Yeast prions [URE3] and [PSI+] are diseases - Wikidata - awgldk - TriplyDB

Yeast prions [URE3] and [PSI+] are diseases

Yeast prions [URE3] and [PSI+] are diseases

http://www.wikidata.org/entity/Q24532887

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Prion switching in response to environmental stress Complex adaptations can drive the evolution of the capacitor [PSI], even with realistic rates of yeast sex The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system The loss of adaptive plasticity during long periods of environmental stasis Prions, protein homeostasis, and phenotypic diversity The strength of selection against the yeast prion [PSI+]Amyloids: friend or foe?A heritable switch in carbon source utilization driven by an unusual yeast prion A systematic survey identifies prions and illuminates sequence features of prionogenic proteins Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease The yeast prions [PSI+] and [URE3] are molecular degenerative diseases Potential roles for prions and protein-only inheritance in cancer Yeast prions and human prion-like proteins: sequence features and prediction methods Yeast prions: structure, biology, and prion-handling systems The [RNQ+] prion: a model of both functional and pathological amyloid Strategies for identifying new prions in yeast The Sua5 protein is essential for normal translational regulation in yeast.Rebels with a cause: molecular features and physiological consequences of yeast prions A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress Screening for toxic amyloid in yeast exemplifies the role of alternative pathway responsible for cytotoxicity Prion amyloid structure explains templating: how proteins can be genes.The expanding universe of prion diseases.Prions, amyloids, and RNA: Pieces of a puzzle.The number and transmission of [PSI] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae.Heterologous prion interactions are altered by mutations in the prion protein Rnq1p.Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1.Pathogenic polyglutamine tracts are potent inducers of spontaneous Sup35 and Rnq1 amyloidogenesis.Compositional determinants of prion formation in yeast Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion Normal levels of the antiprion proteins Btn2 and Cur1 cure most newly formed [URE3] prion variants The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-β structure: evidence from solid-state NMR.Effect of domestication on the spread of the [PIN+] prion in Saccharomyces cerevisiae.[KIL-d] Protein Element Confers Antiviral Activity via Catastrophic Viral Mutagenesis.Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation.Viruses and prions of Saccharomyces cerevisiae Assessment of inactivating stop codon mutations in forty Saccharomyces cerevisiae strains: implications for [PSI] prion- mediated phenotypes.PrionHome: a database of prions and other sequences relevant to prion phenomena.Genomic clustering and homology between HET-S and the NWD2 STAND protein in various fungal genomes Prions are a common mechanism for phenotypic inheritance in wild yeasts.The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.

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P2860

Yeast prions [URE3] and [PSI+] are diseases

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2005年の論文

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Yeast prions [URE3] and [PSI+] are diseases

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Yeast prions [URE3] and [PSI+] are diseases

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Proceedings of the National Academy of Sciences of the United States of America

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Yeast prions [URE3] and [PSI+] are diseases

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Cletus P Kurtzman

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Herman K Edskes

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Toru Nakayashiki

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P2860

Selfish DNA: a sexually-transmitted nuclear parasite.

Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae

Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor

Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast

The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog

Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae

Prions affect the appearance of other prions: the story of [PIN(+)].

Getting started with yeast

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

[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae

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10575-80

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scholarly article

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4315042

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10.1073/PNAS.0504882102

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30

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102

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7719565

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16024723

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Prion protein family

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1180808

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