RPN13/YLR421C Literature Guide Help

Other names published for RPN13: proteasome regulatory particle lid subunit RPN13, YLR421C

RPN13 - All Curated References (67)

Results: 1 - 30 of 67 records
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ReferenceOther 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
Schreiber A and Peter M  (2013) Substrate recognition in selective autophagy and the ubiquitin-proteasome system. Biochim Biophys Acta ()
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
Rosenzweig R, et al.  (2012) Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome. J Biol Chem 287(18):14659-71
Sakata E, et al.  (2012) Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy. Proc Natl Acad Sci U S A 109(5):1479-84
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
Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
Varshavsky A  (2012) Three decades of studies to understand the functions of the ubiquitin family. Methods Mol Biol 832():1-11
Aiken CT, et al.  (2011) Oxidative stress-mediated regulation of proteasome complexes. Mol Cell Proteomics 10(5):R110.006924
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
Gomez TA, et al.  (2011) Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1. BMC Biol 9(1):33
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
Results: 1 - 30 of 67 records
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