Other names published for MRPL32: YmL32, mitochondrial 54S ribosomal protein YmL32, YCR003W
MRPL32 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Protein Physical Properties
- Protein Processing/Modification/Regulation
- Protein Sequence Features
- Protein-protein Interactions
- Protein/Nucleic Acid Structure
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
MRPL32 - Protein Processing/Modification/Regulation (5)
| Reference | Other Genes Addressed |
|---|---|
| Bonn F, et al. (2011) Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria. EMBO J 30(13):2545-56 | |
| Di Bella D, et al. (2010) Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28. Nat Genet 42(4):313-21 | |
| 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 | |
| Tatsuta T, et al. (2007) m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria. EMBO J 26(2):325-35 | |
| Nolden M, et al. (2005) The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 123(2):277-89 |



