochemical studies,{{Cite journal |last1=Koppaka |first1=Vindhya |last2=Thompson |first2=David C. |last3=Chen |first3=Ying |last4=Ellermann |first4=Manuel |last5=Nicolaou |first5=Kyriacos C. |last6=Juvonen |first6=Risto O. |last7=Petersen |first7=Dennis |last8=Deitrich |first8=Richard A. |last9=Hurley |first9=Thomas D. |last10=Vasiliou |first10=Vasilis |date=2012-07-01 |editor-last=Sibley |editor-first=David R. |title=Aldehyde Dehydrogenase Inhibitors: a Comprehensive Review of the Pharmacology, Mechanism of Action, Substrate Specificity, and Clinical Application |url=https://pharmrev.aspetjournals.org/content/64/3/520 |journal=Pharmacological Reviews |language=en |volume=64 |issue=3 |pages=520–539 |doi=10.1124/pr.111.005538 |issn=0031-6997 |pmc=3400832 |pmid=22544865}} although it is unclear whether this is functionally relevant living tissues.

ALDH1A1 is expressed predominantly in metabolic tissues, including the liver, gastrointestinal tract, thyroid, pituitary gland, and adipose tissues.{{Cite web |title=Tissue expression of ALDH1A1 - Summary - The Human Protein Atlas |url=https://www.proteinatlas.org/ENSG00000165092-ALDH1A1/tissue |access-date=2024-12-03 |website=www.proteinatlas.org}} ALDH1A1 is also expressed in the testes where its function in spermatogenesis is subordinate to and compensatory for ALDH1A2 in mice. ALDH1A1 is inhibited by Antabuse (disulfiram),{{Cite journal |last=Omran |first=Ziad |date=2022-01-12 |title=Novel Disulfiram Derivatives as ALDH1a1-Selective Inhibitors |journal=Molecules (Basel, Switzerland) |volume=27 |issue=2 |pages=480 |doi=10.3390/molecules27020480 |doi-access=free |issn=1420-3049 |pmc=8778300 |pmid=35056791}} though the primary pharmacologic target of disulfiram in clinical use is ALDH2. The long clinical history of disulfiram use suggests that ALDH1A1 is not important to normal human physiology. Tumors, specifically in ovarian cancer are found to have a high expression of ALDH1A1{{Cite journal |last=Muralikrishnan |first=Vaishnavi |title=Targeting Aldehyde Dehydrogenases to Eliminate Cancer Stem Cells in Gynecologic Malignancies |url=https://pubmed.ncbi.nlm.nih.gov/32295073/ |journal=MDPI Cancers |pmid=32295073}}.ALDH1A1 is found to cause resistance to chemotherapy.{{Cite journal |last=Muralikrishnan |first=Vaishnavi |title=A Novel ALDH1A1 Inhibitor Blocks Platinum-Induced Senescence and Stemness in Ovarian Cancer |url=https://pmc.ncbi.nlm.nih.gov/articles/PMC9318275/#B12-cancers-14-03437 |journal=MDPI Cancers |pmid=35884498}}

