Other names published for RPL25: L25, YL25, rpl6L, L23, ribosomal 60S subunit protein L25, YOL127W
RPL25 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Cellular Location
- Function/Process
- Genetic Interactions
- Mutants/Phenotypes
- Regulation of
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
RPL25 - Mutants/Phenotypes (21)
| Reference | Other Genes Addressed |
|---|---|
| Steffen KK, et al. (2012) Ribosome deficiency protects against ER stress in Saccharomyces cerevisiae. Genetics 191(1):107-18 | |
| Ambroset C, et al. (2011) Deciphering the molecular basis of wine yeast fermentation traits using a combined genetic and genomic approach. G3 (Bethesda) 1(4):263-81 | |
| Parenteau J, et al. (2011) Introns within Ribosomal Protein Genes Regulate the Production and Function of Yeast Ribosomes. Cell 147(2):320-31 | |
| Reiter A, et al. (2011) Reduction in Ribosomal Protein Synthesis Is Sufficient To Explain Major Effects on Ribosome Production after Short-Term TOR Inactivation in Saccharomyces cerevisiae. Mol Cell Biol 31(4):803-817 | |
| Lo KY and Johnson AW (2009) Reengineering ribosome export. Mol Biol Cell 20(5):1545-54 | |
| Poll G, et al. (2009) rRNA maturation in yeast cells depleted of large ribosomal subunit proteins. PLoS One 4(12):e8249 | |
| Dalley JA, et al. (2008) Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation. Mol Biol Cell 19(7):2876-84 | |
| Chiocchetti A, et al. (2007) Ribosomal proteins Rpl10 and Rps6 are potent regulators of yeast replicative life span. Exp Gerontol 42(4):275-86 | |
| Ross CL, et al. (2007) Functional conservation between structurally diverse ribosomal proteins from Drosophila melanogaster and Saccharomyces cerevisiae: fly L23a can substitute for yeast L25 in ribosome assembly and function. Nucleic Acids Res 35(13):4503-14 | |
| Timney BL, et al. (2006) Simple kinetic relationships and nonspecific competition govern nuclear import rates in vivo. J Cell Biol 175(4):579-93 | |
| Galani K, et al. (2004) Rea1, a dynein-related nuclear AAA-ATPase, is involved in late rRNA processing and nuclear export of 60 S subunits. J Biol Chem 279(53):55411-8 | |
| Inada T, et al. (2002) One-step affinity purification of the yeast ribosome and its associated proteins and mRNAs. RNA 8(7):948-58 | |
| McIntosh KB and Bonham-Smith PC (2001) Establishment of Arabidopsis thaliana ribosomal protein RPL23A-1 as a functional homologue of Saccharomyces cerevisiae ribosomal protein L25. Plant Mol Biol 46(6):673-82 | |
| van Beekvelt CA, et al. (2000) Domain III of Saccharomyces cerevisiae 25 S ribosomal RNA: its role in binding of ribosomal protein L25 and 60 S subunit formation. J Mol Biol 296(1):7-17 | |
| Hurt E, et al. (1999) A novel in vivo assay reveals inhibition of ribosomal nuclear export in ran-cycle and nucleoporin mutants. J Cell Biol 144(3):389-401 | |
| Kooi EA, et al. (1994) Mutational analysis of the C-terminal region of Saccharomyces cerevisiae ribosomal protein L25 in vitro and in vivo demonstrates the presence of two distinct functional elements. J Mol Biol 240(3):243-55 | |
| Rutgers CA, et al. (1991) rRNA binding domain of yeast ribosomal protein L25. Identification of its borders and a key leucine residue. J Mol Biol 218(2):375-85 | |
| Schaap PJ, et al. (1991) Identification and functional analysis of the nuclear localization signals of ribosomal protein L25 from Saccharomyces cerevisiae. J Mol Biol 221(1):225-37 | |
| Rutgers CA, et al. (1990) In vivo and in vitro analysis of structure-function relationships in ribosomal protein L25 from Saccharomyces cerevisiae. Biochim Biophys Acta 1050(1-3):74-9 | |
| Woudt LP, et al. (1986) Conserved sequence elements upstream of the gene encoding yeast ribosomal protein L25 are involved in transcription activation. EMBO J 5(5):1037-40 | |
| elBaradi TT, et al. (1986) The cellular level of yeast ribosomal protein L25 is controlled principally by rapid degradation of excess protein. Curr Genet 10(10):733-9 | |



