ALDH1L1

Aldehyde dehydrogenase 1 family, member L1, also known as ALDH1L1, is a human gene.cite web | title = Entrez Gene: ALDH1L1 aldehyde dehydrogenase 1 family, member L1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10840| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene catalyzes the conversion of 10-formyltetrahydrofolate, NADP, and water to tetrahydrofolate, NADPH, and carbon dioxide. The encoded protein belongs to the aldehyde dehydrogenase family and is responsible for formate oxidation in vivo. Deficiencies in this gene can result in an accumulation of formate and subsequent methanol poisoning.cite web | title = Entrez Gene: ALDH1L1 aldehyde dehydrogenase 1 family, member L1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10840| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Lee KM, Lan Q, Kricker A, "et al." |title=One-carbon metabolism gene polymorphisms and risk of non-Hodgkin lymphoma in Australia. |journal=Hum. Genet. |volume=122 |issue= 5 |pages= 525–33 |year= |pmid= 17891500 |doi= 10.1007/s00439-007-0431-2
*cite journal | author=Stevens VL, McCullough ML, Pavluck AL, "et al." |title=Association of polymorphisms in one-carbon metabolism genes and postmenopausal breast cancer incidence. |journal=Cancer Epidemiol. Biomarkers Prev. |volume=16 |issue= 6 |pages= 1140–7 |year= 2007 |pmid= 17548676 |doi= 10.1158/1055-9965.EPI-06-1037
*cite journal | author=Lim U, Wang SS, Hartge P, "et al." |title=Gene-nutrient interactions among determinants of folate and one-carbon metabolism on the risk of non-Hodgkin lymphoma: NCI-SEER case-control study. |journal=Blood |volume=109 |issue= 7 |pages= 3050–9 |year= 2007 |pmid= 17119116 |doi= 10.1182/blood-2006-07-034330
*cite journal | author=Oleinik NV, Krupenko SA |title=Ectopic expression of 10-formyltetrahydrofolate dehydrogenase in A549 cells induces G1 cell cycle arrest and apoptosis. |journal=Mol. Cancer Res. |volume=1 |issue= 8 |pages= 577–88 |year= 2004 |pmid= 12805405 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Krupenko SA, Oleinik NV |title=10-formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in tumor tissues and possesses suppressor effects on cancer cells. |journal=Cell Growth Differ. |volume=13 |issue= 5 |pages= 227–36 |year= 2002 |pmid= 12065246 |doi=
*cite journal | author=Hong M, Lee Y, Kim JW, "et al." |title=Isolation and characterization of cDNA clone for human liver 10-formyltetrahydrofolate dehydrogenase. |journal=Biochem. Mol. Biol. Int. |volume=47 |issue= 3 |pages= 407–15 |year= 1999 |pmid= 10204077 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Champion KM, Cook RJ, Tollaksen SL, Giometti CS |title=Identification of a heritable deficiency of the folate-dependent enzyme 10-formyltetrahydrofolate dehydrogenase in mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 24 |pages= 11338–42 |year= 1994 |pmid= 7972060 |doi=
*cite journal | author=Johlin FC, Swain E, Smith C, Tephly TR |title=Studies on the mechanism of methanol poisoning: purification and comparison of rat and human liver 10-formyltetrahydrofolate dehydrogenase. |journal=Mol. Pharmacol. |volume=35 |issue= 6 |pages= 745–50 |year= 1989 |pmid= 2733692 |doi=

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