SAN1/YDR143C Literature Guide Help

Other names published for SAN1: ubiquitin-protein ligase SAN1, YDR143C

SAN1 - Primary Literature (19)

ReferenceOther Genes Addressed
Arlow T, et al.  (2013) Proteasome inhibition rescues clinically significant unstable variants of the mismatch repair protein Msh2. Proc Natl Acad Sci U S A 110(1):246-51
Fredrickson EK, et al.  (2013) Means of self-preservation: how an intrinsically disordered ubiquitin-protein ligase averts self-destruction. Mol Biol Cell 24(7):1041-52
Fredrickson EK, et al.  (2013) Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility. J Biol Chem 288(9):6130-9
Guerriero CJ, et al.  (2013) Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligase. J Biol Chem ()
Summers DW, et al.  (2013) The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein. PLoS One 8(1):e52099
Khosrow-Khavar F, et al.  (2012) The yeast ubr1 ubiquitin ligase participates in a prominent pathway that targets cytosolic thermosensitive mutants for degradation. G3 (Bethesda) 2(5):619-28
Prasad R, et al.  (2012) Biosynthetic mode can determine the mechanism of protein quality control. Biochem Biophys Res Commun 425(3):689-95
Theodoraki MA, et al.  (2012) A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast. J Biol Chem 287(28):23911-22
Arlt H, et al.  (2011) An overexpression screen in Saccharomyces cerevisiae identifies novel genes that affect endocytic protein trafficking. Traffic 12(11):1592-603
Fredrickson EK, et al.  (2011) Exposed hydrophobicity is a key determinant of nuclear quality control degradation. Mol Biol Cell 22(13):2384-95
Rosenbaum JC, et al.  (2011) Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. Mol Cell 41(1):93-106
Heck JW, et al.  (2010) Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc Natl Acad Sci U S A 107(3):1106-11
Prasad R, et al.  (2010) A nucleus-based quality control mechanism for cytosolic proteins. Mol Biol Cell 21(13):2117-27
Estruch F, et al.  (2009) A genetic screen in Saccharomyces cerevisiae identifies new genes that interact with mex67-5, a temperature-sensitive allele of the gene encoding the mRNA export receptor. Mol Genet Genomics 281(1):125-34
Iwata A, et al.  (2009) Intranuclear degradation of polyglutamine aggregates by the ubiquitin-proteasome system. J Biol Chem 284(15):9796-803
Gardner RG, et al.  (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15
Dasgupta A, et al.  (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8
Xu Q, et al.  (1993) The Saccharomyces cerevisiae Cdc68 transcription activator is antagonized by San1, a protein implicated in transcriptional silencing. Mol Cell Biol 13(12):7553-65
Schnell R, et al.  (1989) Genetic and molecular characterization of suppressors of SIR4 mutations in Saccharomyces cerevisiae. Genetics 122(1):29-46