ACSL1

Acyl-CoA synthetase long-chain family member 1, also known as ACSL1, is a human gene.cite web | title = Entrez Gene: ACSL1 acyl-CoA synthetase long-chain family member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2180| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation.cite web | title = Entrez Gene: ACSL1 acyl-CoA synthetase long-chain family member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2180| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Stanczak H, Stanczak JJ, Singh I |title=Chromosomal localization of the human gene for palmitoyl-CoA ligase (FACL1). |journal=Cytogenet. Cell Genet. |volume=59 |issue= 1 |pages= 17–9 |year= 1992 |pmid= 1531127 |doi=
*cite journal | author=Amigo L, McElroy MC, Morales MN, Bronfman M |title=Subcellular distribution and characteristics of ciprofibroyl-CoA synthetase in rat liver. Its possible identity with long-chain acyl-CoA synthetase. |journal=Biochem. J. |volume=284 ( Pt 1) |issue= |pages= 283–7 |year= 1992 |pmid= 1599407 |doi=
*cite journal | author=Abe T, Fujino T, Fukuyama R, "et al." |title=Human long-chain acyl-CoA synthetase: structure and chromosomal location. |journal=J. Biochem. |volume=111 |issue= 1 |pages= 123–8 |year= 1992 |pmid= 1607358 |doi=
*cite journal | author=Lageweg W, Wanders RJ, Tager JM |title=Long-chain-acyl-CoA synthetase and very-long-chain-acyl-CoA synthetase activities in peroxisomes and microsomes from rat liver. An enzymological study. |journal=Eur. J. Biochem. |volume=196 |issue= 2 |pages= 519–23 |year= 1991 |pmid= 2007410 |doi=
*cite journal | author=Suzuki H, Kawarabayasi Y, Kondo J, "et al." |title=Structure and regulation of rat long-chain acyl-CoA synthetase. |journal=J. Biol. Chem. |volume=265 |issue= 15 |pages= 8681–5 |year= 1990 |pmid= 2341402 |doi=
*cite journal | author=Singh I, Bhushan A, Relan NK, Hashimoto T |title=Acyl-CoA ligases from rat brain microsomes: an immunochemical study. |journal=Biochim. Biophys. Acta |volume=963 |issue= 3 |pages= 509–14 |year= 1989 |pmid= 2973813 |doi=
*cite journal | author=Bierbach H |title=Studies on long chain fatty acid:CoA ligase from human small intestine. |journal=Gut |volume=21 |issue= 8 |pages= 689–94 |year= 1981 |pmid= 7429333 |doi=
*cite journal | author=Cantú ES, Sprinkle TJ, Ghosh B, Singh I |title=The human palmitoyl-CoA ligase (FACL2) gene maps to the chromosome 4q34-q35 region by fluorescence in situ hybridization (FISH) and somatic cell hybrid panels. |journal=Genomics |volume=28 |issue= 3 |pages= 600–2 |year= 1996 |pmid= 7490105 |doi= 10.1006/geno.1995.1199
*cite journal | author=Wu P, Bremer J |title=Activation of alkylthioacrylic acids in subcellular fractions of rat tissues: a new spectrophotometric method for assay of acyl-CoA synthetase. |journal=Biochim. Biophys. Acta |volume=1215 |issue= 1-2 |pages= 87–92 |year= 1994 |pmid= 7948012 |doi=
*cite journal | author=Singh I, Lazo O, Kremser K |title=Purification of peroxisomes and subcellular distribution of enzyme activities for activation and oxidation of very-long-chain fatty acids in rat brain. |journal=Biochim. Biophys. Acta |volume=1170 |issue= 1 |pages= 44–52 |year= 1993 |pmid= 8399326 |doi=
*cite journal | author=Ghosh B, Barbosa E, Singh I |title=Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression. |journal=Mol. Cell. Biochem. |volume=151 |issue= 1 |pages= 77–81 |year= 1996 |pmid= 8584017 |doi=
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Malhotra KT, Malhotra K, Lubin BH, Kuypers FA |title=Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. |journal=Biochem. J. |volume=344 Pt 1 |issue= |pages= 135–43 |year= 2000 |pmid= 10548543 |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=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Mashek DG, Bornfeldt KE, Coleman RA, "et al." |title=Revised nomenclature for the mammalian long-chain acyl-CoA synthetase gene family. |journal=J. Lipid Res. |volume=45 |issue= 10 |pages= 1958–61 |year= 2005 |pmid= 15292367 |doi= 10.1194/jlr.E400002-JLR200
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Soupene E, Kuypers FA |title=Multiple erythroid isoforms of human long-chain acyl-CoA synthetases are produced by switch of the fatty acid gate domains. |journal=BMC Mol. Biol. |volume=7 |issue= |pages= 21 |year= 2006 |pmid= 16834775 |doi= 10.1186/1471-2199-7-21

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