SUP35/YDR172W Literature Guide Help

Other names published for SUP35: GST1, PNM2, SAL3, SUF12, SUP2, SUP36, [PSI], [PSI(+)], eRF3, YDR172W

SUP35 - Protein Processing/Modification/Regulation (45)

ReferenceOther Genes Addressed
Park YN, et al.  (2012) Differences in the Curing of [PSI(+)] Prion by Various Methods of Hsp104 Inactivation. PLoS One 7(6):e37692
Reidy M, et al.  (2012) Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics 192(1):185-93
Zhong Z, et al.  (2012) [Quantification of the curing effects of phenanthridine on yeast prion [PSI+]]. Sheng Wu Gong Cheng Xue Bao 28(6):737-46
Kabani M, et al.  (2011) A mutation within the C-terminal domain of Sup35p that affects [PSI+] prion propagation. Mol Microbiol 81(3):640-58
Newnam GP, et al.  (2011) Destabilization and recovery of a yeast prion after mild heat shock. J Mol Biol 408(3):432-48
Shorter J  (2011) The Mammalian disaggregase machinery: hsp110 synergizes with hsp70 and hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 6(10):e26319
Tsuji T, et al.  (2011) Single-particle tracking of quantum dot-conjugated prion proteins inside yeast cells. Biochem Biophys Res Commun 405(4):638-43
Reidy M and Masison DC  (2010) Sti1 Regulation of Hsp70 and Hsp90 Is Critical for Curing of Saccharomyces cerevisiae [PSI+] Prions by Hsp104. Mol Cell Biol 30(14):3542-52
Sideri TC, et al.  (2010) Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast. Proc Natl Acad Sci U S A 107(14):6394-9
Roberts BE, et al.  (2009) A synergistic small-molecule combination directly eradicates diverse prion strain structures. Nat Chem Biol 5(12):936-46
Strawn LA, et al.  (2009) Mutants of the Paf1 complex alter phenotypic expression of the yeast prion [PSI+]. Mol Biol Cell 20(8):2229-41
Alexandrov IM, et al.  (2008) Appearance and Propagation of Polyglutamine-based Amyloids in Yeast: TYROSINE RESIDUES ENABLE POLYMER FRAGMENTATION. J Biol Chem 283(22):15185-92
Fabret C, et al.  (2008) A novel mutant of the Sup35 protein of Saccharomyces cerevisiae defective in translation termination and in GTPase activity still supports cell viability. BMC Mol Biol 9:22
Feng BY, et al.  (2008) Small-molecule aggregates inhibit amyloid polymerization. Nat Chem Biol 4(3):197-9
Higurashi T, et al.  (2008) Specificity of the J-protein Sis1 in the propagation of 3 yeast prions. Proc Natl Acad Sci U S A 105(43):16596-601
Kryndushkin DS, et al.  (2008) Curing of the [URE3] prion by Btn2p, a Batten disease-related protein. EMBO J 27(20):2725-35
Kurahashi H, et al.  (2008) A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates. Mol Cell Biol 28(10):3313-23
Sadlish H, et al.  (2008) Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE 3(3):e1763
Shorter J and Lindquist S  (2008) Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J 27(20):2712-24
Tessarz P, et al.  (2008) Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol Microbiol 68(1):87-97
Tyedmers J, et al.  (2008) Prion switching in response to environmental stress. PLoS Biol 6(11):e294
Allen KD, et al.  (2007) Effects of ubiquitin system alterations on the formation and loss of a yeast prion. J Biol Chem 282(5):3004-13
Byrne LJ, et al.  (2007) Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride. Proc Natl Acad Sci U S A 104(28):11688-93
Chabelskaya S, et al.  (2007) Inactivation of NMD increases viability of sup45 nonsense mutants in Saccharomyces cerevisiae. BMC Mol Biol 8:71
Kodama H, et al.  (2007) The role of N-terminal domain of translational release factor eRF3 for the control of functionality and stability in S. cerevisiae. Genes Cells 12(5):639-50
Shewmaker F, et al.  (2007) Ure2p Function Is Enhanced by Its Prion Domain in Saccharomyces cerevisiae. Genetics 176(3):1557-65
von der Haar T, et al.  (2007) Development of a Novel Yeast Cell-Based System for Studying the Aggregation of Alzheimer's Disease-Associated Abeta Peptides in vivo. Neurodegener Dis 4(2-3):136-47
Krzewska J and Melki R  (2006) Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. EMBO J 25(4):822-33
Park KW, et al.  (2006) De novo appearance and "strain" formation of yeast prion [PSI+] are regulated by the heat-shock transcription factor. Genetics 173(1):35-47
Shkundina IS, et al.  (2006) The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variants. Genetics 172(2):827-35