Other names published for RPT4: CRL13, PCS1, SUG2, proteasome regulatory particle base subunit RPT4, YOR259C
RPT4 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
RPT4 - Protein Sequence Features (11)
| Reference | Other Genes Addressed |
|---|---|
| Beck F, et al. (2012) Near-atomic resolution structural model of the yeast 26S proteasome. Proc Natl Acad Sci U S A 109(37):14870-5 | |
| Dange T, et al. (2011) Blm10 protein promotes proteasomal substrate turnover by an active gating mechanism. J Biol Chem 286(50):42830-9 | |
| Tian G, et al. (2011) An asymmetric interface between the regulatory and core particles of the proteasome.LID - 10.1038/nsmb.2147 [doi] Nat Struct Mol Biol () | |
| Funakoshi M, et al. (2009) Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell 137(5):887-99 | |
| Park S, et al. (2009) Hexameric assembly of the proteasomal ATPases is templated through their C termini. Nature 459(7248):866-70 | |
| McDonald HB, et al. (2002) Mutational analysis reveals a role for the C terminus of the proteasome subunit Rpt4p in spindle pole body duplication in Saccharomyces cerevisiae. Genetics 162(2):705-20 | |
| Frohlich KU (2001) An AAA family tree. J Cell Sci 114(Pt 9):1601-2 | |
| Russell SJ, et al. (2001) Selective chemical inactivation of AAA proteins reveals distinct functions of proteasomal ATPases. Chem Biol 8(10):941-50 | |
| Glickman MH, et al. (1998) The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol 18(6):3149-62 | |
| 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 | |
| Russell SJ, et al. (1996) Isolation and characterization of SUG2. A novel ATPase family component of the yeast 26 S proteasome. J Biol Chem 271(51):32810-7 |




