The 38 papers which experimentally study the biological roles of both TFs of the PCTFP (Cyc8-Mot3)
Wickner RB, et al. (2012) Study of amyloids using yeast. Methods Mol Biol 849():321-46
Kitagaki H and Takagi H (2014) Mitochondrial metabolism and stress response of yeast: Applications in fermentation technologies. J Biosci Bioeng 117(4):383-393
Tuite MF (2015) Yeast prions: Paramutation at the protein level? Semin Cell Dev Biol 44():51-61
Du Z (2011) The complexity and implications of yeast prion domains. Prion 5(4):311-6
Zheng J, et al. (2010) Epistatic relationships reveal the functional organization of yeast transcription factors. Mol Syst Biol 6():420
Wickner RB, et al. (2010) The Relationship of Prions and Translation. Wiley Interdiscip Rev RNA 1(1):81-89
Kastaniotis AJ and Zitomer RS (2000) Rox1 mediated repression. Oxygen dependent repression in yeast. Adv Exp Med Biol 475():185-95
Crow ET and Li L (2011) Newly identified prions in budding yeast, and their possible functions. Semin Cell Dev Biol 22(5):452-9
Shorter J (2010) Emergence and natural selection of drug-resistant prions. Mol Biosyst 6(7):1115-30
Newby GA and Lindquist S (2013) Blessings in disguise: biological benefits of prion-like mechanisms. Trends Cell Biol 23(6):251-9
Wear MP, et al. (2015) Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates. PLoS One 10(8):e0136362
Chernova TA, et al. (2014) Physiological and environmental control of yeast prions. FEMS Microbiol Rev 38(2):326-44
Sertil O, et al. (2003) Synergistic repression of anaerobic genes by Mot3 and Rox1 in Saccharomyces cerevisiae. Nucleic Acids Res 31(20):5831-7
Wickner RB, et al. (2013) Viruses and prions of Saccharomyces cerevisiae. Adv Virus Res 86():1-36
Moosavi B, et al. (2016) Actin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in Yeast. Traffic 17(1):5-20
Alexandrov AI and Ter-Avanesyan MD (2013) Could yeast prion domains originate from polyQ/N tracts? Prion 7(3):209-14
Gatbonton T, et al. (2006) Telomere length as a quantitative trait: genome-wide survey and genetic mapping of telomere length-control genes in yeast. PLoS Genet 2(3):e35
Harbi D and Harrison PM (2014) Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation. PLoS One 9(6):e100615
Ter Linde JJ and Steensma HY (2003) Transcriptional regulation of YML083c under aerobic and anaerobic conditions. Yeast 20(5):439-54
Desimone AM and Laney JD (2010) Corepressor-directed preacetylation of histone h3 in promoter chromatin primes rapid transcriptional switching of cell-type-specific genes in yeast. Mol Cell Biol 30(13):3342-56
Lee SK, et al. (2010) Activation of a Poised RNAPII-Dependent Promoter Requires Both SAGA and Mediator. Genetics 184(3):659-72
Wickner RB, et al. (2015) Yeast prions: structure, biology, and prion-handling systems. Microbiol Mol Biol Rev 79(1):1-17
Tuite MF, et al. (2011) Fungal prions: structure, function and propagation. Top Curr Chem 305():257-98
Garcia DM and Jarosz DF (2014) Rebels with a cause: molecular features and physiological consequences of yeast prions. FEMS Yeast Res 14(1):136-47
Yu H and Gerstein M (2006) Genomic analysis of the hierarchical structure of regulatory networks. Proc Natl Acad Sci U S A 103(40):14724-31
An L, et al. (2016) Emergence and evolution of yeast prion and prion-like proteins. BMC Evol Biol 16(1):24
Kastaniotis AJ, et al. (2000) Roles of transcription factor Mot3 and chromatin in repression of the hypoxic gene ANB1 in yeast. Mol Cell Biol 20(19):7088-98
Abramova NE, et al. (2001) Regulatory mechanisms controlling expression of the DAN/TIR mannoprotein genes during anaerobic remodeling of the cell wall in Saccharomyces cerevisiae. Genetics 157(3):1169-77
Tuite MF (2013) The natural history of yeast prions. Adv Appl Microbiol 84():85-137
Wickner RB, et al. (2010) Prion amyloid structure explains templating: how proteins can be genes. FEMS Yeast Res 10(8):980-91
Alberti S, et al. (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137(1):146-58
Halfmann R, et al. (2010) Prions, protein homeostasis, and phenotypic diversity. Trends Cell Biol 20(3):125-133
Mennella TA, et al. (2003) Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-independent exclusion of TATA binding protein. Eukaryot Cell 2(6):1288-303
Sugiyama S and Tanaka M (2014) Self-propagating amyloid as a critical regulator for diverse cellular functions. J Biochem 155(6):345-51
Wickner RB and Kelly AC (2015) Prions are affected by evolution at two levels. Cell Mol Life Sci ()
Cascarina SM and Ross ED (2014) Yeast prions and human prion-like proteins: sequence features and prediction methods. Cell Mol Life Sci 71(11):2047-63
Li L and Kowal AS (2012) Environmental regulation of prions in yeast. PLoS Pathog 8(11):e1002973
Klinkenberg LG, et al. (2005) Combinatorial repression of the hypoxic genes of Saccharomyces cerevisiae by DNA binding proteins Rox1 and Mot3. Eukaryot Cell 4(4):649-60