ACAD9

ACAD9

Acyl-Coenzyme A dehydrogenase family, member 9, also known as ACAD9, is a human gene.cite web | title = Entrez Gene: ACAD9 acyl-Coenzyme A dehydrogenase family, member 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=28976| accessdate = ]

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References

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*cite journal | author=Szafranski K, Schindler S, Taudien S, "et al." |title=Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns. |journal=Genome Biol. |volume=8 |issue= 8 |pages= R154 |year= 2008 |pmid= 17672918 |doi= 10.1186/gb-2007-8-8-r154
*cite journal | author=He M, Rutledge SL, Kelly DR, "et al." |title=A new genetic disorder in mitochondrial fatty acid beta-oxidation: ACAD9 deficiency. |journal=Am. J. Hum. Genet. |volume=81 |issue= 1 |pages= 87–103 |year= 2007 |pmid= 17564966 |doi= 10.1086/519219
*cite journal | author=Oey NA, Ruiter JP, Ijlst L, "et al." |title=Acyl-CoA dehydrogenase 9 (ACAD 9) is the long-chain acyl-CoA dehydrogenase in human embryonic and fetal brain. |journal=Biochem. Biophys. Res. Commun. |volume=346 |issue= 1 |pages= 33–7 |year= 2006 |pmid= 16750164 |doi= 10.1016/j.bbrc.2006.05.088
*cite journal | author=Ensenauer R, He M, Willard JM, "et al." |title=Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids. |journal=J. Biol. Chem. |volume=280 |issue= 37 |pages= 32309–16 |year= 2005 |pmid= 16020546 |doi= 10.1074/jbc.M504460200
*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=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=Oey NA, den Boer ME, Ruiter JP, "et al." |title=High activity of fatty acid oxidation enzymes in human placenta: implications for fetal-maternal disease. |journal=J. Inherit. Metab. Dis. |volume=26 |issue= 4 |pages= 385–92 |year= 2004 |pmid= 12971426 |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=Zhang J, Zhang W, Zou D, "et al." |title=Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family. |journal=Biochem. Biophys. Res. Commun. |volume=297 |issue= 4 |pages= 1033–42 |year= 2002 |pmid= 12359260 |doi=

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  • Acyl CoA dehydrogenase — is the enzyme used to catalyze the first step of β oxidation in Fatty acid metabolism. ReactionThe following reaction is the oxidation of the fatty acid by FAD.The enzyme catalyzes the formation of a double bond between the C 2 and C 3. The end… …   Wikipedia

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