CIC1/YHR052W Literature Guide Help

Other names published for CIC1: NSA3, YHR052W

CIC1 - Additional Literature (27)

ReferenceOther 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
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
Kimura A, et al.  (2012) N-myristoylation of the Rpt2 subunit regulates intracellular localization of the yeast 26S proteasome. Biochemistry 51(44):8856-66
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
Henderson A, et al.  (2011) Dependence of proteasome processing rate on substrate unfolding. J Biol Chem 286(20):17495-502
Albanese V, et al.  (2010) A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis. J Cell Biol 189(1):69-81
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
Helbig AO, et al.  (2010) Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels. BMC Genomics 11(1):685
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
Prakash S, et al.  (2009) Substrate selection by the proteasome during degradation of protein complexes. Nat Chem Biol 5(1):29-36
Warkocki Z, et al.  (2009) Reconstitution of both steps of Saccharomyces cerevisiae splicing with purified spliceosomal components. Nat Struct Mol Biol 16(12):1237-43
Lebreton A, et al.  (2008) 60S ribosomal subunit assembly dynamics defined by semi-quantitative mass spectrometry of purified complexes. Nucleic Acids Res 36(15):4988-99
Fuentes JL, et al.  (2007) In vivo functional characterization of the Saccharomyces cerevisiae 60S biogenesis GTPase Nog1. Mol Genet Genomics 278(1):105-23
Liu C, et al.  (2007) Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells. Biotechniques 42(2):158, 160, 162
Oeffinger M, et al.  (2007) Comprehensive analysis of diverse ribonucleoprotein complexes. Nat Methods 4(11):951-6
Pertschy B, et al.  (2007) Cytoplasmic Recycling of 60S Preribosomal Factors Depends on the AAA Protein Drg1. Mol Cell Biol 27(19):6581-92
Smith DM, et al.  (2007) Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry. Mol Cell 27(5):731-44
Fry RC, et al.  (2006) The DNA-damage signature in Saccharomyces cerevisiae is associated with single-strand breaks in DNA. BMC Genomics 7():313
Germino M, et al.  (2006) A vector for double epitope tagging with a recyclable marker. Yeast 23(10):763-9
Salamat-Miller N, et al.  (2006) A network-based analysis of polyanion-binding proteins utilizing yeast protein arrays. Mol Cell Proteomics 5(12):2263-78
Wade CH, et al.  (2006) The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains over 200 genes. Yeast 23(4):293-306
Dechamps C, et al.  (2005) Multicopy suppression screen in the msb3 msb4 Saccharomyces cerevisiae double mutant, affected in Ypt/RabGAP activity. Biotechnol Lett 27(19):1439-49
Graindorge JS, et al.  (2005) Deletion of EFL1 results in heterogeneity of the 60 S GTPase-associated rRNA conformation. J Mol Biol 352(2):355-69
Lebaron S, et al.  (2005) The splicing ATPase prp43p is a component of multiple preribosomal particles. Mol Cell Biol 25(21):9269-82
Denison C and Kodadek T  (2004) Toward a general chemical method for rapidly mapping multi-protein complexes. J Proteome Res 3(3):417-25
Hayano T, et al.  (2003) Proteomic analysis of human Nop56p-associated pre-ribosomal ribonucleoprotein complexes. Possible link between Nop56p and the nucleolar protein treacle responsible for Treacher Collins syndrome. J Biol Chem 278(36):34309-19
Loidl G, et al.  (1999) Bivalency as a principle for proteasome inhibition. Proc Natl Acad Sci U S A 96(10):5418-22