PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22100631-13 2012 The second, ALDH1L1, also known as FDH, is required for DNA nucleotide biosynthesis, and is upregulated at high concentrations of folate. Folic Acid 130-136 aldehyde dehydrogenase 1 family member L1 Homo sapiens 12-19 22100631-13 2012 The second, ALDH1L1, also known as FDH, is required for DNA nucleotide biosynthesis, and is upregulated at high concentrations of folate. Folic Acid 130-136 aldehyde dehydrogenase 1 family member L1 Homo sapiens 35-38 22100631-16 2012 Our second hypothesis is that folate interacts with one of these response elements to upregulate ALDH1A1 and ALDH1L1 expression in order to decrease acetaldehyde concentrations and promote DNA stability, thereby decreasing cancer susceptibility. Folic Acid 30-36 aldehyde dehydrogenase 1 family member L1 Homo sapiens 109-116 19933275-3 2010 Recently, we have shown that one of the enzymes of folate metabolism, 10-formyltetrahydrofolate dehydrogenase (FDH), requires a 4-PP prosthetic group for catalysis. Folic Acid 51-57 aldehyde dehydrogenase 1 family member L1 Homo sapiens 70-109 21779486-1 2011 FDH (10-formyltetrahydrofolate dehydrogenase, the product of the ALDH1L1 gene), a major folate-metabolizing enzyme in the cytosol, is involved in the regulation of cellular proliferation. Folic Acid 24-30 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-3 21779486-1 2011 FDH (10-formyltetrahydrofolate dehydrogenase, the product of the ALDH1L1 gene), a major folate-metabolizing enzyme in the cytosol, is involved in the regulation of cellular proliferation. Folic Acid 24-30 aldehyde dehydrogenase 1 family member L1 Homo sapiens 65-72 20729910-9 2010 Dephosphorylation of cofilin and inhibition of motility in response to FDH can also be prevented by the increased folate in media. Folic Acid 114-120 aldehyde dehydrogenase 1 family member L1 Homo sapiens 71-74 20498374-1 2010 Cytosolic 10-formyltetrahydrofolate dehydrogenase (FDH, ALDH1L1) is an abundant enzyme of folate metabolism. Folic Acid 29-35 aldehyde dehydrogenase 1 family member L1 Homo sapiens 51-54 20498374-1 2010 Cytosolic 10-formyltetrahydrofolate dehydrogenase (FDH, ALDH1L1) is an abundant enzyme of folate metabolism. Folic Acid 29-35 aldehyde dehydrogenase 1 family member L1 Homo sapiens 56-63 19933275-3 2010 Recently, we have shown that one of the enzymes of folate metabolism, 10-formyltetrahydrofolate dehydrogenase (FDH), requires a 4-PP prosthetic group for catalysis. Folic Acid 51-57 aldehyde dehydrogenase 1 family member L1 Homo sapiens 111-114 18848533-4 2009 The N-terminal domain of FDH (residues 1-310) carries the folate binding site and shares sequence homology and structural topology with other enzymes utilizing 10-formyl-THF as a substrate. Folic Acid 58-64 aldehyde dehydrogenase 1 family member L1 Homo sapiens 25-28 18848533-0 2009 FDH: an aldehyde dehydrogenase fusion enzyme in folate metabolism. Folic Acid 48-54 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-3 19147541-11 2009 JNK activation in response to FDH was inhibited by high supplementation of reduced folate leucovorin, further indicating a functional connection between folate metabolism and mitogen-activated protein kinase pathways. Folic Acid 83-89 aldehyde dehydrogenase 1 family member L1 Homo sapiens 30-33 19147541-11 2009 JNK activation in response to FDH was inhibited by high supplementation of reduced folate leucovorin, further indicating a functional connection between folate metabolism and mitogen-activated protein kinase pathways. Folic Acid 153-159 aldehyde dehydrogenase 1 family member L1 Homo sapiens 30-33 16627483-3 2006 FDH has been proposed to: 1) inhibit purine biosynthesis by depleting 10-formyl-THF pools, 2) maintain cellular folate concentrations by sequestering THF, 3) deplete the supply of folate-activated one-carbon units, and 4) stimulate the generation of THF-activated one-carbon unit synthesis by channeling folate cofactors to other folate-dependent enzymes. Folic Acid 112-118 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-3 17111379-6 2007 These data provide the first evidence for localized differences in folate metabolism within the early neural tube and suggest that folate might modulate proliferation via effects on midline Aldh1l1(+) cells. Folic Acid 131-137 aldehyde dehydrogenase 