Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein. - Wikidata - awgldk - TriplyDB

Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein.

Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein.

http://www.wikidata.org/entity/Q34443813

about

Yeast prions [URE3] and [PSI+] are diseases The yeast prions [PSI+] and [URE3] are molecular degenerative diseases Yeast prions: structure, biology, and prion-handling systems A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structure Heterologous cross-seeding mimics cross-species prion conversion in a yeast model.Prion amyloid structure explains templating: how proteins can be genes.Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.Characterization of an Nmr homolog that modulates GATA factor-mediated nitrogen metabolite repression in Cryptococcus neoformans.Sporadic distribution of prion-forming ability of Sup35p from yeasts and fungi.Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability The [URE3] prion is not conserved among Saccharomyces species Relationship between prion propensity and the rates of individual molecular steps of fibril assembly.Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.Prion diseases of yeast: amyloid structure and biology.Prion-forming ability of Ure2 of yeasts is not evolutionarily conserved.Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel β-sheet structure.Prion species barrier between the closely related yeast proteins is detected despite coaggregation.Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae.Prions in yeast.Study of amyloids using yeast Prions are affected by evolution at two levels Prions of fungi: inherited structures and biological roles The [URE3] prion in Candida.Prion-prion interactions Prion variants and species barriers among Saccharomyces Ure2 proteins.Recent advances in nitrogen regulation: a comparison between Saccharomyces cerevisiae and filamentous fungi The cellular concentration of the yeast Ure2p prion protein affects its propagation as a prion Disulfide bond formation significantly accelerates the assembly of Ure2p fibrils because of the proximity of a potential amyloid stretch.The story of stolen chaperones: how overexpression of Q/N proteins cures yeast prions.The yeast prion protein Ure2: insights into the mechanism of amyloid formation.Yeast and Fungal Prions.A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates.Conservation of the prion properties of Ure2p through evolution.The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products.Architecture of Ure2p prion filaments: the N-terminal domains form a central core fiber.Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission.The [PSI+] prion of Saccharomyces cerevisiae can be propagated by an Hsp104 orthologue from Candida albicans.Amyloid diseases of yeast: prions are proteins acting as genes.

P2860

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P2860

Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein.

http://www.wikidata.org/entity/Q34443813

description

2002 nî lūn-bûn

@nan

2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

name

Conservation of a portion of t ...... with the full-length protein.

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Conservation of a portion of t ...... with the full-length protein.

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Conservation of a portion of t ...... with the full-length protein.

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type

label

Conservation of a portion of t ...... with the full-length protein.

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Conservation of a portion of t ...... with the full-length protein.

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Conservation of a portion of t ...... with the full-length protein.

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prefLabel

Conservation of a portion of t ...... with the full-length protein.

@ast

Conservation of a portion of t ...... with the full-length protein.

@en

Conservation of a portion of t ...... with the full-length protein.

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P1433

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P1433

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

P1476

Conservation of a portion of t ...... with the full-length protein.

@en

P2093

Herman K Edskes

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P2860

The genome sequence of Schizosaccharomyces pombe

Transmission of prions

Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast

The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p

Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae

The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors.

Getting started with yeast

Multifunctional yeast high-copy-number shuttle vectors

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

Mice devoid of PrP are resistant to scrapie

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16384-16391

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scholarly article

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10.1073/PNAS.162349599

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P478

99 Suppl 4

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2002-08-12T00:00:00Z

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Prion protein family

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139898

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