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Med."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0425","doi-asserted-by":"crossref","first-page":"32044","DOI":"10.1074\/jbc.M114.585547","article-title":"The endoplasmic reticulum-based acetyltransferases, ATase1 and ATase2, associate with the oligosaccharyltransferase to acetylate correctly folded polypeptides","volume":"289","author":"Ding","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0430","first-page":"11","article-title":"Novel direct assay for acetyl-CoA: alpha-glucosaminide N-acetyltransferase using BODIPY-glucosamine as a substrate","volume":"28","author":"Choi","year":"2015","journal-title":"JIMD Rep."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0435","doi-asserted-by":"crossref","first-page":"1544","DOI":"10.1172\/JCI109614","article-title":"Inhibition by propionyl-coenzyme A of N-acetylglutamate synthetase in rat liver mitochondria. 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Res."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0450","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1042\/bj2160233","article-title":"Inhibition of ureagenesis by valproate in rat hepatocytes. Role of N-acetylglutamate and acetyl-CoA","volume":"216","author":"Coude","year":"1983","journal-title":"Biochem. J."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0455","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/0304-4165(83)90356-2","article-title":"Role of N-acetylglutamate and acetyl-CoA in the inhibition of ureagenesis by isovaleric acid in isolated rat hepatocytes","volume":"761","author":"Coude","year":"1983","journal-title":"Biochim. Biophys. 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Microbiol."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0500","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1038\/33185","article-title":"Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4alpha","volume":"392","author":"Hertz","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.ymgme.2019.05.002_bb0505","doi-asserted-by":"crossref","first-page":"24451","DOI":"10.1074\/jbc.M500732200","article-title":"Thioesterase activity and acyl-CoA\/fatty acid cross-talk of hepatocyte nuclear factor-4{alpha}","volume":"280","author":"Hertz","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0510","doi-asserted-by":"crossref","first-page":"2354","DOI":"10.1194\/jlr.M035436","article-title":"Divergence between human and murine peroxisome proliferator-activated receptor alpha ligand specificities","volume":"54","author":"Oswal","year":"2013","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0515","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1194\/jlr.M072447","article-title":"Fatty acid binding profile of the liver X receptor alpha","volume":"58","author":"Bedi","year":"2017","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0520","first-page":"83","article-title":"Metabolic interplay between peroxisomes and other subcellular organelles including mitochondria and the endoplasmic reticulum","volume":"3","author":"Wanders","year":"2015","journal-title":"Front. Cell. Dev. Biol."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0525","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1172\/JCI108764","article-title":"A possible role for malonyl-CoA in the regulation of hepatic fatty acid oxidation and ketogenesis","volume":"60","author":"McGarry","year":"1977","journal-title":"J. Clin. Invest."},{"issue":"Suppl. 3","key":"10.1016\/j.ymgme.2019.05.002_bb0530","doi-asserted-by":"crossref","first-page":"S405","DOI":"10.2337\/diabetes.51.2007.S405","article-title":"Malonyl-CoA signaling, lipid partitioning, and glucolipotoxicity: role in beta-cell adaptation and failure in the etiology of diabetes","volume":"51","author":"Prentki","year":"2002","journal-title":"Diabetes"},{"key":"10.1016\/j.ymgme.2019.05.002_bb0535","doi-asserted-by":"crossref","first-page":"12624","DOI":"10.1073\/pnas.1834402100","article-title":"Hypothalamic malonyl-CoA as a mediator of feeding behavior","volume":"100","author":"Hu","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0540","doi-asserted-by":"crossref","first-page":"17075","DOI":"10.1073\/pnas.0707060104","article-title":"Mitochondrial dysfunction due to long-chain Acyl-CoA dehydrogenase deficiency causes hepatic steatosis and hepatic insulin resistance","volume":"104","author":"Zhang","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0545","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1002\/biof.5520180212","article-title":"The clinical use of HMG CoA-reductase inhibitors and the associated depletion of coenzyme Q10. 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Res."