SUP35/YDR172W Literature Guide Help

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

SUP35 - Regulation of (37)

ReferenceOther Genes Addressed
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
Reidy M, et al.  (2012) Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics 192(1):185-93
Hines JK, et al.  (2011) Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements. Prion 5(4):238-44
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
Nevzglyadova OV, et al.  (2011) The effect of red pigment on the amyloidization of yeast proteins. Yeast 28(7):505-26
Radchenko E, et al.  (2011) SUP35 expression is enhanced in yeast containing [ISP+], a prion form of the transcriptional regulator Sfp1. Prion 5(4):317-22
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
Verges KJ, et al.  (2011) Strain conformation, primary structure and the propagation of the yeast prion [PSI(+)]. Nat Struct Mol Biol 18(4):493-9
Duennwald ML and Shorter J  (2010) Countering amyloid polymorphism and drug resistance with minimal drug cocktails. Prion 4(4):244-51
Kalastavadi T and True HL  (2010) Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation. J Biol Chem 285(27):20748-55
Senechal P, et al.  (2009) The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion. PLoS One 4(9):e6939
Tang H, et al.  (2009) Fibrinogen has chaperone-like activity. Biochem Biophys Res Commun 378(3):662-7
[No authors listed]  (2009) [The influence of mutations at ATG triplets of the open reading frame SUP35 on viability of the yeast Saccharomyces cerevisiae] Genetika 45(2):178-84
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
Sharma D and Masison DC  (2008) Functionally redundant isoforms of a yeast hsp70 chaperone subfamily have different antiprion effects. Genetics 179(3):1301-11
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
Kryndushkin D and Wickner RB  (2007) Nucleotide Exchange Factors for Hsp70s Are Required for [URE3] Prion Propagation in Saccharomyces cerevisiae. Mol Biol Cell 18(6):2149-54
Satpute-Krishnan P, et al.  (2007) Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance. PLoS Biol 5(2):e24
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
Tutar Y  (2006) Heat shock proteins, substrate specificity and modulation of function. Protein Pept Lett 13(7):699-705
Roberts BT, et al.  (2004) [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast. Yeast 21(2):107-17