The removal of ALDH1A1 in mice through genetic knockout results in viable animals that are fertile and healthy. The only validated phenotype of these mice is a resistance to high fat diet-induced obesity{{Cite journal |last1=Kiefer |first1=Florian W. |last2=Vernochet |first2=Cecile |last3=O'Brien |first3=Patrick |last4=Spoerl |first4=Steffen |last5=Brown |first5=Jonathan D. |last6=Nallamshetty |first6=Shriram |last7=Zeyda |first7=Maximilian |last8=Stulnig |first8=Thomas M. |last9=Cohen |first9=David E. |last10=Kahn |first10=C. Ronald |last11=Plutzky |first11=Jorge |date=June 2012 |title=Retinaldehyde dehydrogenase 1 regulates a thermogenic program in white adipose tissue |journal=Nature Medicine |language=en |volume=18 |issue=6 |pages=918–925 |doi=10.1038/nm.2757 |issn=1546-170X |pmc=3792792 |pmid=22561685}} while whole body ALDH1A1 removal does not affect fertility or neurological function. This biology closely replicates the clinical profile of Antabuse (disulfiram). Disulfiram and other ALDH1A1 inhibitors have been shown to cause ALDH1A1-dependent weight loss in obese animals.{{Cite journal |last1=Bernier |first1=Michel |last2=Mitchell |first2=Sarah J. |last3=Wahl |first3=Devin |last4=Diaz |first4=Antonio |last5=Singh |first5=Abhishek |last6=Seo |first6=Wonhyo |last7=Wang |first7=Mingy |last8=Ali |first8=Ahmed |last9=Kaiser |first9=Tamzin |last10=Price |first10=Nathan L. |last11=Aon |first11=Miguel A. |last12=Kim |first12=Eun-Young |last13=Petr |first13=Michael A. |last14=Cai |first14=Huan |last15=Warren |first15=Alessa |date=2020-08-04 |title=Disulfiram Treatment Normalizes Body Weight in Obese Mice |journal=Cell Metabolism |language=English |volume=32 |issue=2 |pages=203–214.e4 |doi=10.1016/j.cmet.2020.04.019 |issn=1550-4131 |pmc=7957855 |pmid=32413333}} This has increased interest in disulfiram as an alternative weight loss therapy to Ozempic,{{Cite web |date=2020-05-14 |title=Repurposed drug helps obese mice lose weight, improve metabolic function |url=https://www.nih.gov/news-events/news-releases/repurposed-drug-helps-obese-mice-lose-weight-improve-metabolic-function |access-date=2024-12-03 |website=National Institutes of Health (NIH) |language=EN}} yet the rare but potentially fatal liver-damaging effects of disulfiram due to its broad lack of selectivity as well as the alcohol-disulfiram reaction make it unattractive as a weight loss therapy.{{Cite web |title=Disulfiram: Package Insert / Prescribing Information |url=https://www.drugs.com/pro/disulfiram.html |access-date=2024-12-03 |website=Drugs.com |language=en}} Subsequent efforts to produce ALDH1A1-specific inhibitors have resulted in preclinical compounds that induce weight loss through increased metabolic activity.{{Cite journal |last1=Haenisch |first1=Michael |last2=Treuting |first2=Piper M. |last3=Brabb |first3=Thea |last4=Goldstein |first4=Alex S. |last5=Berkseth |first5=Kathryn |last6=Amory |first6=John K. |last7=Paik |first7=Jisun |date=2018-01-01 |title=Pharmacological inhibition of ALDH1A enzymes suppresses weight gain in a mouse model of diet-induced obesity |journal=Obesity Research & Clinical Practice |volume=12 |issue=1 |pages=93–101 |doi=10.1016/j.orcp.2017.08.003 |issn=1871-403X |pmc=5816716 |pmid=28919001}}

ALDH1A1 is often attributed with multiple biological roles as studies prior to human genome sequencing operated under the assumption that only one ALDH1 gene existed rather than the five isozymes that are annotated today.{{Cite journal |last1=Vasiliou |first1=V. |last2=Bairoch |first2=A. |last3=Tipton |first3=K. F. |last4=Nebert |first4=D. W. |date=August 1999 |title=Eukaryotic aldehyde dehydrogenase (ALDH) genes: human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping |url=https://pubmed.ncbi.nlm.nih.gov/10780262/ |journal=Pharmacogenetics |volume=9 |issue=4 |pages=421–434 |issn=0960-314X |pmid=10780262}} Accordingly, ALDH1A1 is often attributed with a role in alcohol metabolism through oxidation of acetaldehyde, however, single nucleotide polymorphisms (SNPs) in this enzyme show little evidence of linkage to alcoholism in humans.{{cite journal | vauthors = Sherva R, Rice JP, Neuman RJ, Rochberg N, Saccone NL, Bierut LJ | title = Associations and interactions between SNPs in the alcohol metabolizing genes and alcoholism phenotypes in European Americans | journal = Alcoholism: Clinical and Experimental Research | volume = 33 | issue = 5 | pages = 848–57 | date = May 2009 | pmid = 19298322 | pmc = 2892966 | doi = 10.1111/j.1530-0277.2009.00904.x }}{{cite journal | vauthors = Liu J, Zhou Z, Hodgkinson CA, Yuan Q, Shen PH, Mulligan CJ, Wang A, Gray RR, Roy A, Virkkunen M, Goldman D, Enoch MA | display-authors = 6 | title = Haplotype-based study of the association of alcohol-metabolizing genes with alcohol dependence in four independent populations | journal = Alcoholism: Clinical and Experimental Research | volume = 35 | issue = 2 | pages = 304–16 | date = February 2011 | pmid = 21083667 | pmc = 3026908 | doi = 10.1111/j.1530-0277.2010.01346.x }} Despite established naming conventions, many studies still incorrectly use ALDH1 to describe the family of isozymes. For instance, many cancers studies have been interpreted to report on ALDH1A1 activity when the actual protein was ALDH1A3.{{Cite journal |last1=Ginestier |first1=Christophe |last2=Hur |first2=Min Hee |last3=Charafe-Jauffret |first3=Emmanuelle |last4=Monville |first4=Florence |last5=Dutcher |first5=Julie |last6=Brown |first6=Marty |last7=Jacquemier |first7=Jocelyne |last8=Viens |first8=Patrice |last9=Kleer |first9=Celina G. |last10=Liu |first10=Suling |last11=Schott |first11=Anne |last12=Hayes |first12=Dan |last13=Birnbaum |first13=Daniel |last14=Wicha |first14=Max S. |last15=Dontu |first15=Gabriela |date=2007-11-15 |title=ALDH1 Is a Marker of Normal and Malignant Human Mammary Stem Cells and a Predictor of Poor Clinical Outcome |journal=Cell Stem Cell |language=English |volume=1 |issue=5 |pages=555–567 |doi=10.1016/j.stem.2007.08.014 |issn=1934-5909 |pmc=2423808 |pmid=18371393}}

