Other names published for RIP1: ubiquinol--cytochrome-c reductase catalytic subunit RIP1, YEL024W
RIP1 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
- Substrates/Ligands/Cofactors
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
RIP1 - Protein Processing/Modification/Regulation (22)
| Reference | Other Genes Addressed |
|---|---|
| Doggett JS, et al. (2012) Endochin-like quinolones are highly efficacious against acute and latent experimental toxoplasmosis. Proc Natl Acad Sci U S A 109(39):15936-41 | |
| Atkinson A, et al. (2011) The LYR protein Mzm1 functions in the insertion of the Rieske Fe/S protein in yeast mitochondria. Mol Cell Biol 31(19):3988-96 | |
| Mathieu L, et al. (2011) A transcriptome screen in yeast identifies a novel assembly factor for the mitochondrial complex III. Mitochondrion 11(3):391-6 | |
| Vogtle FN, et al. (2011) Mitochondrial protein turnover: role of the precursor intermediate peptidase Oct1 in protein stabilization. Mol Biol Cell 22(13):2135-43 | |
| Bayot A, et al. (2010) Identification of novel oxidized protein substrates and physiological partners of the mitochondrial ATP-dependent Lon-like protease Pim1. J Biol Chem 285(15):11445-57 | |
| Martinez-Pastor M, et al. (2010) Adaptive changes of the yeast mitochondrial proteome in response to salt stress. OMICS 14(5):541-52 | |
| Cape JL, et al. (2009) Substrate redox potential controls superoxide production kinetics in the cytochrome bc complex. Biochemistry 48(45):10716-23 | |
| Covian R and Trumpower BL (2009) The Rate-limiting Step in the Cytochrome bc1 Complex (Ubiquinol-Cytochrome c Oxidoreductase) Is Not Changed by Inhibition of Cytochrome b-dependent Deprotonation: IMPLICATIONS FOR THE MECHANISM OF UBIQUINOL OXIDATION AT CENTER P OF THE bc1 COMPLEX. J Biol Chem 284(21):14359-67 | |
| Massoni A, et al. (2009) Exploring the dynamics of the yeast proteome by means of 2-DE. Proteomics 9(20):4674-85 | |
| Rintala E, et al. (2009) Low oxygen levels as a trigger for enhancement of respiratory metabolism in Saccharomyces cerevisiae. BMC Genomics 10():461 | |
| Gallas MR, et al. (2006) Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import. Mol Biol Cell 17(9):4051-62 | |
| Fisher N, et al. (2004) Disruption of the interaction between the Rieske iron-sulfur protein and cytochrome b in the yeast bc1 complex owing to a human disease-associated mutation within cytochrome b. Eur J Biochem 271(7):1292-8 | |
| Gutierrez-Cirlos EB, et al. (2002) Failure to insert the iron-sulfur cluster into the Rieske iron-sulfur protein impairs both center N and center P of the cytochrome bc1 complex. J Biol Chem 277(52):50703-9 | |
| Nett JH and Trumpower BL (1999) Intermediate length Rieske iron-sulfur protein is present and functionally active in the cytochrome bc1 complex of Saccharomyces cerevisiae. J Biol Chem 274(14):9253-7 | |
| Nett JH, et al. (1998) Processing of the presequence of the Schizosaccharomyces pombe Rieske iron-sulfur protein occurs in a single step and can be converted to two-step processing by mutation of a single proline to serine in the presequence. J Biol Chem 273(15):8652-8 | |
| Nett JH, et al. (1997) Two-step processing is not essential for the import and assembly of functionally active iron-sulfur protein into the cytochrome bc1 complex in Saccharomyces cerevisiae. J Biol Chem 272(4):2212-7 | |
| Nett JH and Trumpower BL (1996) Dissociation of import of the Rieske iron-sulfur protein into Saccharomyces cerevisiae mitochondria from proteolytic processing of the presequence. J Biol Chem 271(43):26713-6 | |
| Haucke V, et al. (1995) The yeast mitochondrial protein import receptor Mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence. J Biol Chem 270(10):5565-70 | |
| Ramabadran RS and Beattie DS (1992) Processing of the intermediate form of the iron-sulfur protein of the BC1 complex to the mature form after import into yeast mitochondria. Arch Biochem Biophys 296(1):279-85 | |
| Graham LA and Trumpower BL (1991) Mutational analysis of the mitochondrial Rieske iron-sulfur protein of Saccharomyces cerevisiae. III. Import, protease processing, and assembly into the cytochrome bc1 complex of iron-sulfur protein lacking the iron-sulfur cluster. J Biol Chem 266(33):22485-92 | |
| Fu W, et al. (1990) Import of the iron-sulfur protein of the cytochrome b.c1 complex into yeast mitochondria. J Biol Chem 265(27):16541-7 | |
| Crivellone MD, et al. (1988) Assembly of the mitochondrial membrane system. Analysis of structural mutants of the yeast coenzyme QH2-cytochrome c reductase complex. J Biol Chem 263(28):14323-33 |



