Primary Literature
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- Mancini C, et al. (2015) An atypical form of AOA2 with myoclonus associated with mutations in SETX and AFG3L2. BMC Med Genet 16:16 PMID: 25927548
- Botelho SC, et al. (2013) Dislocation by the m-AAA protease increases the threshold hydrophobicity for retention of transmembrane helices in the inner membrane of yeast mitochondria. J Biol Chem 288(7):4792-8 PMID: 23283966
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- Lee S, et al. (2011) Electron cryomicroscopy structure of a membrane-anchored mitochondrial AAA protease. J Biol Chem 286(6):4404-11 PMID: 21147776
- Pierson TM, et al. (2011) Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases. PLoS Genet 7(10):e1002325 PMID: 22022284
- Di Bella D, et al. (2010) Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28. Nat Genet 42(4):313-21 PMID: 20208537
- Leroy I, et al. (2010) Processing of the dynamin Msp1p in S. pombe reveals an evolutionary switch between its orthologs Mgm1p in S. cerevisiae and OPA1 in mammals. FEBS Lett 584(14):3153-7 PMID: 20621843
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- Augustin S, et al. (2009) An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases. Mol Cell 35(5):574-85 PMID: 19748354
- Suppanz IE, et al. (2009) The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria. Mol Biol Cell 20(2):572-80 PMID: 19019989
- Pierrel F, et al. (2008) Coa2 is an assembly factor for yeast cytochrome c oxidase biogenesis that facilitates the maturation of Cox1. Mol Cell Biol 28(16):4927-39 PMID: 18541668
- Duvezin-Caubet S, et al. (2007) OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondria. Mol Biol Cell 18(9):3582-90 PMID: 17615298
- Hofacker M, et al. (2007) Structural and functional fingerprint of the mitochondrial ATP-binding cassette transporter Mdl1 from Saccharomyces cerevisiae. J Biol Chem 282(6):3951-61 PMID: 17150958
- Tatsuta T, et al. (2007) m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria. EMBO J 26(2):325-35 PMID: 17245427
- Ishihara N, et al. (2006) Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J 25(13):2966-77 PMID: 16778770
- Rugarli EI and Langer T (2006) Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia. Trends Mol Med 12(6):262-9 PMID: 16647881
- Nolden M, et al. (2005) The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 123(2):277-89 PMID: 16239145
- Korbel D, et al. (2004) Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits. EMBO Rep 5(7):698-703 PMID: 15205678
- Atorino L, et al. (2003) Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia. J Cell Biol 163(4):777-87 PMID: 14623864
- Kaser M, et al. (2003) Oma1, a novel membrane-bound metallopeptidase in mitochondria with activities overlapping with the m-AAA protease. J Biol Chem 278(47):46414-23 PMID: 12963738
- Kolodziejczak M, et al. (2002) A higher plant mitochondrial homologue of the yeast m-AAA protease. Molecular cloning, localization, and putative function. J Biol Chem 277(46):43792-8 PMID: 12228240
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- Savel'ev AS, et al. (1998) ATP-dependent proteolysis in mitochondria. m-AAA protease and PIM1 protease exert overlapping substrate specificities and cooperate with the mtHsp70 system. J Biol Chem 273(32):20596-602 PMID: 9685417
- Arlt H, et al. (1996) The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. Cell 85(6):875-85 PMID: 8681382
- Langer T and Neupert W (1996) Regulated protein degradation in mitochondria. Experientia 52(12):1069-76 PMID: 8988248
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