Other names published for SUP35: GST1, PNM2, SAL3, SUF12, SUP2, SUP36, [PSI], [PSI(+)], eRF3, YDR172W
SUP35 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
SUP35 - Regulation of (37)
| Reference | Other 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 |



