SUP35/YDR172W Literature Guide Help

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

SUP35 - Protein-protein Interactions (137)

Results: 1 - 30 of 137 records
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ReferenceOther Genes Addressed
Bateman DA and Wickner RB  (2012) [PSI+] Prion transmission barriers protect Saccharomyces cerevisiae from infection: intraspecies 'species barriers'. Genetics 190(2):569-79
Duennwald ML, et al.  (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346
Gong H, et al.  (2012) Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast. PLoS Genet 8(4):e1002634
Helsen CW and Glover JR  (2012) Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104). J Biol Chem 287(1):542-56
Kervestin S, et al.  (2012) Testing the faux-UTR model for NMD: analysis of Upf1p and Pab1p competition for binding to eRF3/Sup35p. Biochimie 94(7):1560-71
Kiktev DA, et al.  (2012) Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol 32(24):4960-70
Kochneva-Pervukhova NV, et al.  (2012) Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast. PLoS One 7(1):e29832
Portillo AM, et al.  (2012) Effect of electrostatics on aggregation of prion protein Sup35 peptide. J Phys Condens Matter 24(16):164205
Richardson R, et al.  (2012) Mass spectrometric identification of proteins that interact through specific domains of the poly(A) binding protein. Mol Genet Genomics 287(9):711-30
Sabate R, et al.  (2012) Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions. Biomacromolecules 13(2):474-83
Saibil HR, et al.  (2012) Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures. Proc Natl Acad Sci U S A 109(37):14906-11
Wang IF, et al.  (2012) The self-interaction of native TDP-43 C terminus inhibits its degradation and contributes to early proteinopathies. Nat Commun 3():766
Winkler J, et al.  (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198(3):387-404
Chernova TA, et al.  (2011) Prion induction by the short-lived, stress-induced protein lsb2 is regulated by ubiquitination and association with the actin cytoskeleton. Mol Cell 43(2):242-52
Inoue Y, et al.  (2011) Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP-dependent manner. Genes Cells 16(5):545-56
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
Lin JY, et al.  (2011) Inter-Allelic Prion Propagation Reveals Conformational Relationships among a Multitude of [PSI] Strains. PLoS Genet 7(9):e1002297
Liu Y, et al.  (2011) Prefibrillar aggregates of yeast prion Sup35NM and its variant are toxic to mammalian cells. Neurol Sci 32(6):1147-52
McGlinchey RP, et al.  (2011) Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci U S A 108(13):5337-41
Newnam GP, et al.  (2011) Destabilization and recovery of a yeast prion after mild heat shock. J Mol Biol 408(3):432-48
Redeker V, et al.  (2011) Qualitative and quantitative multiplexed proteomic analysis of complex yeast protein fractions that modulate the assembly of the yeast prion sup35p. PLoS One 6(9):e23659
Sideri TC, et al.  (2011) Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant. J Biol Chem 286(45):38924-31
Ader C, et al.  (2010) Amyloid-like interactions within nucleoporin FG hydrogels. Proc Natl Acad Sci U S A 107(14):6281-5
Berhanu WM and Masunov AE  (2010) Natural polyphenols as inhibitors of amyloid aggregation. Molecular dynamics study of GNNQQNY heptapeptide decamer. Biophys Chem 149(1-2):12-21
Derdowski A, et al.  (2010) A size threshold limits prion transmission and establishes phenotypic diversity. Science 330(6004):680-3
Duennwald ML and Shorter J  (2010) Countering amyloid polymorphism and drug resistance with minimal drug cocktails. Prion 4(4):244-51
Erhardt M, et al.  (2010) Extra N-terminal residues have a profound effect on the aggregation properties of the potential yeast prion protein mca1. PLoS One 5(3):e9929
Garrity SJ, et al.  (2010) Conversion of a yeast prion protein to an infectious form in bacteria. Proc Natl Acad Sci U S A 107(23):10596-601
Goehler H, et al.  (2010) Pathogenic polyglutamine tracts are potent inducers of spontaneous sup35 and rnq1 amyloidogenesis. PLoS One 5(3):e9642
Khoshnevis S, et al.  (2010) The iron-sulphur protein RNase L inhibitor functions in translation termination. EMBO Rep 11(3):214-9
Results: 1 - 30 of 137 records
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