Prion properties of the Sup35 protein of yeast Pichia methanolica. - Wikidata - awgldk - TriplyDB

Prion properties of the Sup35 protein of yeast Pichia methanolica.

Prion properties of the Sup35 protein of yeast Pichia methanolica.

http://www.wikidata.org/entity/Q34661848

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Prions, protein homeostasis, and phenotypic diversity The strength of selection against the yeast prion [PSI+]A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions The conversion of 3' UTRs into coding regions Dissection and design of yeast prions The yeast prions [PSI+] and [URE3] are molecular degenerative diseases Yeast prions: structure, biology, and prion-handling systems Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.Heterologous cross-seeding mimics cross-species prion conversion in a yeast model.Prion amyloid structure explains templating: how proteins can be genes.N-terminal region of Saccharomyces cerevisiae eRF3 is essential for the functioning of the eRF1/eRF3 complex beyond translation termination.A novel mutant of the Sup35 protein of Saccharomyces cerevisiae defective in translation termination and in GTPase activity still supports cell viability.Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.Genetic interactions between [PSI+] and nonstop mRNA decay affect phenotypic variation [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.Induction of distinct [URE3] yeast prion strains.Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo.Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104.Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation.Sporadic distribution of prion-forming ability of Sup35p from yeasts and fungi.Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein.Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]The [PSI+] prion exists as a dynamic cloud of variants Evolutionary capacitance may be favored by natural selection.The [URE3] prion is not conserved among Saccharomyces species Radically different amyloid conformations dictate the seeding specificity of a chimeric Sup35 prion.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.Newly identified prions in budding yeast, and their possible functions.The sensitive [SWI (+)] prion: new perspectives on yeast prion diversity.Propagation of yeast prions.Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104).Prion species barrier between the closely related yeast proteins is detected despite coaggregation.[PSI+] Prion transmission barriers protect Saccharomyces cerevisiae from infection: intraspecies 'species barriers'.Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+].A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast.

P2860

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P2860

Prion properties of the Sup35 protein of yeast Pichia methanolica.

http://www.wikidata.org/entity/Q34661848

description

2000 nî lūn-bûn

@nan

2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

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2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

Prion properties of the Sup35 protein of yeast Pichia methanolica.

@ast

Prion properties of the Sup35 protein of yeast Pichia methanolica.

@en

Prion properties of the Sup35 protein of yeast Pichia methanolica.

@nl

type

label

Prion properties of the Sup35 protein of yeast Pichia methanolica.

@ast

Prion properties of the Sup35 protein of yeast Pichia methanolica.

@en

Prion properties of the Sup35 protein of yeast Pichia methanolica.

@nl

prefLabel

Prion properties of the Sup35 protein of yeast Pichia methanolica.

@ast

Prion properties of the Sup35 protein of yeast Pichia methanolica.

@en

Prion properties of the Sup35 protein of yeast Pichia methanolica.

@nl

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P1433

The EMBO Journal

P1476

Prion properties of the Sup35 protein of yeast Pichia methanolica.

@en

P2093

Chechenova MB

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Frolova NS

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Kochneva-Pervukhova NV

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Kushnirov VV

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Ter-Avanesyan MD

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P2860

Prion Protein Biology

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

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

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

The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae

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

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation.

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.

P304

324-331

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scholarly article

P356

10.1093/EMBOJ/19.3.324

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P407

P433

3

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P478

19

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P577

2000-02-01T00:00:00Z

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P5875

12659729

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P698

10654931

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P921

Prion protein family

P932

305569

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