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0555","doi-asserted-by":"crossref","first-page":"2248","DOI":"10.1161\/01.CIR.100.22.2248","article-title":"Arrhythmias and conduction defects as presenting symptoms of fatty acid oxidation disorders in children","volume":"100","author":"Bonnet","year":"1999","journal-title":"Circulation"},{"key":"10.1016\/j.ymgme.2019.05.002_bb0560","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1023\/A:1025106909213","article-title":"Diffusion-weighted imaging in the assessment of neurological damage in patients with methylmalonic aciduria","volume":"26","author":"Burlina","year":"2003","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0565","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1007\/s10545-014-9730-7","article-title":"A detailed analysis of methylmalonic acid kinetics during hemodialysis and after combined liver\/kidney transplantation in a patient with mut (0) methylmalonic acidemia","volume":"37","author":"Vernon","year":"2014","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0570","series-title":"GeneReviews((R))","article-title":"Isolated methylmalonic acidemia","author":"Manoli","year":"1993"},{"key":"10.1016\/j.ymgme.2019.05.002_bb0575","doi-asserted-by":"crossref","first-page":"1054","DOI":"10.1002\/mds.25538","article-title":"A treatable new cause of chorea: beta-ketothiolase deficiency","volume":"28","author":"Buhas","year":"2013","journal-title":"Mov. Disord."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0580","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1007\/s10545-011-9289-5","article-title":"Diagnosis and management of glutaric aciduria type I--revised recommendations","volume":"34","author":"Kolker","year":"2011","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0585","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/s10545-016-9999-9","article-title":"Proposed recommendations for diagnosing and managing individuals with glutaric aciduria type I: second revision","volume":"40","author":"Boy","year":"2017","journal-title":"J. Inherit. Metab. 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Res."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0630","doi-asserted-by":"crossref","first-page":"e23","DOI":"10.1371\/journal.pgen.0010023","article-title":"Medium-chain acyl-CoA dehydrogenase deficiency in gene-targeted mice","volume":"1","author":"Tolwani","year":"2005","journal-title":"PLoS Genet."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0635","doi-asserted-by":"crossref","first-page":"2069","DOI":"10.1093\/hmg\/10.19.2069","article-title":"Gestational, pathologic and biochemical differences between very long-chain acyl-CoA dehydrogenase deficiency and long-chain acyl-CoA dehydrogenase deficiency in the mouse","volume":"10","author":"Cox","year":"2001","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0640","doi-asserted-by":"crossref","first-page":"1403","DOI":"10.1172\/JCI12590","article-title":"Lack of mitochondrial trifunctional protein in mice causes neonatal hypoglycemia and sudden death","volume":"107","author":"Ibdah","year":"2001","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0645","first-page":"271","article-title":"Screen for abnormal mitochondrial phenotypes in mouse embryonic stem cells identifies a model for succinyl-CoA ligase deficiency and mtDNA depletion","volume":"7","author":"Donti","year":"2014","journal-title":"Dis. Model. Mech."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0650","doi-asserted-by":"crossref","first-page":"52909","DOI":"10.1074\/jbc.M310533200","article-title":"A knock-out mouse model for methylmalonic aciduria resulting in neonatal lethality","volume":"278","author":"Peters","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0655","doi-asserted-by":"crossref","first-page":"35995","DOI":"10.1074\/jbc.M105467200","article-title":"Fatal propionic acidemia in mice lacking propionyl-CoA carboxylase and its rescue by postnatal, liver-specific supplementation via a transgene","volume":"276","author":"Miyazaki","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0660","doi-asserted-by":"crossref","first-page":"1316","DOI":"10.1038\/mt.2013.68","article-title":"Generation of a hypomorphic model of propionic acidemia amenable to gene therapy testing","volume":"21","author":"Guenzel","year":"2013","journal-title":"Mol. Ther."},{"key":"10.1016\/j.ymgme.2019.05.002_bb0665","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1089\/hum.2010.008","article-title":"Liver-directed recombinant adeno-associated viral gene delivery rescues a lethal mouse model of methylmalonic acidemia and provides long-term phenotypic correction","volume":"21","author":"Carrillo-Carrasco","year":"2010","journal-title":"Hum. 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