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{{Infobox_gene}}
{{PBB_Controls
'''Long-chain-fatty-acid—CoA ligase 1''' is an [[enzyme]] that in humans is encoded by the ''ACSL1'' [[gene]].<ref name="pmid2341402">{{cite journal | vauthors = Suzuki H, Kawarabayasi Y, Kondo J, Abe T, Nishikawa K, Kimura S, Hashimoto T, Yamamoto T | title = Structure and regulation of rat long-chain acyl-CoA synthetase | journal = The Journal of Biological Chemistry | volume = 265 | issue = 15 | pages = 8681–5 | date = May 1990 | pmid = 2341402 | pmc =  | doi =  }}</ref><ref name="pmid1531127">{{cite journal | vauthors = Stanczak H, Stanczak JJ, Singh I | title = Chromosomal localization of the human gene for palmitoyl-CoA ligase (FACL1) | journal = Cytogenetics and Cell Genetics | volume = 59 | issue = 1 | pages = 17–9 | date = Feb 1992 | pmid = 1531127 | pmc =  | doi = 10.1159/000133189 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ACSL1 acyl-CoA synthetase long-chain family member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2180| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Structure==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Acyl-CoA synthetase long-chain family member 1
| HGNCid = 3569
| Symbol = ACSL1
| AltSymbols =; ACS1; FACL1; FACL2; LACS; LACS1; LACS2
| OMIM = 152425
| ECnumber = 
| Homologene = 37561
| MGIid = 102797
| GeneAtlas_image1 = PBB_GE_ACSL1_201963_at_tn.png
| GeneAtlas_image2 = PBB_GE_ACSL1_207275_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0004467 |text = long-chain-fatty-acid-CoA ligase activity}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005777 |text = peroxisome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006631 |text = fatty acid metabolic process}} {{GNF_GO|id=GO:0007586 |text = digestion}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2180
    | Hs_Ensembl = ENSG00000151726
    | Hs_RefseqProtein = NP_001986
    | Hs_RefseqmRNA = NM_001995
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 185913744
    | Hs_GenLoc_end = 185984209
    | Hs_Uniprot = P33121
    | Mm_EntrezGene = 14081
    | Mm_Ensembl = ENSMUSG00000018796
    | Mm_RefseqmRNA = XM_991183
    | Mm_RefseqProtein = XP_996277
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 47969859
    | Mm_GenLoc_end = 48034867
    | Mm_Uniprot = Q6GTG6
  }}
}}
'''Acyl-CoA synthetase long-chain family member 1''', also known as '''ACSL1''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
===Gene===
{{PBB_Summary
 
| section_title =  
The ACSL4 gene is located on the 4th chromosome, with its specific location being 4q35.1. The gene contains 28 exons.<ref name="entrez" />
| 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.<ref name="entrez">{{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 = }}</ref>
             
}}
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.<ref name="entrez"/>
 
In melanocytic cells ACSL1 gene expression may be regulated by [[Microphthalmia-associated transcription factor|MITF]].<ref name="pmid19067971">{{cite journal | vauthors = Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E | title = Novel MITF targets identified using a two-step DNA microarray strategy | journal = Pigment Cell & Melanoma Research | volume = 21 | issue = 6 | pages = 665–76 | date = Dec 2008 | pmid = 19067971 | doi = 10.1111/j.1755-148X.2008.00505.x }}</ref>
 
==Function==
 
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.<ref name="entrez" />  Several transcript variants encoding different isoforms have been found for this gene. This specific protein is most commonly found in mitochondria and peroxisomes.<ref>{{cite journal | vauthors = 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 = Biochimica et Biophysica Acta | volume = 1170 | issue = 1 | pages = 44–52 | date = Sep 1993 | pmid = 8399326 | doi=10.1016/0005-2760(93)90174-8}}</ref>
 
==Clinical significance==
 
ACSL1 was shown to be involved in nonspecific mental retardation and fatty-acid metabolism.<ref>{{cite journal | vauthors = Meloni I, Muscettola M, Raynaud M, Longo I, Bruttini M, Moizard MP, Gomot M, Chelly J, des Portes V, Fryns JP, Ropers HH, Magi B, Bellan C, Volpi N, Yntema HG, Lewis SE, Schaffer JE, Renieri A | title = FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation | journal = Nature Genetics | volume = 30 | issue = 4 | pages = 436–40 | date = Apr 2002 | pmid = 11889465 | doi = 10.1038/ng857 }}</ref> Since the ACSL4 gene is highly expressed in brain, where it encodes a brain specific isoform, an ASCL1 mutation may be an efficient diagnostic tool in mentally retarded males.<ref>{{cite journal | vauthors = Longo I, Frints SG, Fryns JP, Meloni I, Pescucci C, Ariani F, Borghgraef M, Raynaud M, Marynen P, Schwartz C, Renieri A, Froyen G | title = A third MRX family (MRX68) is the result of mutation in the long chain fatty acid-CoA ligase 4 (FACL4) gene: proposal of a rapid enzymatic assay for screening mentally retarded patients | journal = Journal of Medical Genetics | volume = 40 | issue = 1 | pages = 11–7 | date = Jan 2003 | pmid = 12525535 | doi = 10.1136/jmg.40.1.11 | pmc=1735250}}</ref>
 