ALDH1A1 possesses unique taxon-specific traits across mammals. Found uniquely in rabbits compared to other mammals, ALDH1A1 appears to function as a corneal crystallin that helps to maintain the transparency of the cornea. In other species such as humans, this role is performed by ALDH3A1.{{cite journal | vauthors = Jester JV, Moller-Pedersen T, Huang J, Sax CM, Kays WT, Cavangh HD, Petroll WM, Piatigorsky J | display-authors = 6 | title = The cellular basis of corneal transparency: evidence for 'corneal crystallins' | journal = Journal of Cell Science | volume = 112 | issue = 5 | pages = 613–22 | date = March 1999 | pmid = 9973596 | doi = 10.1242/jcs.112.5.613 | series = 112 }} In beavers, the ALDH1A1 gene has undergone genomic expansion, resulting in approximately 10 copies of the genomic locus, which is putatively linked to a role in lipid balance.{{Cite journal |last1=Zhang |first1=Quanwei |last2=Tombline |first2=Gregory |last3=Ablaeva |first3=Julia |last4=Zhang |first4=Lei |last5=Zhou |first5=Xuming |last6=Smith |first6=Zachary |last7=Zhao |first7=Yang |last8=Xiaoli |first8=Alus M. |last9=Wang |first9=Zhen |last10=Lin |first10=Jhih-Rong |last11=Jabalameli |first11=M. Reza |last12=Mitra |first12=Joydeep |last13=Nguyen |first13=Nha |last14=Vijg |first14=Jan |last15=Seluanov |first15=Andrei |date=2021-11-09 |title=Genomic expansion of Aldh1a1 protects beavers against high metabolic aldehydes from lipid oxidation |journal=Cell Reports |volume=37 |issue=6 |pages=109965 |doi=10.1016/j.celrep.2021.109965 |issn=2211-1247 |pmc=8656434 |pmid=34758328}}

