Other names published for RPN1: HRD2, NAS1, proteasome regulatory particle base subunit RPN1, YHR027C
RPN1 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
RPN1 - Additional Literature (63)
| Reference | Other Genes Addressed |
|---|---|
| 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 | |
| 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 | |
| Chen L, et al. (2011) Sts1 plays a key role in targeting proteasomes to the nucleus. J Biol Chem 286(4):3104-18 | |
| Franzosa EA, et al. (2011) Heterozygous yeast deletion collection screens reveal essential targets of hsp90. PLoS One 6(11):e28211 | |
| 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 | |
| Joshi KK, et al. (2011) A proteasome assembly defect in rpn3 mutants is associated with Rpn11 instability and increased sensitivity to stress. J Mol Biol 410(3):383-99 | |
| 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 | |
| Sekiguchi T, et al. (2011) Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast. Biochem Biophys Res Commun 411(3):555-61 | |
| Wang Y, et al. (2011) Ubiquitin-dependent Proteasomal Degradation of Human Liver Cytochrome P450 2E1: IDENTIFICATION OF SITES TARGETED FOR PHOSPHORYLATION AND UBIQUITINATION. J Biol Chem 286(11):9443-56 | |
| 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) Proteasome assembly influences interaction with ubiquitinated proteins and shuttle factors. J Biol Chem 285(11):8330-9 | |
| 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 | |
| Cortajarena AL, et al. (2010) Designed proteins to modulate cellular networks. ACS Chem Biol 5(6):545-52 | |
| Fatimababy AS, et al. (2010) Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis. FEBS J 277(3):796-816 | |
| 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 | |
| Garza RM, et al. (2009) In vitro analysis of Hrd1p-mediated retrotranslocation of its multispanning membrane substrate 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase. J Biol Chem 284(22):14710-22 |



