RNQ1/YCL028W Literature Guide Help

Other names published for RNQ1: [PIN(+)], YCL028W

RNQ1 Literature Curation Summary

Curated References for RNQ1: 174

Date of last curation: 2013-03-27

ReferenceOther Genes Addressed
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 ()
Reidy M, et al.  (2013) Schizosaccharomyces pombe Disaggregation Machinery Chaperones Support Saccharomyces cerevisiae Growth and Prion Propagation. Eukaryot Cell 12(5):739-45
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
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
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
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
Hofmann J, et al.  (2012) Creutzfeldt-Jakob disease and mad cows: lessons learnt from yeast cells. Swiss Med Wkly 142():1-11
Kelly AC, et al.  (2012) Sex, prions, and plasmids in yeast. Proc Natl Acad Sci U S A 109(40):E2683-90
Kochneva-Pervukhova NV, et al.  (2012) Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast. PLoS One 7(1):e29832
Liebman SW and Chernoff YO  (2012) Prions in yeast. Genetics 191(4):1041-72
Ma Z, et al.  (2012) Multiple roles for the Ess1 prolyl isomerase in the RNA polymerase II transcription cycle. Mol Cell Biol 32(17):3594-607
Reidy M, et al.  (2012) Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics 192(1):185-93
Sharma J and Liebman SW  (2012) [PSI(+) ] prion variant establishment in yeast.LID - 10.1111/mmi.12024 [doi] Mol Microbiol ()
Soto C  (2012) Transmissible proteins: expanding the prion heresy. Cell 149(5):968-77
Staniforth GL and Tuite MF  (2012) Fungal prions. Prog Mol Biol Transl Sci 107():417-56
Treusch S and Lindquist S  (2012) An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component. J Cell Biol 197(3):369-79
Wickner RB  (2012) Discovering protein-based inheritance through yeast genetics. J Biol Chem 287(18):14432-42
Wickner RB, et al.  (2012) Study of amyloids using yeast. Methods Mol Biol 849():321-46
Winkler J, et al.  (2012) Chaperone networks in protein disaggregation and prion propagation. J Struct Biol 179(2):152-60
Winkler J, et al.  (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198(3):387-404
Zhao X, et al.  (2012) Sequestration of Sup35 by aggregates of huntingtin fragments causes toxicity of [PSI+] yeast. J Biol Chem 287(28):23346-55
Afanasieva EG, et al.  (2011) Interspecies transmission of prions. Biochemistry (Mosc) 76(13):1375-84
Bruce KL and Chernoff YO  (2011) Sequence specificity and fidelity of prion transmission in yeast. Semin Cell Dev Biol 22(5):444-51
Bryan AW Jr, et al.  (2011) STITCHER: Dynamic assembly of likely amyloid and prion beta-structures from secondary structure predictions.LID - 10.1002/prot.23203 [doi] Proteins ()
Chernova TA, et al.  (2011) Prion induction by the short-lived, stress-induced protein lsb2 is regulated by ubiquitination and association with the actin cytoskeleton. Mol Cell 43(2):242-52