==Interactions==
 
ACSL1 expression is regulated by SHP2 activity.<ref>{{cite journal | vauthors = Cooke M, Orlando U, Maloberti P, Podestá EJ, Cornejo Maciel F | title = Tyrosine phosphatase SHP2 regulates the expression of acyl-CoA synthetase ACSL4 | journal = Journal of Lipid Research | volume = 52 | issue = 11 | pages = 1936–48 | date = Nov 2011 | pmid = 21903867 | doi = 10.1194/jlr.m015552 | pmc=3196225}}</ref> Additionally, ACSL4 interacts with [[ACSL3]], [[Amyloid precursor protein|APP]], [[DSE (gene)|DSE]], [[ELAVL1]], [[HECW2]], MINOS1, [[PARK2]], [[SPG20]], [[SUMO2]], [[TP53]], [[TUBGCP3]], [[Ubiquitin C|UBC]], [[Ubiquitin D|UBD]], and [[YWHAQ]].<ref name="entrez"/>


==References==
==References==
{{reflist|2}}
{{reflist|33em}}
==Further reading==
 
{{refbegin | 2}}
==Further reading ==
{{PBB_Further_reading
{{refbegin|33em}}
| citations =
* {{cite journal | vauthors = 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 = The Biochemical Journal | volume = 284 | issue = 1 | pages = 283–7 | date = May 1992 | pmid = 1599407 | pmc = 1132728 | doi =  10.1042/bj2840283}}
*{{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 | vauthors = Abe T, Fujino T, Fukuyama R, Minoshima S, Shimizu N, Toh H, Suzuki H, Yamamoto T | title = Human long-chain acyl-CoA synthetase: structure and chromosomal location | journal = Journal of Biochemistry | volume = 111 | issue = 1 | pages = 123–8 | date = Jan 1992 | pmid = 1607358 | 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 | vauthors = 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 = European Journal of Biochemistry / FEBS | volume = 196 | issue = 2 | pages = 519–23 | date = Mar 1991 | pmid = 2007410 | doi = 10.1111/j.1432-1033.1991.tb15844.x }}
*{{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 | vauthors = Singh I, Bhushan A, Relan NK, Hashimoto T | title = Acyl-CoA ligases from rat brain microsomes: an immunochemical study | journal = Biochimica et Biophysica Acta | volume = 963 | issue = 3 | pages = 509–14 | date = Dec 1988 | pmid = 2973813 | doi = 10.1016/0005-2760(88)90319-0 }}
*{{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 | vauthors = Bierbach H | title = Studies on long chain fatty acid:CoA ligase from human small intestine | journal = Gut | volume = 21 | issue = 8 | pages = 689–94 | date = Aug 1980 | pmid = 7429333 | pmc = 1419104 | doi = 10.1136/gut.21.8.689 }}
*{{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 | vauthors = 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 | date = Aug 1995 | pmid = 7490105 | doi = 10.1006/geno.1995.1199 }}
*{{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 | vauthors = 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 = Biochimica et Biophysica Acta | volume = 1215 | issue = 1–2 | pages = 87–92 | date = Nov 1994 | pmid = 7948012 | doi = 10.1016/0005-2760(94)90095-7 }}
*{{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 | vauthors = 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 = Biochimica et Biophysica Acta | volume = 1170 | issue = 1 | pages = 44–52 | date = Sep 1993 | pmid = 8399326 | doi = 10.1016/0005-2760(93)90174-8 }}
*{{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 | vauthors = Ghosh B, Barbosa E, Singh I | title = Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression | journal = Molecular and Cellular Biochemistry | volume = 151 | issue = 1 | pages = 77–81 | date = Oct 1995 | pmid = 8584017 | doi = 10.1007/BF01076899 }}
*{{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 | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = Sep 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{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 | vauthors = Malhotra KT, Malhotra K, Lubin BH, Kuypers FA | title = Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors | journal = The Biochemical Journal | volume = 344 | issue = 1 | pages = 135–43 | date = Nov 1999 | pmid = 10548543 | pmc = 1220623 | doi = 10.1042/0264-6021:3440135 }}
*{{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 | vauthors = Mashek DG, Bornfeldt KE, Coleman RA, Berger J, Bernlohr DA, Black P, DiRusso CC, Farber SA, Guo W, Hashimoto N, Khodiyar V, Kuypers FA, Maltais LJ, Nebert DW, Renieri A, Schaffer JE, Stahl A, Watkins PA, Vasiliou V, Yamamoto TT | title = Revised nomenclature for the mammalian long-chain acyl-CoA synthetase gene family | journal = Journal of Lipid Research | volume = 45 | issue = 10 | pages = 1958–61 | date = Oct 2004 | pmid = 15292367 | doi = 10.1194/jlr.E400002-JLR200 }}
*{{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 | vauthors = 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 Molecular Biology | volume = 7 | pages = 21 | year = 2006 | pmid = 16834775 | pmc = 1543647 | doi = 10.1186/1471-2199-7-21 }}
*{{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 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC gene info|ACSL1}}
 
