ACOT8

Acyl-CoA thioesterase 8, also known as ACOT8, is a human gene.cite web | title = Entrez Gene: ACOT8 acyl-CoA thioesterase 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10005| accessdate = ]

PBB_Summary
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summary_text = The protein encoded by this gene is a peroxisomal thioesterase that appears to be involved more in the oxidation of fatty acids rather than in their formation. The encoded protein can bind to the human immunodeficiency virus-1 protein Nef, and mediate Nef-induced down-regulation of CD4 in T-cells. Multiple transcript variants encoding several different isoforms have been found for this gene.cite web | title = Entrez Gene: ACOT8 acyl-CoA thioesterase 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10005| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Hunt MC, Alexson SE |title=The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. |journal=Prog. Lipid Res. |volume=41 |issue= 2 |pages= 99–130 |year= 2002 |pmid= 11755680 |doi=
*cite journal | author=Liu LX, Margottin F, Le Gall S, "et al." |title=Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. |journal=J. Biol. Chem. |volume=272 |issue= 21 |pages= 13779–85 |year= 1997 |pmid= 9153233 |doi=
*cite journal | author=Watanabe H, Shiratori T, Shoji H, "et al." |title=A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. |journal=Biochem. Biophys. Res. Commun. |volume=238 |issue= 1 |pages= 234–9 |year= 1997 |pmid= 9299485 |doi= 10.1006/bbrc.1997.7217
*cite journal | author=Jones JM, Nau K, Geraghty MT, "et al." |title=Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9216–23 |year= 1999 |pmid= 10092594 |doi=
*cite journal | author=Liu LX, Heveker N, Fackler OT, "et al." |title=Mutation of a conserved residue (D123) required for oligomerization of human immunodeficiency virus type 1 Nef protein abolishes interaction with human thioesterase and results in impairment of Nef biological functions. |journal=J. Virol. |volume=74 |issue= 11 |pages= 5310–9 |year= 2000 |pmid= 10799608 |doi=
*cite journal | author=Cohen GB, Rangan VS, Chen BK, "et al." |title=The human thioesterase II protein binds to a site on HIV-1 Nef critical for CD4 down-regulation. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 23097–105 |year= 2000 |pmid= 10807905 |doi= 10.1074/jbc.M000536200
*cite journal | author=Jones JM, Gould SJ |title=Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. |journal=Biochem. Biophys. Res. Commun. |volume=275 |issue= 1 |pages= 233–40 |year= 2000 |pmid= 10944470 |doi= 10.1006/bbrc.2000.3285
*cite journal | author=Fossey SC, Mychaleckyj JC, Pendleton JK, "et al." |title=A high-resolution 6.0-megabase transcript map of the type 2 diabetes susceptibility region on human chromosome 20. |journal=Genomics |volume=76 |issue= 1-3 |pages= 45–57 |year= 2001 |pmid= 11549316 |doi= 10.1006/geno.2001.6584
*cite journal | author=Deloukas P, Matthews LH, Ashurst J, "et al." |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a
*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=Ishizuka M, Toyama Y, Watanabe H, "et al." |title=Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis. |journal=Exp. Cell Res. |volume=297 |issue= 1 |pages= 127–41 |year= 2004 |pmid= 15194431 |doi= 10.1016/j.yexcr.2004.02.029
*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=Hunt MC, Yamada J, Maltais LJ, "et al." |title=A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases. |journal=J. Lipid Res. |volume=46 |issue= 9 |pages= 2029–32 |year= 2005 |pmid= 16103133 |doi= 10.1194/jlr.E500003-JLR200
*cite journal | author=Westin MA, Hunt MC, Alexson SE |title=The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes. |journal=J. Biol. Chem. |volume=280 |issue= 46 |pages= 38125–32 |year= 2006 |pmid= 16141203 |doi= 10.1074/jbc.M508479200
*cite journal | author=Takagi M, Suto F, Suga T, Yamada J |title=Sterol Regulatory Element-Binding Protein-2 modulates human brain acyl-CoA hydrolase gene transcription. |journal=Mol. Cell. Biochem. |volume=275 |issue= 1-2 |pages= 199–206 |year= 2006 |pmid= 16335799 |doi=
*cite journal | author=Hunt MC, Rautanen A, Westin MA, "et al." |title=Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. |journal=FASEB J. |volume=20 |issue= 11 |pages= 1855–64 |year= 2006 |pmid= 16940157 |doi= 10.1096/fj.06-6042com
*cite journal | author=Yamaori S, Ukena E, Fujiyama N, "et al." |title=Nafamostat is hydrolysed by human liver cytosolic long-chain acyl-CoA hydrolase. |journal=Xenobiotica |volume=37 |issue= 3 |pages= 260–70 |year= 2007 |pmid= 17624024 |doi=

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