Other names published for AFG3: YTA10, AAA family ATPase AFG3, YER017C
AFG3 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Cross-species Expression
- Disease Gene Related
- Fungal Related Genes/Proteins
- Non-Fungal Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
AFG3 - Non-Fungal Related Genes/Proteins (22)
| Reference | Other Genes Addressed |
|---|---|
| Lopez LM, et al. (2012) Evolutionary conserved longevity genes and human cognitive abilities in elderly cohorts. Eur J Hum Genet 20(3):341-7 | |
| 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 | |
| Di Bella D, et al. (2010) Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28. Nat Genet 42(4):313-21 | |
| Augustin S, et al. (2009) An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases. Mol Cell 35(5):574-85 | |
| Smith ED, et al. (2008) Quantitative evidence for conserved longevity pathways between divergent eukaryotic species. Genome Res 18(4):564-70 | |
| 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):3582-3590 | |
| Rugarli EI and Langer T (2006) Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia. Trends Mol Med 12(6):262-9 | |
| Nolden M, et al. (2005) The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 123(2):277-89 | |
| 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 | |
| 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 | |
| Frohlich KU (2001) An AAA family tree. J Cell Sci 114(Pt 9):1601-2 | |
| Langer T (2000) AAA proteases: cellular machines for degrading membrane proteins. Trends Biochem Sci 25(5):247-51 | |
| Casari G, et al. (1998) Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease. Cell 93(6):973-83 | |
| Gottesman S, et al. (1997) Protein quality control: triage by chaperones and proteases. Genes Dev 11(7):815-23 | |
| Suzuki CK, et al. (1997) ATP-dependent proteases that also chaperone protein biogenesis. Trends Biochem Sci 22(4):118-23 | |
| Swaffield JC and Purugganan MD (1997) The evolution of the conserved ATPase domain (CAD): reconstructing the history of an ancient protein module. J Mol Evol 45(5):549-63 | |
| Guzelin E, et al. (1996) Afg3p, a mitochondrial ATP-dependent metalloprotease, is involved in degradation of mitochondrially-encoded Cox1, Cox3, Cob, Su6, Su8 and Su9 subunits of the inner membrane complexes III, IV and V. FEBS Lett 381(1-2):42-6 | |
| Paul MF and Tzagoloff A (1995) Mutations in RCA1 and AFG3 inhibit F1-ATPase assembly in Saccharomyces cerevisiae. FEBS Lett 373(1):66-70 | |
| Guelin E, et al. (1994) Sequence of the AFG3 gene encoding a new member of the FtsH/Yme1/Tma subfamily of the AAA-protein family. Yeast 10(10):1389-94 | |
| Pajic A, et al. (1994) Yta10p is required for the ATP-dependent degradation of polypeptides in the inner membrane of mitochondria. FEBS Lett 353(2):201-6 | |
| Schnall R, et al. (1994) Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex. Yeast 10(9):1141-55 | |
| Tauer R, et al. (1994) Yta10p, a member of a novel ATPase family in yeast, is essential for mitochondrial function. FEBS Lett 353(2):197-200 |