1 family member L1 Homo sapiens 190-197 16712799-10 2006 FDH-resistant cells have strongly up-regulated dihydrofolate reductase (DHFR) that is proposed to be a mechanism for the alteration of folate pools and a key component of the acquired resistance. Folic Acid 54-60 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-3 16627483-0 2006 Regulation of folate-mediated one-carbon metabolism by 10-formyltetrahydrofolate dehydrogenase. Folic Acid 14-20 aldehyde dehydrogenase 1 family member L1 Homo sapiens 55-94 16627483-1 2006 10-Formyltetrahydrofolate dehydrogenase (FDH) catalyzes the NADP(+)-dependent conversion of 10-formyltetrahydrofolate to CO(2) and tetrahydrofolate (THF) and is an abundant high affinity folate-binding protein. Folic Acid 19-25 aldehyde dehydrogenase 1 family member L1 Homo sapiens 41-44 16627483-2 2006 Although several activities have been ascribed to FDH, its metabolic role in folate-mediated one-carbon metabolism is not well understood. Folic Acid 77-83 aldehyde dehydrogenase 1 family member L1 Homo sapiens 50-53 16627483-3 2006 FDH has been proposed to: 1) inhibit purine biosynthesis by depleting 10-formyl-THF pools, 2) maintain cellular folate concentrations by sequestering THF, 3) deplete the supply of folate-activated one-carbon units, and 4) stimulate the generation of THF-activated one-carbon unit synthesis by channeling folate cofactors to other folate-dependent enzymes. Folic Acid 180-186 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-3 16627483-3 2006 FDH has been proposed to: 1) inhibit purine biosynthesis by depleting 10-formyl-THF pools, 2) maintain cellular folate concentrations by sequestering THF, 3) deplete the supply of folate-activated one-carbon units, and 4) stimulate the generation of THF-activated one-carbon unit synthesis by channeling folate cofactors to other folate-dependent enzymes. Folic Acid 180-186 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-3 16627483-3 2006 FDH has been proposed to: 1) inhibit purine biosynthesis by depleting 10-formyl-THF pools, 2) maintain cellular folate concentrations by sequestering THF, 3) deplete the supply of folate-activated one-carbon units, and 4) stimulate the generation of THF-activated one-carbon unit synthesis by channeling folate cofactors to other folate-dependent enzymes. Folic Acid 180-186 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-3 16627483-5 2006 Both low and high FDH expression reduced total cellular folate concentrations by 60%, elevated rates of folate catabolism, and depleted cellular 5-methyl-THF and S-adenosylmethionine levels. Folic Acid 56-62 aldehyde dehydrogenase 1 family member L1 Homo sapiens 18-21 16627483-5 2006 Both low and high FDH expression reduced total cellular folate concentrations by 60%, elevated rates of folate catabolism, and depleted cellular 5-methyl-THF and S-adenosylmethionine levels. Folic Acid 104-110 aldehyde dehydrogenase 1 family member L1 Homo sapiens 18-21 16627483-8 2006 We conclude that low FDH expression facilitates the incorporation of one-carbon units into the one-carbon pool, whereas high levels of FDH expression deplete the folate-activated one-carbon pool by catalyzing the conversion of 10-formyl-THF to THF. Folic Acid 162-168 aldehyde dehydrogenase 1 family member L1 Homo sapiens 135-138 16627483-10 2006 FDH expression does deplete cellular 5-methyl-THF and S-adenosylmethionine levels indicating that FDH impairs the folate-dependent homocysteine remethylation cycle. Folic Acid 114-120 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-3 16627483-10 2006 FDH expression does deplete cellular 5-methyl-THF and S-adenosylmethionine levels indicating that FDH impairs the folate-dependent homocysteine remethylation cycle. Folic Acid 114-120 aldehyde dehydrogenase 1 family member L1 Homo sapiens 98-101 10585460-6 1999 All the mutants, however, were able to bind folate, although with lower affinity than wild-type N(t)-FDH. Folic Acid 44-50 aldehyde dehydrogenase 1 family member L1 Homo sapiens 96-104 27384481-1 2016 Among ALDH isoforms, ALDH1L1 in the folate pathway showed highly increased expression in non-small-cell lung cancer cells (NSCLC). Folic Acid 36-42 aldehyde dehydrogenase 1 family member L1 Homo sapiens 21-28 8975761-3 1996 The present study was designed to determine whether components of folate-dependent formate