SUP35/YDR172W Literature Guide Help

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

SUP35 - Cross-species Expression (18)

ReferenceOther Genes Addressed
Afanasieva EG, et al.  (2011) Molecular Basis for Transmission Barrier and Interference between Closely Related Prion Proteins in Yeast. J Biol Chem 286(18):15773-80
Chen B, et al.  (2010) Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission. Mol Microbiol 76(6):1483-99
Mathur V, et al.  (2010) Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast. Mol Biol Cell 21(9):1449-61
Speare JO, et al.  (2010) GPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells. EMBO J 29(4):782-94
Krammer C, et al.  (2009) The yeast Sup35NM domain propagates as a prion in mammalian cells. Proc Natl Acad Sci U S A 106(2):462-7
Tang H, et al.  (2009) Fibrinogen has chaperone-like activity. Biochem Biophys Res Commun 378(3):662-7
Kalastavadi T and True HL  (2008) Prion protein insertional mutations increase aggregation propensity but not fiber stability. BMC Biochem 9:7
Krammer C, et al.  (2008) Dynamic interactions of Sup35p and PrP prion protein domains modulate aggregate nucleation and seeding. Prion 2(3):99-106
Krammer C, et al.  (2008) Prion protein/protein interactions: fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells. FASEB J 22(3):762-73
Li LB, et al.  (2007) Suppression of polyglutamine toxicity by the yeast sup35 prion domain in Drosophila. J Biol Chem 282(52):37694-701
Tessier PM and Lindquist S  (2007) Prion recognition elements govern nucleation, strain specificity and species barriers. Nature 447(7144):556-61
[No authors listed]  (2007) [Conservation of the MC domains in eukaryotic release factor 3] Genetika 43(1):38-44
Ono B, et al.  (2006) Production of a Polymer-Forming Fusion Protein in Escerichia coli Strain BL21. Biosci Biotechnol Biochem 70(12):2813-23
Lundmark K, et al.  (2005) Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism. Proc Natl Acad Sci U S A 102(17):6098-102
Zadorskii SP, et al.  (2003) [Suppression of nonsense and frameshift mutations obtained by different methods for inactivating the translation termination factor eRF3 in yeast Saccharomyces cerevisiae] Genetika 39(4):489-94
Le Goff C, et al.  (2002) Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo. Genes Cells 7(10):1043-57
Osherovich LZ and Weissman JS  (2001) Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Cell 106(2):183-94
Santoso A, et al.  (2000) Molecular basis of a yeast prion species barrier. Cell 100(2):277-88