SUP35/YDR172W Literature Guide Help

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

SUP35 - Substrates/Ligands/Cofactors (15)

ReferenceOther Genes Addressed
Shoemaker CJ and Green R  (2011) Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast. Proc Natl Acad Sci U S A 108(51):E1392-8
Shoemaker CJ, et al.  (2010) Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay. Science 330(6002):369-72
Song Y, et al.  (2010) Quantitative Effects of Magnesium Chloride Stress on Aggregation of Sup35p in [psi(-)] Yeast Cells. Protein Pept Lett 17(12):1489-94
Suhre MH, et al.  (2009) Influence of divalent copper, manganese and zinc ions on fibril nucleation and elongation of the amyloid-like yeast prion determinant Sup35p-NM. J Inorg Biochem 103(12):1711-20
Krammer C, et al.  (2008) Dynamic interactions of Sup35p and PrP prion protein domains modulate aggregate nucleation and seeding. Prion 2(3):99-106
Dong J, et al.  (2007) Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions. J Biol Chem 282(47):34204-12
Chen CY, et al.  (2005) Characterization and enzymatic degradation of Sup35NM, a yeast prion-like protein. Protein Sci 14(9):2228-35
Krishnan R and Lindquist SL  (2005) Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435(7043):765-72
Cole DJ, et al.  (2004) Estimating the number of prions in yeast cells. Math Med Biol 21(4):369-95
Kobayashi T, et al.  (2004) The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay. J Biol Chem 279(44):45693-700
Salas-Marco J and Bedwell DM  (2004) GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination. Mol Cell Biol 24(17):7769-78
Bach S, et al.  (2003) Isolation of drugs active against mammalian prions using a yeast-based screening assay. Nat Biotechnol 21(9):1075-81
Kryndushkin DS, et al.  (2002) Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions. J Biol Chem 277(26):23702-8
Ness F, et al.  (2002) Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast. Mol Cell Biol 22(15):5593-605
Tuite MF and McLaughlin CS  (1984) The effects of paromomycin on the fidelity of translation in a yeast cell-free system. Biochim Biophys Acta 783(2):166-70