{{Portal|Mitochondria}}
 
[[Category:Human proteins]]
 
 
{{gene-4-stub}}

Latest revision as of 17:45, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Long-chain-fatty-acid—CoA ligase 1 is an enzyme that in humans is encoded by the ACSL1 gene.[1][2][3]

Structure

Gene

The ACSL4 gene is located on the 4th chromosome, with its specific location being 4q35.1. The gene contains 28 exons.[3]

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.[3]

In melanocytic cells ACSL1 gene expression may be regulated by MITF.[4]

Function

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.[3] Several transcript variants encoding different isoforms have been found for this gene. This specific protein is most commonly found in mitochondria and peroxisomes.[5]

Clinical significance

ACSL1 was shown to be involved in nonspecific mental retardation and fatty-acid metabolism.[6] Since the ACSL4 gene is highly expressed in brain, where it encodes a brain specific isoform, an ASCL1 mutation may be an efficient diagnostic tool in mentally retarded males.[7]

Interactions

ACSL1 expression is regulated by SHP2 activity.[8] Additionally, ACSL4 interacts with ACSL3, APP, DSE, ELAVL1, HECW2, MINOS1, PARK2, SPG20, SUMO2, TP53, TUBGCP3, UBC, UBD, and YWHAQ.[3]

References

  1. ↑ Suzuki H, Kawarabayasi Y, Kondo J, Abe T, Nishikawa K, Kimura S, Hashimoto T, Yamamoto T (May 1990). "Structure and regulation of rat long-chain acyl-CoA synthetase". The Journal of Biological Chemistry. 265 (15): 8681–5. PMID 2341402.
  2. ↑ Stanczak H, Stanczak JJ, Singh I (Feb 1992). "Chromosomal localization of the human gene for palmitoyl-CoA ligase (FACL1)". Cytogenetics and Cell Genetics. 59 (1): 17–9. doi:10.1159/000133189. PMID 1531127.
  3. ↑ 3.0 3.1 3.2 3.3 3.4 "Entrez Gene: ACSL1 acyl-CoA synthetase long-chain family member 1".
  4. ↑ Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E (Dec 2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell & Melanoma Research. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
  5. ↑ Singh I, Lazo O, Kremser K (Sep 1993). "Purification of peroxisomes and subcellular distribution of enzyme activities for activation and oxidation of very-long-chain fatty acids in rat brain". Biochimica et Biophysica Acta. 1170 (1): 44–52. doi:10.1016/0005-2760(93)90174-8. PMID 8399326.
  6. ↑ Meloni I, Muscettola M, Raynaud M, Longo I, Bruttini M, Moizard MP, Gomot M, Chelly J, des Portes V, Fryns JP, Ropers HH, Magi B, Bellan C, Volpi N, Yntema HG, Lewis SE, Schaffer JE, Renieri A (Apr 2002). "FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation". Nature Genetics. 30 (4): 436–40. doi:10.1038/ng857. PMID 11889465.
  7. ↑ Longo I, Frints SG, Fryns JP, Meloni I, Pescucci C, Ariani F, Borghgraef M, Raynaud M, Marynen P, Schwartz C, Renieri A, Froyen G (Jan 2003). "A third MRX family (MRX68) is the result of mutation in the long chain fatty acid-CoA ligase 4 (FACL4) gene: proposal of a rapid enzymatic assay for screening mentally retarded patients". Journal of Medical Genetics. 40 (1): 11–7. doi:10.1136/jmg.40.1.11. PMC 1735250. PMID 12525535.
  8. ↑ Cooke M, Orlando U, Maloberti P, Podestá EJ, Cornejo Maciel F (Nov 2011). "Tyrosine phosphatase SHP2 regulates the expression of acyl-CoA synthetase ACSL4". Journal of Lipid Research. 52 (11): 1936–48. doi:10.1194/jlr.m015552. PMC 3196225. PMID 21903867.

Further reading

External links


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