Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
1 to 25 of 39  Show
  1. 1
    "Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family."
    Zhang J., Zhang W., Zou D., Chen G., Wan T., Zhang M., Cao X.
    Biochem. Biophys. Res. Commun. 297:1033-1042(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY.
    Category: Expression, Sequences.
    Tissue: Dendritic cell.
    Source: UniProtKB/Swiss-Prot (reviewed).
  2. 2
    "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 12928 other entries.

  3. 3
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  4. 4
    "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Category: Sequences.
    Tissue: Lung and Uterus.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 50459 other entries.

  5. 5
    "A new genetic disorder in mitochondrial fatty acid beta-oxidation: ACAD9 deficiency."
    He M., Rutledge S.L., Kelly D.R., Palmer C.A., Murdoch G., Majumder N., Nicholls R.D., Pei Z., Watkins P.A., Vockley J.
    Am. J. Hum. Genet. 81:87-103(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ACAD9 DEFICIENCY.
    Category: Pathology & Biotech.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is mapped to 4 other entries.

  6. 6
    "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3138 other entries.

  7. 7
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NDUFAF1 AND ECSIT, INVOLVEMENT IN ACAD9 DEFICIENCY, VARIANTS ACAD9 DEFICIENCY LYS-413 AND HIS-518.
    Category: Function, Subcellular Location, Pathology & Biotech, Interaction, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 and mapped to 4 other entries.

  8. 8
    Cited for: INVOLVEMENT IN ACAD9 DEFICIENCY, VARIANTS ACAD9 DEFICIENCY ILE-44; TRP-193; PHE-234; GLN-266; SER-303; THR-326; CYS-417 AND TRP-532.
    Category: Pathology & Biotech, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 and mapped to 4 other entries.

  9. 9
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 18268 other entries.

  10. 10
    "ACAD9, a complex I assembly factor with a moonlighting function in fatty acid oxidation deficiencies."
    Nouws J., Te Brinke H., Nijtmans L.G., Houten S.M.
    Hum. Mol. Genet. 23:1311-1319(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-426.
    Category: Function, Pathology & Biotech.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is mapped to 4 other entries.

  11. 11
    "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: Sequences.
    Tissue: Liver.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 11670 other entries.

  12. 12
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 6426 other entries.

  13. 13
    "Riboflavin-responsive oxidative phosphorylation complex I deficiency caused by defective ACAD9: new function for an old gene."
    Gerards M., van den Bosch B.J., Danhauser K., Serre V., van Weeghel M., Wanders R.J., Nicolaes G.A., Sluiter W., Schoonderwoerd K., Scholte H.R., Prokisch H., Rotig A., de Coo I.F., Smeets H.J.
    Brain 134:210-219(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ACAD9 DEFICIENCY LYS-127; TRP-469 AND TRP-532.
    Category: Pathology & Biotech, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is mapped to 4 other entries.

  14. 14
    Category: Pathology & Biotech, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4 other entries.

  15. 15
    Cited for: VARIANT ACAD9 DEFICIENCY CYS-414.
    Category: Pathology & Biotech, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  16. 16
    "A patient with complex I deficiency caused by a novel ACAD9 mutation not responding to riboflavin treatment."
    Nouws J., Wibrand F., van den Brand M., Venselaar H., Duno M., Lund A.M., Trautner S., Nijtmans L., Ostergard E.
    JIMD Rep. 12:37-45(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ACAD9 DEFICIENCY VAL-220.
    Category: Pathology & Biotech, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  17. 17
    Category: Pathology & Biotech, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 17 other entries.

  18. 18
    "High activity of fatty acid oxidation enzymes in human placenta: implications for fetal-maternal disease."
    Oey N.A., den Boer M.E., Ruiter J.P., Wanders R.J., Duran M., Waterham H.R., Boer K., van der Post J.A., Wijburg F.A.
    J. Inherit. Metab. Dis. 26:385-392(2003) [PubMed] [Europe PMC] [Abstract]
    Annotation: Very high activity of CPT2 and VCLAD involved in the metabolism of long-chain fatty acids. Fatty acid oxidation may play role in energy generation in placenta and deficiency in may result in placental dysfunction and gestational complications.Imported.
    Source: GeneRIF:28976.

    This publication is mapped to 9 other entries.

  19. 19
    "Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids."
    Ensenauer R., He M., Willard J.M., Goetzman E.S., Corydon T.J., Vandahl B.B., Mohsen A.W., Isaya G., Vockley J.
    J. Biol. Chem. 280:32309-32316(2005) [PubMed] [Europe PMC] [Abstract]
    Category: Subcellular Location.
    Annotation: ACAD9 may play a role in the turnover of lipid membrane unsaturated fatty acids that are essential for membrane integrity and structureImported.
    Source: GeneRIF:28976.

    This publication is mapped to 5 other entries.

  20. 20
    "Acyl-CoA dehydrogenase 9 (ACAD 9) is the long-chain acyl-CoA dehydrogenase in human embryonic and fetal brain."
    Oey N.A., Ruiter J.P., Ijlst L., Attie-Bitach T., Vekemans M., Wanders R.J., Wijburg F.A.
    Biochem. Biophys. Res. Commun. 346:33-37(2006) [PubMed] [Europe PMC] [Abstract]
    Category: Expression.
    Annotation: acyl-CoA dehydrogenase 9 (ACAD 9)was identified as the long-chain ACAD in human embryonic and fetal brain and central nervous tissue using in situ hybridization as well as enzymatic studiesImported.
    Source: GeneRIF:28976.

    This publication is mapped to 5 other entries.

  21. 21
    "Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns."
    Szafranski K., Schindler S., Taudien S., Hiller M., Huse K., Jahn N., Schreiber S., Backofen R., Platzer M.
    Genome Biol. 8:R154-R154(2007) [PubMed] [Europe PMC] [Abstract]
    Category: Sequences.
    Annotation: Validated occurrence of an unusual TG 3' splice site in intron 10.Imported.
    Source: GeneRIF:28976.

    This publication is mapped to 240 other entries.

  22. 22
    "Carnitine palmitoyltransferase I and Acyl-CoA dehydrogenase 9 in retina: insights of retinopathy in mitochondrial trifunctional protein defects."
    Roomets E., Kivela T., Tyni T.
    Invest. Ophthalmol. Vis. Sci. 49:1660-1664(2008) [PubMed] [Europe PMC] [Abstract]
    Category: Expression.
    Annotation: Accumulation of 3-hydroxylated intermediates of long-chain fatty acids may contribute to the pathogenesis of retinopathy in MTP deficiencies.Imported.
    Source: GeneRIF:28976.

    This publication is mapped to 20 other entries.

  23. 23
    "Defining the human deubiquitinating enzyme interaction landscape."
    Sowa M.E., Bennett E.J., Gygi S.P., Harper J.W.
    Cell 138:389-403(2009) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:Q9H845.

    This publication is mapped to 1015 other entries.

  24. 24
    "Quantitative nanoproteomics for protein complexes (QNanoPX) related to estrogen transcriptional action."
    Cheng P.C., Chang H.K., Chen S.H.
    Mol. Cell Proteomics 9:209-224(2010) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:Q9H845.

    This publication is mapped to 228 other entries.

  25. 25
    "A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome."
    Richter R., Rorbach J., Pajak A., Smith P.M., Wessels H.J., Huynen M.A., Smeitink J.A., Lightowlers R.N., Chrzanowska-Lightowlers Z.M.
    EMBO J. 29:1116-1125(2010) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:Q9H845.

    This publication is cited by 1 and mapped to 230 other entries.

1 to 25 of 39  Show
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again