| Immunodeficiency with susceptibility to lymphoma with complex genotype affecting energy metabolism (FBP1, ACAD9) and vesicle trafficking (RAB27A). | Immunodeficiency with susceptibility to lymphoma with complex genotype affecting energy metabolism (FBP1, ACAD9) and vesicle trafficking (RAB27A).
Brauer N, Maruta Y, Lisci M, Strege K, Oschlies I, Nakamura H, Böhm S, Lehmberg K, Brandhoff L, Ehl S, Parvaneh N, Klapper W, Fukuda M, Griffiths GM, Hennies HC, Niehues T, Ammann S., Free PMC Article | 07/5/2023 |
| Mutations in the ND6, NDUFV1 or ACAD9 genes are responsible for the mitochondrial complex I deficiency. | Evaluation of mitochondrial bioenergetics, dynamics, endoplasmic reticulum-mitochondria crosstalk, and reactive oxygen species in fibroblasts from patients with complex I deficiency.
Leipnitz G, Mohsen AW, Karunanidhi A, Seminotti B, Roginskaya VY, Markantone DM, Grings M, Mihalik SJ, Wipf P, Van Houten B, Vockley J., Free PMC Article | 11/24/2018 |
| Study identified new mutations in ACAD9 responsible for a wide spectrum of heart diseases in the presence of elevated serum lactate levels. | Evidence of a wide spectrum of cardiac involvement due to ACAD9 mutations: Report on nine patients.
Dewulf JP, Barrea C, Vincent MF, De Laet C, Van Coster R, Seneca S, Marie S, Nassogne MC. | 09/2/2017 |
| ACAD9 mutation is the most frequent cause of cardiac hypertrophy and isolated complex I deficiency. | High incidence and variable clinical outcome of cardiac hypertrophy due to ACAD9 mutations in childhood.
Collet M, Assouline Z, Bonnet D, Rio M, Iserin F, Sidi D, Goldenberg A, Lardennois C, Metodiev MD, Haberberger B, Haack T, Munnich A, Prokisch H, Rötig A., Free PMC Article | 07/29/2017 |
| Case Report: neonatal multiorgan failure due to ACAD9 mutation and complex I deficiency with mitochondrial hyperplasia in liver, cardiac myocytes, skeletal muscle, and renal tubules. | Neonatal multiorgan failure due to ACAD9 mutation and complex I deficiency with mitochondrial hyperplasia in liver, cardiac myocytes, skeletal muscle, and renal tubules.
Leslie N, Wang X, Peng Y, Valencia CA, Khuchua Z, Hata J, Witte D, Huang T, Bove KE. | 06/11/2016 |
| In cells where it is strongly expressed, ACAD9 plays a physiological role in fatty acid oxidation. | Complex I assembly function and fatty acid oxidation enzyme activity of ACAD9 both contribute to disease severity in ACAD9 deficiency.
Schiff M, Haberberger B, Xia C, Mohsen AW, Goetzman ES, Wang Y, Uppala R, Zhang Y, Karunanidhi A, Prabhu D, Alharbi H, Prochownik EV, Haack T, Häberle J, Munnich A, Rötig A, Taylor RW, Nicholls RD, Kim JJ, Prokisch H, Vockley J., Free PMC Article | 02/20/2016 |
| Our results underscore the importance of the ACAD9 protein in complex I assembly and suggest that the enzymatic activity is a rudiment of the duplication event. | ACAD9, a complex I assembly factor with a moonlighting function in fatty acid oxidation deficiencies.
Nouws J, Te Brinke H, Nijtmans LG, Houten SM. | 10/18/2014 |
| Strong candidate gene for mitochondrial disease, based on recessive mutations detected in infantile patients | Molecular diagnosis of infantile mitochondrial disease with targeted next-generation sequencing.
