Other names published for RPN13: proteasome regulatory particle lid subunit RPN13, YLR421C
RPN13 LITERATURE TOPICS
- Curated Literature
- Additional Literature
- All Curated References
- Primary Literature
- Reviews
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
RPN13 - Additional Literature (46)
| Reference | Other Genes Addressed |
|---|---|
| Concannon C and Lahue RS (2013) The 26S proteasome drives trinucleotide repeat expansions. Nucleic Acids Res () | |
| Peth A, et al. (2013) Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs. J Biol Chem 288(11):7781-90 | |
| 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 | |
| Elsasser S, et al. (2012) Binding of ubiquitin conjugates to proteasomes as visualized with native gels. Methods Mol Biol 832():403-22 | |
| Enenkel C (2012) Using Native Gel Electrophoresis and Phosphofluoroimaging to Analyze GFP-Tagged Proteasomes. Methods Mol Biol 832():339-48 | |
| Ha SW, et al. (2012) The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits. Biochem Biophys Res Commun 419(2):226-31 | |
| Jacobson T, et al. (2012) Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast. J Cell Sci 125(Pt 21):5073-83 | |
| Kao A, et al. (2012) Mapping the structural topology of the yeast 19S proteasomal regulatory particle using chemical cross-linking and probabilistic modeling. Mol Cell Proteomics 11(12):1566-77 | |
| Kimura A, et al. (2012) N-myristoylation of the Rpt2 subunit regulates intracellular localization of the yeast 26S proteasome. Biochemistry 51(44):8856-66 | |
| Lasker K, et al. (2012) Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proc Natl Acad Sci U S A 109(5):1380-7 | |
| Takagi K, et al. (2012) Structural basis for specific recognition of Rpt1p, an ATPase subunit of 26 S proteasome, by proteasome-dedicated chaperone Hsm3p. J Biol Chem 287(15):12172-82 | |
| Bonzanni N, et al. (2011) The role of proteosome-mediated proteolysis in modulating potentially harmful transcription factor activity in Saccharomyces cerevisiae. Bioinformatics 27(13):i283-i287 | |
| Hatanaka A, et al. (2011) Fub1p, a novel protein isolated by boundary screening, binds the proteasome complex. Genes Genet Syst 86(5):305-14 | |
| Henderson A, et al. (2011) Dependence of proteasome processing rate on substrate unfolding. J Biol Chem 286(20):17495-502 | |
| Inobe T, et al. (2011) Defining the geometry of the two-component proteasome degron. Nat Chem Biol 7(3):161-7 | |
| Kraut DA and Matouschek A (2011) Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization. ACS Chem Biol 6(10):1087-95 | |
| Park S, et al. (2011) Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response. J Biol Chem 286(42):36652-66 | |
| Sakata E, et al. (2011) The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle. Mol Cell 42(5):637-49 | |
| Tomko RJ Jr and Hochstrasser M (2011) Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joining. Mol Cell 44(6):907-17 | |
| White RR, et al. (2011) Characterisation of the Trichinella spiralis Deubiquitinating Enzyme, TsUCH37, an Evolutionarily Conserved Proteasome Interaction Partner. PLoS Negl Trop Dis 5(10):e1340 | |
| Wu S, et al. (2011) An integrated top-down and bottom-up strategy for characterization of protein isoforms and modifications. Methods Mol Biol 694():291-304 | |
| Ziv I, et al. (2011) A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis. Mol Cell Proteomics 10(5):M111.009753 | |
| Chandra A, et al. (2010) Synthetic lethality of rpn11-1 rpn10Delta is linked to altered proteasome assembly and activity. Curr Genet 56(6):543-57 | |
| Kikuchi J, et al. (2010) Co- and post-translational modifications of the 26S proteasome in yeast. Proteomics 10(15):2769-79 | |
| Voloshin O, et al. (2010) Tubulin chaperone E binds microtubules and proteasomes and protects against misfolded protein stress. Cell Mol Life Sci 67(12):2025-38 | |
| Wang X, et al. (2010) Regulation of the 26S Proteasome Complex During Oxidative Stress. Sci Signal 3(151):ra88 | |
| Bech-Otschir D, et al. (2009) Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome. Nat Struct Mol Biol 16(2):219-25 | |
| Funakoshi M, et al. (2009) Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell 137(5):887-99 | |
| Liu C, et al. (2009) A genome-wide synthetic dosage lethality screen reveals multiple pathways that require the functioning of ubiquitin-binding proteins Rad23 and Dsk2. BMC Biol 7(1):75 | |
| Saeki Y, et al. (2009) Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle. Cell 137(5):900-13 |