oxidation, e.g., folate and 10-CHO-H4-folate dehydrogenase (10-FDH), exist in retina and whether differences in these components might explain species-determined susceptibility to methanol intoxication. Folic Acid 66-72 aldehyde dehydrogenase 1 family member L1 Homo sapiens 154-157 30362096-2 2018 Alcohol consumption affects folate-related genes and enzymes including two major folate-metabolizing enzymes, ALDH1L1 and ALDH1L2. Folic Acid 28-34 aldehyde dehydrogenase 1 family member L1 Homo sapiens 110-117 30362096-2 2018 Alcohol consumption affects folate-related genes and enzymes including two major folate-metabolizing enzymes, ALDH1L1 and ALDH1L2. Folic Acid 81-87 aldehyde dehydrogenase 1 family member L1 Homo sapiens 110-117 30362096-3 2018 ALDH1L1 (cytosolic 10-formyltetrahydrofolate dehydrogenase) is a regulatory enzyme in folate metabolism that controls the overall flux of one-carbon groups in folate-dependent biosynthetic pathways. Folic Acid 38-44 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-7 30362096-3 2018 ALDH1L1 (cytosolic 10-formyltetrahydrofolate dehydrogenase) is a regulatory enzyme in folate metabolism that controls the overall flux of one-carbon groups in folate-dependent biosynthetic pathways. Folic Acid 86-92 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-7 30362096-3 2018 ALDH1L1 (cytosolic 10-formyltetrahydrofolate dehydrogenase) is a regulatory enzyme in folate metabolism that controls the overall flux of one-carbon groups in folate-dependent biosynthetic pathways. Folic Acid 86-92 aldehyde dehydrogenase 1 family member L1 Homo sapiens 9-58 31737034-8 2019 ALDH1L1, one of the folate-metabolizing enzymes, serves a regulatory function in folate metabolism restricting the flux of one-carbon groups through biosynthetic processes. Folic Acid 20-26 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-7 31737034-8 2019 ALDH1L1, one of the folate-metabolizing enzymes, serves a regulatory function in folate metabolism restricting the flux of one-carbon groups through biosynthetic processes. Folic Acid 81-87 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-7 31737034-11 2019 ALDH1L1 has much higher frequency of non-synonymous exonic SNPs than most other genes for folate enzymes. Folic Acid 90-96 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-7 31737034-13 2019 The effects of these SNPs on the enzyme is not clear but studies indicate that some coding and non-coding ALDH1L1 SNPs are associated with altered risk of certain cancer types and it is also likely that specific haplotypes define the metabolic response to dietary folate. Folic Acid 264-270 aldehyde dehydrogenase 1 family member L1 Homo sapiens 106-113 31737034-14 2019 This review discusses the role of ALDH1L1 in folate metabolism and etiology of diseases with the focus on non-synonymous coding ALDH1L1 SNPs and their effects on the enzyme structure/function, metabolic role and association with cancer. Folic Acid 45-51 aldehyde dehydrogenase 1 family member L1 Homo sapiens 34-41 30794800-1 2019 ALDH1L1 (cytosolic 10-formyltetrahydrofolate dehydrogenase) is the enzyme in folate metabolism commonly downregulated in human cancers. Folic Acid 38-44 aldehyde dehydrogenase 1 family member L1 Homo sapiens 0-7 30794800-4 2019 In agreement with the ALDH1L1 loss in cancer, its re-expression leads to inhibition of proliferation and to apoptosis, but also affects migration and invasion of cancer cells through a specific folate-dependent mechanism involved in invasive phenotype. Folic Acid 194-200 aldehyde dehydrogenase 1 family member L1 Homo sapiens 22-29 23519469-1 2013 We have investigated the role of ceramide in the cellular adaptation to folate stress induced by Aldh1l1, the enzyme involved in the regulation of folate metabolism. Folic Acid 72-78 aldehyde dehydrogenase 1 family member L1 Homo sapiens 97-104 26961134-8 2016 Four DM CpGs identified by SNPs in MTRR, MTHFR, and FTHFD were significantly associated with alcohol consumption and/or breast folate. Folic Acid 127-133 aldehyde dehydrogenase 1 family member L1 Homo sapiens 52-57 23519469-1 2013 We have investigated the role of ceramide in the cellular adaptation to folate stress induced by Aldh1l1, the enzyme involved in the regulation of folate metabolism. Folic Acid 147-153 aldehyde dehydrogenase 1 family member L1 Homo sapiens 97-104