Calvo SE, Compton AG, Hershman SG, Lim SC, Lieber DS, Tucker EJ, Laskowski A, Garone C, Liu S, Jaffe DB, Christodoulou J, Fletcher JM, Bruno DL, Goldblatt J, Dimauro S, Thorburn DR, Mootha VK., Free PMC Article | 10/10/2012 |
| Our data support a new function for ACAD9 in complex I function, making this gene an important new candidate for patients with complex I deficiency, which could be improved by riboflavin treatment. | Riboflavin-responsive oxidative phosphorylation complex I deficiency caused by defective ACAD9: new function for an old gene.
Gerards M, van den Bosch BJ, Danhauser K, Serre V, van Weeghel M, Wanders RJ, Nicolaes GA, Sluiter W, Schoonderwoerd K, Scholte HR, Prokisch H, Rötig A, de Coo IF, Smeets HJ. | 01/22/2011 |
| ACAD9 screening of 120 additional complex I-defective index cases led us to identify two additional unrelated cases and a total of five pathogenic ACAD9 alleles. | Exome sequencing identifies ACAD9 mutations as a cause of complex I deficiency.
Haack TB, Danhauser K, Haberberger B, Hoser J, Strecker V, Boehm D, Uziel G, Lamantea E, Invernizzi F, Poulton J, Rolinski B, Iuso A, Biskup S, Schmidt T, Mewes HW, Wittig I, Meitinger T, Zeviani M, Prokisch H. | 01/1/2011 |
| Observational study of gene-disease association. (HuGE Navigator) | Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O'Brien SJ., Free PMC Article | 12/5/2010 |
| Data show that two closely related metabolic enzymes, ACAD9 and VLCAD, diverged at the root of the vertebrate lineage to function in two separate mitochondrial metabolic pathways and have clinical implications for the diagnosis of complex I deficiency. | Acyl-CoA dehydrogenase 9 is required for the biogenesis of oxidative phosphorylation complex I.
Nouws J, Nijtmans L, Houten SM, van den Brand M, Huynen M, Venselaar H, Hoefs S, Gloerich J, Kronick J, Hutchin T, Willems P, Rodenburg R, Wanders R, van den Heuvel L, Smeitink J, Vogel RO. | 11/6/2010 |
| Validated occurrence of an unusual TG 3' splice site in intron 10. | 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., Free PMC Article | 05/18/2009 |
| Accumulation of 3-hydroxylated intermediates of long-chain fatty acids may contribute to the pathogenesis of retinopathy in MTP deficiencies. | Carnitine palmitoyltransferase I and Acyl-CoA dehydrogenase 9 in retina: insights of retinopathy in mitochondrial trifunctional protein defects.
Roomets E, Kivelä T, Tyni T. | 01/21/2010 |
| We now report three cases of ACAD9 deficiency. | A new genetic disorder in mitochondrial fatty acid beta-oxidation: ACAD9 deficiency.
He M, Rutledge SL, Kelly DR, Palmer CA, Murdoch G, Majumder N, Nicholls RD, Pei Z, Watkins PA, Vockley J., Free PMC Article | 01/21/2010 |
| ACAD9 may play a role in the turnover of lipid membrane unsaturated fatty acids that are essential for membrane integrity and structure | Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids.
Ensenauer R, He M, Willard JM, Goetzman ES, Corydon TJ, Vandahl BB, Mohsen AW, Isaya G, Vockley J. | 01/21/2010 |
| 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 studies | Acyl-CoA dehydrogenase 9 (ACAD 9) is the long-chain acyl-CoA dehydrogenase in human embryonic and fetal brain.
Oey NA, Ruiter JP, Ijlst L, Attie-Bitach T, Vekemans M, Wanders RJ, Wijburg FA. | 01/21/2010 |
| 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. | High activity of fatty acid oxidation enzymes in human placenta: implications for fetal-maternal disease.
Oey NA, den Boer ME, Ruiter JP, Wanders RJ, Duran M, Waterham HR, Boer K, van der Post JA, Wijburg FA. | 01/21/2010 |