EGD2/YHR193C Literature Guide Help

Other names published for EGD2: YHR193C

EGD2 - Additional Literature (20)

ReferenceOther Genes Addressed
Sung MK, et al.  (2013) Genome-wide bimolecular fluorescence complementation analysis of SUMO interactome in yeast. Genome Res 23(4):736-46
Zhang Y, et al.  (2012) NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum. Mol Biol Cell 23(16):3027-40
Dearmond PD, et al.  (2011) Thermodynamic analysis of protein-ligand interactions in complex biological mixtures using a shotgun proteomics approach. J Proteome Res 10(11):4948-58
Hayashi S, et al.  (2011) EGD1 (beta-NAC) mRNA is localized in a novel cytoplasmic structure in Saccharomyces cerevisiae. Genes Cells 16(3):316-29
Gallego O, et al.  (2010) A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Mol Syst Biol 6():430
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
Mendu V, et al.  (2010) Cpr1 cyclophilin and Ess1 parvulin prolyl isomerases interact with the tombusvirus replication protein and inhibit viral replication in yeast model host. Virology 406(2):342-51
Lin FM, et al.  (2009) Comparative proteomic analysis of tolerance and adaptation of ethanologenic Saccharomyces cerevisiae to furfural, a lignocellulosic inhibitory compound. Appl Environ Microbiol 75(11):3765-76
Lin FM, et al.  (2009) Temporal quantitative proteomics of Saccharomyces cerevisiae in response to a nonlethal concentration of furfural. Proteomics 9(24):5471-83
Dalley JA, et al.  (2008) Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation. Mol Biol Cell 19(7):2876-84
Guerrero C, et al.  (2008) Characterization of the proteasome interaction network using a QTAX-based tag-team strategy and protein interaction network analysis. Proc Natl Acad Sci U S A 105(36):13333-8
Grallath S, et al.  (2007) L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle. EMBO Rep 8(11):1086
Wu D, et al.  (2007) Covert genetic selections to optimize phenotypes. PLoS ONE 2(11):e1200
Grallath S, et al.  (2006) L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle. EMBO Rep 7(1):78-84
Raasi S, et al.  (2005) Diverse polyubiquitin interaction properties of ubiquitin-associated domains. Nat Struct Mol Biol 12(8):708-14
Spreter T, et al.  (2005) The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain. J Biol Chem 280(16):15849-54
Bro C, et al.  (2003) Transcriptional, proteomic, and metabolic responses to lithium in galactose-grown yeast cells. J Biol Chem 278(34):32141-9
George R, et al.  (2002) The nascent polypeptide-associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo. FEBS Lett 516(1-3):213-6
Gautschi M, et al.  (2001) RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin. Proc Natl Acad Sci U S A 98(7):3762-7
Beatrix B, et al.  (2000) The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functions. J Biol Chem 275(48):37838-45