{{Reflist}}

• {{UCSC gene info|ALDH1A1}}

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• {{cite journal | vauthors = Walsh N, Dowling P, O'Donovan N, Henry M, Meleady P, Clynes M | title = Aldehyde dehydrogenase 1A1 and gelsolin identified as novel invasion-modulating factors in conditioned medium of pancreatic cancer cells | journal = Journal of Proteomics | volume = 71 | issue = 5 | pages = 561–71 | date = December 2008 | pmid = 18848913 | doi = 10.1016/j.jprot.2008.09.002 | url = http://doras.dcu.ie/2363/1/Aldehyde_dehydrogenase_1A1_and_gelsolin.pdf }}
• {{cite journal | vauthors = Barley K, Dracheva S, Byne W | title = Subcortical oligodendrocyte- and astrocyte-associated gene expression in subjects with schizophrenia, major depression and bipolar disorder | journal = Schizophrenia Research | volume = 112 | issue = 1–3 | pages = 54–64 | date = July 2009 | pmid = 19447584 | doi = 10.1016/j.schres.2009.04.019 | s2cid = 39003080 }}
• {{cite journal | vauthors = Ekhart C, Doodeman VD, Rodenhuis S, Smits PH, Beijnen JH, Huitema AD | title = Influence of polymorphisms of drug metabolizing enzymes (CYP2B6, CYP2C9, CYP2C19, CYP3A4, CYP3A5, GSTA1, GSTP1, ALDH1A1 and ALDH3A1) on the pharmacokinetics of cyclophosphamide and 4-hydroxycyclophosphamide | journal = Pharmacogenetics and Genomics | volume = 18 | issue = 6 | pages = 515–23 | date = June 2008 | pmid = 18496131 | doi = 10.1097/FPC.0b013e3282fc9766 | s2cid = 5604777 }}
• {{cite journal | vauthors = Rodriguez FJ, Giannini C, Asmann YW, Sharma MK, Perry A, Tibbetts KM, Jenkins RB, Scheithauer BW, Anant S, Jenkins S, Eberhart CG, Sarkaria JN, Gutmann DH | display-authors = 6 | title = Gene expression profiling of NF-1-associated and sporadic pilocytic astrocytoma identifies aldehyde dehydrogenase 1 family member L1 (ALDH1L1) as an underexpressed candidate biomarker in aggressive subtypes | journal = Journal of Neuropathology and Experimental Neurology | volume = 67 | issue = 12 | pages = 1194–204 | date = December 2008 | pmid = 19018242 | pmc = 2730602 | doi = 10.1097/NEN.0b013e31818fbe1e }}
• {{cite journal | vauthors = Carpentino JE, Hynes MJ, Appelman HD, Zheng T, Steindler DA, Scott EW, Huang EH | title = Aldehyde dehydrogenase-expressing colon stem cells contribute to tumorigenesis in the transition from colitis to cancer | journal = Cancer Research | volume = 69 | issue = 20 | pages = 8208–15 | date = October 2009 | pmid = 19808966 | pmc = 2776663 | doi = 10.1158/0008-5472.CAN-09-1132 }}
• {{cite journal | vauthors = Ma S, Chan KW, Lee TK, Tang KH, Wo JY, Zheng BJ, Guan XY | title = Aldehyde dehydrogenase discriminates the CD133 liver cancer stem cell populations | journal = Molecular Cancer Research | volume = 6 | issue = 7 | pages = 1146–53 | date = July 2008 | pmid = 18644979 | doi = 10.1158/1541-7786.MCR-08-0035 | doi-access = free }}
• {{cite journal | vauthors = Xiao T, Shoeb M, Siddiqui MS, Zhang M, Ramana KV, Srivastava SK, Vasiliou V, Ansari NH | display-authors = 6 | title = Molecular cloning and oxidative modification of human lens ALDH1A1: implication in impaired detoxification of lipid aldehydes | journal = Journal of Toxicology and Environmental Health. Part A | volume = 72 | issue = 9 | pages = 577–84 | year = 2009 | pmid = 19296407 | pmc = 5645793 | doi = 10.1080/15287390802706371 | bibcode = 2009JTEHA..72..577X }}
• {{cite journal | vauthors = Cañestro C, Catchen JM, Rodríguez-Marí A, Yokoi H, Postlethwait JH | title = Consequences of lineage-specific gene loss on functional evolution of surviving paralogs: ALDH1A and retinoic acid signaling in vertebrate genomes | journal = PLOS Genetics | volume = 5 | issue = 5 | pages = e1000496 | date = May 2009 | pmid = 19478994 | pmc = 2682703 | doi = 10.1371/journal.pgen.1000496 | editor1-last = Gojobori | editor1-first = Takashi | doi-access = free }}
• {{cite journal | vauthors = Saito A, Kawamoto M, Kamatani N | title = Association study between single-nucleotide polymorphisms in 199 drug-related genes and commonly measured quantitative traits of 752 healthy Japanese subjects | journal = Journal of Human Genetics | volume = 54 | issue = 6 | pages = 317–23 | date = June 2009 | pmid = 19343046 | doi = 10.1038/jhg.2009.31 | doi-access = free }}
• {{cite journal | vauthors = Chen YC, Chen YW, Hsu HS, Tseng LM, Huang PI, Lu KH, Chen DT, Tai LK, Yung MC, Chang SC, Ku HH, Chiou SH, Lo WL | display-authors = 6 | title = Aldehyde dehydrogenase 1 is a putative marker for cancer stem cells in head and neck squamous cancer | journal = Biochemical and Biophysical Research Communications | volume = 385 | issue = 3 | pages = 307–13 | date = July 2009 | pmid = 19450560 | doi = 10.1016/j.bbrc.2009.05.048 }}
