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
- Literature Curation Summary
- SUP35 Summary Paragraph
- Pubmed Search
- Expanded Pubmed Search
- All genome-wide analysis papers
- Search Google Scholar
SUP35 Literature Curation Summary
Curated References for SUP35: 738
Date of last curation: 2013-04-12
| Reference | Other Genes Addressed |
|---|---|
| Arai C, et al. (2013) Clearance of yeast prions by misfolded multi-transmembrane proteins. Biochimie 95(6):1223-32 | |
| Bateman DA and Wickner RB (2013) The [PSI(+)] Prion Exists as a Dynamic Cloud of Variants. PLoS Genet 9(1):e1003257 | |
| Firczuk H, et al. (2013) An in vivo control map for the eukaryotic mRNA translation machinery. Mol Syst Biol 9():635 | |
| Grousl T, et al. (2013) Heat Shock-Induced Accumulation of Translation Elongation and Termination Factors Precedes Assembly of Stress Granules in S. cerevisiae. PLoS One 8(2):e57083 | |
| Hofmann JP, et al. (2013) Cell-to-cell propagation of infectious cytosolic protein aggregates. Proc Natl Acad Sci U S A 110(15):5951-6 | |
| Kurata S, et al. (2013) Possible steps of complete disassembly of post-termination complex by yeast eEF3 deduced from inhibition by translocation inhibitors. Nucleic Acids Res 41(1):264-76 | |
| Lancaster DL, et al. (2013) Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. J Biol Chem 288(2):1266-76 | |
| Oishi K, et al. (2013) A bipolar functionality of Q/N-rich proteins: Lsm4 amyloid causes clearance of yeast prions. Microbiologyopen () | |
| Osborne KL, et al. (2013) Thermodynamic analysis of structural transitions during GNNQQNY aggregation. Proteins () | |
| Reidy M, et al. (2013) Schizosaccharomyces pombe Disaggregation Machinery Chaperones Support Saccharomyces cerevisiae Growth and Prion Propagation. Eukaryot Cell 12(5):739-45 | |
| Tartakoff AM, et al. (2013) Septin-containing barriers control the differential inheritance of cytoplasmic elements. Cell Rep 3(1):223-36 | |
| Tomson BN and Arndt KM (2013) The many roles of the conserved eukaryotic Paf1 complex in regulating transcription, histone modifications, and disease states. Biochim Biophys Acta 1829(1):116-26 | |
| Tycko R and Wickner RB (2013) Molecular Structures of Amyloid and Prion Fibrils: Consensus versus Controversy. Acc Chem Res () | |
| Wickner RB, et al. (2013) Amyloids and yeast prion biology. Biochemistry 52(9):1514-27 | |
| Wickner RB, et al. (2013) Viruses and Prions of Saccharomyces cerevisiae. Adv Virus Res 86():1-36 | |
| Yang Z, et al. (2013) Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability. PLoS Genet 9(1):e1003236 | |
| Zhao JH, et al. (2013) Molecular modeling to investigate the binding of Congo red toward GNNQQNY protofibril and in silico virtual screening for the identification of new aggregation inhibitors. J Mol Model 19(1):151-62 | |
| Alexandrov AI, et al. (2012) The effects of amino Acid composition of glutamine-rich domains on amyloid formation and fragmentation. PLoS One 7(10):e46458 | |
| Bateman DA and Wickner RB (2012) [PSI+] Prion transmission barriers protect Saccharomyces cerevisiae from infection: intraspecies 'species barriers'. Genetics 190(2):569-79 | |
| Bucciantini M, et al. (2012) Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1. FASEB J 26(2):818-31 | |
| Cheng PN, et al. (2012) Amyloid beta-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity. Nat Chem 4(11):927-33 | |
| Desantis ME, et al. (2012) Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients. Cell 151(4):778-93 | |
| Duennwald ML, et al. (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346 | |
| Espargaro A, et al. (2012) Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact 11(1):89 | |
| Gong H, et al. (2012) Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast. PLoS Genet 8(4):e1002634 | |
| Halfmann R, et al. (2012) Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 482(7385):363-8 | |
| Harbi D, et al. (2012) PrionHome: A Database of Prions and Other Sequences Relevant to Prion Phenomena. PLoS ONE 7(2):e31785 | |
| Helsen CW and Glover JR (2012) A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ]. Prion 6(3):234-9 | |
| 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 | |
| Hofmann J, et al. (2012) Creutzfeldt-Jakob disease and mad cows: lessons learnt from yeast cells. Swiss Med Wkly 142():1-11 |





