A yeast prion provides a mechanism for genetic variation and phenotypic diversity

By H. True, Susan Lindquist. Nature, 2000

692 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/76979ce64f26a763bf02754154fddbcea081ef31

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Citations in the corpus

Sequencing and comparison of yeast species to identify genes and regulatory elements (2003, background): “They also include the loss and gain of stop codons (by a nucleotide substitution or a frame-shifting indel), which may result in the rapid change of protein segments or the translation of previously non-coding region”
A systematic survey identifies prions and illuminates sequence features of prionogenic proteins (2009, background): “All known prions, except for the initially discovered disease-causing prion PrP, are benign, and in some cases can confer selectable advantages (Saupe et al., 2000; True and Lindquist, 2000; True et al., 2004).”
The 'evolvability' of promiscuous protein functions (2005, background): “For example, the rates and patterns of genetic and phenotypic variability may vary with the severity of the selection pressur”
Distinct tau prion strains propagate in cells and mice and define different tauopathies (2014, background): “In contrast, yeast prions are adaptive and confer phenotypic diversity and rapid evolution of new traits in times of stress (True and Lindquist, 2000).”
Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. (2008, background): “…behavioral phenotypes associated with neurodegenerative disease in the model systems of S. cerevisiae, C. elegans, and Drosophilia melanogaster (Warrick et al. 1998; Faber et al. 1999; Feany and Bender 2000; Krobitsch and Lindquist 2000; Satyal et al. 2000; Parker et al. 2001; Morley et al. 2002).”
Extended Phenotypes and Extended Organisms (2004, background): “Metastable proteins, like prions and prion-like proteins, embody a sort of heritable memory that can, as in the prion-like transcription factors of yeast, even specify the nature of genes (Prusiner 1998; Wickner and Taylor et al. 1999; True and Lindquist 2000).”
Protein folding and misfolding (2003, background): “Nevertheless, there is increasing evidence that the unique properties of amyloid structures have been exploited by some species, including bacteria, fungi and even mammals, for specific (and carefully regulated) purpose”
Functional amyloid--from bacteria to humans. (2007, background): “In addition, yeast populations harboring the aggregated form of Sup35p have selective growth advantages under some conditions [16,33, 43 ].”
Robustness and Evolvability (2010, background): “An empirical low recombination model capacitor system for which post-mutation evolvability might be important is the yeast prion [PSI+] [29, 46–48].”
The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease (2012, background): “These phenotypes can be advantageous, benign or deleterious depending on the genetic background and environmental conditions (Alberti et al., 2009; Eaglestone et al., 1999; McGlinchey et al., 2011; Nakayashiki et al., 2005; Namy et al., 2008; True and Lindquist, 2000; True et al., 2004).”