• {{cite journal | vauthors = Tabakoff B, Saba L, Printz M, Flodman P, Hodgkinson C, Goldman D, Koob G, Richardson HN, Kechris K, Bell RL, Hübner N, Heinig M, Pravenec M, Mangion J, Legault L, Dongier M, Conigrave KM, Whitfield JB, Saunders J, Grant B, Hoffman PL | display-authors = 6 | title = Genetical genomic determinants of alcohol consumption in rats and humans | journal = BMC Biology | volume = 7 | pages = 70 | date = October 2009 | pmid = 19874574 | pmc = 2777866 | doi = 10.1186/1741-7007-7-70 | doi-access = free }}
• {{cite journal | vauthors = Morimoto K, Kim SJ, Tanei T, Shimazu K, Tanji Y, Taguchi T, Tamaki Y, Terada N, Noguchi S | display-authors = 6 | title = Stem cell marker aldehyde dehydrogenase 1-positive breast cancers are characterized by negative estrogen receptor, positive human epidermal growth factor receptor type 2, and high Ki67 expression | journal = Cancer Science | volume = 100 | issue = 6 | pages = 1062–8 | date = June 2009 | pmid = 19385968 | doi = 10.1111/j.1349-7006.2009.01151.x | s2cid = 22510108 | doi-access = free | pmc = 11158415 }}
• {{cite journal | vauthors = Ekhart C, Rodenhuis S, Smits PH, Beijnen JH, Huitema AD | title = Relations between polymorphisms in drug-metabolising enzymes and toxicity of chemotherapy with cyclophosphamide, thiotepa and carboplatin | journal = Pharmacogenetics and Genomics | volume = 18 | issue = 11 | pages = 1009–15 | date = November 2008 | pmid = 18854779 | doi = 10.1097/FPC.0b013e328313aaa4 | s2cid = 2979088 }}
• {{cite journal | vauthors = Wan C, Shi Y, Zhao X, Tang W, Zhang M, Ji B, Zhu H, Xu Y, Li H, Feng G, He L | display-authors = 6 | title = Positive association between ALDH1A2 and schizophrenia in the Chinese population | journal = Progress in Neuro-Psychopharmacology & Biological Psychiatry | volume = 33 | issue = 8 | pages = 1491–5 | date = November 2009 | pmid = 19703508 | doi = 10.1016/j.pnpbp.2009.08.008 | s2cid = 32862839 }}
• {{cite journal | vauthors = Low SK, Kiyotani K, Mushiroda T, Daigo Y, Nakamura Y, Zembutsu H | title = Association study of genetic polymorphism in ABCC4 with cyclophosphamide-induced adverse drug reactions in breast cancer patients | journal = Journal of Human Genetics | volume = 54 | issue = 10 | pages = 564–71 | date = October 2009 | pmid = 19696793 | doi = 10.1038/jhg.2009.79 | doi-access = free }}
• {{cite journal | vauthors = Moore SM, Liang T, Graves TJ, McCall KM, Carr LG, Ehlers CL | title = Identification of a novel cytosolic aldehyde dehydrogenase allele, ALDH1A1*4 | journal = Human Genomics | volume = 3 | issue = 4 | pages = 304–7 | date = July 2009 | pmid = 19706361 | pmc = 2885287 | doi = 10.1186/1479-7364-3-4-304 | doi-access = free }}
• {{cite journal | vauthors = Chang B, Liu G, Xue F, Rosen DG, Xiao L, Wang X, Liu J | title = ALDH1 expression correlates with favorable prognosis in ovarian cancers | journal = Modern Pathology | volume = 22 | issue = 6 | pages = 817–23 | date = June 2009 | pmid = 19329942 | pmc = 2692456 | doi = 10.1038/modpathol.2009.35 }}
• {{cite journal | vauthors = Lind PA, Eriksson CJ, Wilhelmsen KC | title = The role of aldehyde dehydrogenase-1 (ALDH1A1) polymorphisms in harmful alcohol consumption in a Finnish population | journal = Human Genomics | volume = 3 | issue = 1 | pages = 24–35 | date = September 2008 | pmid = 19129088 | pmc = 3525184 | doi = 10.1186/1479-7364-3-1-24 | doi-access = free }}
• {{cite journal | vauthors = Moreb JS, Baker HV, Chang LJ, Amaya M, Lopez MC, Ostmark B, Chou W | title = ALDH isozymes downregulation affects cell growth, cell motility and gene expression in lung cancer cells | journal = Molecular Cancer | volume = 7 | issue = 1 | pages = 87 | date = November 2008 | pmid = 19025616 | pmc = 2605459 | doi = 10.1186/1476-4598-7-87 | doi-access = free }}
• {{cite journal | vauthors = Dancik GM, Varisli L, Vlahopoulos SA | title = The Molecular Context of Oxidant Stress Response in Cancer Establishes ALDH1A1 as a Critical Target: What This Means for Acute Myeloid Leukemia. | journal = International Journal of Molecular Sciences | date = 2023 | volume = 24 | issue = 11 | pages = 9372 | doi = 10.3390/ijms24119372 | pmid = 37298333 | pmc = 10253856 | doi-access = free }}

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{{NLM content}}

{{Aldehyde dehydrogenases}}

Category:Enzymes

Category:Ophthalmology