PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31697031-9 2020 RESULTS: Toxicity of long-chain aldehydes to FALDH-deficient cells owing to accumulation under the profound epidermis layer improves oxidative stress in the cell resulting in keratinocyte hyperproliferation. Aldehydes 32-41 aldehyde dehydrogenase 3 family member A2 Homo sapiens 45-50 32506993-1 2020 BACKGROUND: Sjogren-Larsson syndrome (SLS) is a rare genetic neurocutaneous disease caused by mutations in ALDH3A2 that results in deficiency of fatty aldehyde dehydrogenase and accumulation of fatty aldehydes and alcohols. Aldehydes 200-209 aldehyde dehydrogenase 3 family member A2 Homo sapiens 107-114 25432520-7 2015 Sjogren-Larsson syndrome (SLS) is caused by defects in the microsomal fatty aldehyde dehydrogenase (FALDH) leading to the accumulation of fatty alcohols and fatty aldehydes. Aldehydes 163-172 aldehyde dehydrogenase 3 family member A2 Homo sapiens 70-98 32021380-8 2020 The primary role of FALDH is oxidation of medium and long-chain aliphatic aldehydes derived from fatty alcohol, phytanic acid, ether glycerolipids and sphingolipids. Aldehydes 74-83 aldehyde dehydrogenase 3 family member A2 Homo sapiens 20-25 28543186-1 2018 Sjogren-Larsson syndrome (SLS) is caused by an autosomal recessive mutation in ALDH3A2, which encodes the fatty aldehyde dehydrogenase responsible for the metabolism of long-chain aliphatic aldehydes and alcohols. Aldehydes 190-199 aldehyde dehydrogenase 3 family member A2 Homo sapiens 79-86 28543186-1 2018 Sjogren-Larsson syndrome (SLS) is caused by an autosomal recessive mutation in ALDH3A2, which encodes the fatty aldehyde dehydrogenase responsible for the metabolism of long-chain aliphatic aldehydes and alcohols. Aldehydes 190-199 aldehyde dehydrogenase 3 family member A2 Homo sapiens 106-134 27012748-15 2016 The major neutralizing enzymes include fatty aldehyde dehydrogenase (FALDH), aldose reductase (AR) and alcohol dehydrogenase (ADH), which transform the aldehyde to the corresponding carboxylic acid or alcohols, respectively, or by biding to the thiol group in glutathione (GSH) by the action of glutathione-S-transferase (GST). Aldehydes 45-53 aldehyde dehydrogenase 3 family member A2 Homo sapiens 69-74 25344796-11 2015 The only derivative carrying a free carboxyl group (N-adipoyl APAL) was surprisingly better substrate than ABAL in PsAMADH2 reaction indicating that also negatively charged aldehydes might be good substrates for ALDH10 family. Aldehydes 173-182 aldehyde dehydrogenase 3 family member A2 Homo sapiens 212-218 31273323-2 2019 It is an inborn error of lipid metabolism caused by biallelic mutations in the ALDH3A2 gene encoding the fatty aldehyde dehydrogenase that plays a pivotal role in metabolism of long-chain aliphatic aldehydes and alcohols. Aldehydes 198-207 aldehyde dehydrogenase 3 family member A2 Homo sapiens 79-86 31273323-2 2019 It is an inborn error of lipid metabolism caused by biallelic mutations in the ALDH3A2 gene encoding the fatty aldehyde dehydrogenase that plays a pivotal role in metabolism of long-chain aliphatic aldehydes and alcohols. Aldehydes 198-207 aldehyde dehydrogenase 3 family member A2 Homo sapiens 105-133 27547594-2 2016 It is caused by inactivating mutations in ALDH3A2, which codes for fatty aldehyde dehydrogenase (FALDH) and results in abnormal metabolism of long-chain aliphatic aldehydes and alcohols. Aldehydes 163-172 aldehyde dehydrogenase 3 family member A2 Homo sapiens 42-49 27547594-2 2016 It is caused by inactivating mutations in ALDH3A2, which codes for fatty aldehyde dehydrogenase (FALDH) and results in abnormal metabolism of long-chain aliphatic aldehydes and alcohols. Aldehydes 163-172 aldehyde dehydrogenase 3 family member A2 Homo sapiens 67-95 27547594-2 2016 It is caused by inactivating mutations in ALDH3A2, which codes for fatty aldehyde dehydrogenase (FALDH) and results in abnormal metabolism of long-chain aliphatic aldehydes and alcohols. Aldehydes 163-172 aldehyde dehydrogenase 3 family member A2 Homo sapiens 97-102 25432520-7 2015 Sjogren-Larsson syndrome (SLS) is caused by defects in the microsomal fatty aldehyde dehydrogenase (FALDH) leading to the accumulation of fatty alcohols and fatty aldehydes. Aldehydes 163-172 aldehyde dehydrogenase 3 family member A2 Homo sapiens 100-105 18174527-11 2008 CONCLUSION: Oxidative stress induced by reactive aldehydes, such as HNE, is implicated in the development of insulin resistance in 3T3-L1 adipocytes, which is alleviated by FALDH. Aldehydes 49-58 aldehyde dehydrogenase 3 family member A2 Homo sapiens 173-178 21187079-3 2011 The oxidation of FOH and GGOH into their aldehyde intermediates were mainly mediated by alcohol dehydrogenases 1 (in the liver and colon) and 7 (in the stomach and lung), and the subsequent step into the carboxylic acids was catalyzed by a microsomal aldehyde dehydrogenase. Aldehydes 41-49 aldehyde dehydrogenase 3 family member A2 Homo sapiens 240-273 24036493-3 2014 The fatty aldehyde generated by these pathways is chiefly metabolized to fatty acid by fatty aldehyde dehydrogenase (FALDH, alternately known as ALDH3A2), which also functions to oxidize fatty alcohols as a component of the fatty alcohol:NAD oxidoreductase (FAO) enzyme complex. Aldehydes 10-18 aldehyde dehydrogenase 3 family member A2 Homo sapiens 87-115 24036493-3 2014 The fatty aldehyde generated by these pathways is chiefly metabolized to fatty acid by fatty aldehyde dehydrogenase (FALDH, alternately known as ALDH3A2), which also functions to oxidize fatty alcohols as a component of the fatty alcohol:NAD oxidoreductase (FAO) enzyme complex. Aldehydes 10-18 aldehyde dehydrogenase 3 family member A2 Homo sapiens 117-122 24036493-3 2014 The fatty aldehyde generated by these pathways is chiefly metabolized to fatty acid by fatty aldehyde dehydrogenase (FALDH, alternately known as ALDH3A2), which also functions to oxidize fatty alcohols as a component of the fatty alcohol:NAD oxidoreductase (FAO) enzyme complex. Aldehydes 10-18 aldehyde dehydrogenase 3 family member A2 Homo sapiens 145-152 19965611-3 2010 Using a fluorescent aldehyde, pyrenedecanal, and HPLC with fluorescence detection, we developed a novel method to monitor fatty aldehyde dehydrogenase activity by quantification of the product pyrenedecanoic acid together with the substrate pyrenedecanal and possible side products, such as aldehyde adducts. Aldehydes 20-28 aldehyde dehydrogenase 3 family member A2 Homo sapiens 122-150 15834613-2 2005 Sjogren-Larsson Syndrome (SLS) is caused by an autosomal recessive defect in the gene coding for fatty aldehyde dehydrogenase (FALDH), an enzyme necessary for the oxidation of long-chain aliphatic aldehydes to fatty acid as one enzyme of the fatty alcohol:nicotinamide-adenine dinucleotide (NAD+)-oxidoreductase complex (FAO). Aldehydes 197-206 aldehyde dehydrogenase 3 family member A2 Homo sapiens 97-125 18035827-9 2007 A structural model of FALDH has been constructed, and catalytically important residues have been proposed to be involved in alcohol and aldehyde oxidation: Gln-120, Glu-207, Cys-241, Phe-333, Tyr-410 and His-411. Aldehydes 136-144 aldehyde dehydrogenase 3 family member A2 Homo sapiens 22-27 16525484-7 2006 Toxicity of long-chain aldehydes for FALDH-deficient cells decreased almost to the level of unaffected keratinocytes. Aldehydes 23-32 aldehyde dehydrogenase 3 family member A2 Homo sapiens 37-42 15834613-2 2005 Sjogren-Larsson Syndrome (SLS) is caused by an autosomal recessive defect in the gene coding for fatty aldehyde dehydrogenase (FALDH), an enzyme necessary for the oxidation of long-chain aliphatic aldehydes to fatty acid as one enzyme of the fatty alcohol:nicotinamide-adenine dinucleotide (NAD+)-oxidoreductase complex (FAO). Aldehydes 197-206 aldehyde dehydrogenase 3 family member A2 Homo sapiens 127-132 15834613-8 2005 Moreover, FALDH-transduced cells regained resistance over exposure to long chain aldehydes, which are otherwise toxic to FALDH-deficient cells. Aldehydes 81-90 aldehyde dehydrogenase 3 family member A2 Homo sapiens 10-15 15834613-8 2005 Moreover, FALDH-transduced cells regained resistance over exposure to long chain aldehydes, which are otherwise toxic to FALDH-deficient cells. Aldehydes 81-90 aldehyde dehydrogenase 3 family member A2 Homo sapiens 121-126