RAD23/YEL037C Literature Guide Help

Other names published for RAD23: YEL037C

RAD23 - Primary Literature (66)

ReferenceOther Genes Addressed
Rosenzweig R, et al.  (2012) Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome. J Biol Chem 287(18):14659-71
Fishbain S, et al.  (2011) Rad23 escapes degradation because it lacks a proteasome initiation region. Nat Commun 2():192
Inobe T, et al.  (2011) Defining the geometry of the two-component proteasome degron. Nat Chem Biol 7(3):161-7
Liu C, et al.  (2011) Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase. J Biol Chem 286(51):43660-7
Barbin L, et al.  (2010) The Cdc48-Ufd1-Npl4 complex is central in ubiquitin-proteasome triggered catabolite degradation of fructose-1,6-bisphosphatase. Biochem Biophys Res Commun 394(2):335-41
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
Chen M, et al.  (2010) Arabidopsis HEMERA/pTAC12 initiates photomorphogenesis by phytochromes. Cell 141(7):1230-40
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
Li Y, et al.  (2010) Rad4 regulates protein turnover at a postubiquitylation step. Mol Biol Cell 21(1):177-85
Marblestone JG, et al.  (2010) Novel approach for characterizing ubiquitin E3 ligase function. J Biomol Screen 15(10):1220-8
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
Wade SL, et al.  (2009) The Snf1 kinase and proteasome-associated Rad23 regulate UV-responsive gene expression. EMBO J 28(19):2919-31
Wang S, et al.  (2009) N-terminal deletion of Peptide:N-glycanase results in enhanced deglycosylation activity. PLoS One 4(12):e8335
Zhang L, et al.  (2009) Assays for chromatin remodeling during nucleotide excision repair in Saccharomyces cerevisiae. Methods 48(1):19-22
Auesukaree C, et al.  (2008) Ddi1p and Rad23p play a cooperative role as negative regulators in the PHO pathway in Saccharomyces cerevisiae. Biochem Biophys Res Commun 365(4):821-5
Chen L and Madura K  (2008) Centrin/Cdc31 is a novel regulator of protein degradation. Mol Cell Biol 28(5):1829-40
Rosenzweig R, et al.  (2008) The central unit within the 19S regulatory particle of the proteasome. Nat Struct Mol Biol 15(6):573-80
Hwang GW  (2007) A Ubiquitin-proteasome System as a Factor that Determine the Sensitivity to Methylmercury. Yakugaku Zasshi 127(3):463-8
Romero-Perez L, et al.  (2007) Sts1 can overcome the loss of Rad23 and Rpn10 and represents a novel regulator of the ubiquitin/proteasome pathway. J Biol Chem 282(49):35574-82
Daniel JA, et al.  (2006) Diverse functions of spindle assembly checkpoint genes in Saccharomyces cerevisiae. Genetics 172(1):53-65
Diaz-Martinez LA, et al.  (2006) Yeast UBL-UBA proteins have partially redundant functions in cell cycle control. Cell Div 1:28
Heiligenstein S, et al.  (2006) Retrotranslocation of a viral A/B toxin from the yeast endoplasmic reticulum is independent of ubiquitination and ERAD. EMBO J 25(20):4717-27
Ishii T, et al.  (2006) Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway. EMBO J 25(23):5492-503
Kim I, et al.  (2006) The Png1-Rad23 complex regulates glycoprotein turnover. J Cell Biol 172(2):211-9
Chuang SM, et al.  (2005) Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A. Mol Cell Biol 25(1):403-13
Heessen S, et al.  (2005) The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation. Mol Cell 18(2):225-35
Lee JH, et al.  (2005) Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins. Proc Natl Acad Sci U S A 102(26):9144-9
Richly H, et al.  (2005) A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120(1):73-84
Biswas S, et al.  (2004) The N-terminus of yeast peptide: N-glycanase interacts with the DNA repair protein Rad23. Biochem Biophys Res Commun 323(1):149-55
Elsasser S, et al.  (2004) Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J Biol Chem 279(26):26817-22