Prion amyloid structure explains templating: how proteins can be genes. - Wikidata - awgldk - TriplyDB

Prion amyloid structure explains templating: how proteins can be genes.

Prion amyloid structure explains templating: how proteins can be genes.

http://www.wikidata.org/entity/Q30392820

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The complexity and implications of yeast prion domains Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.[PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain.Viruses and prions of Saccharomyces cerevisiae Assessment of inactivating stop codon mutations in forty Saccharomyces cerevisiae strains: implications for [PSI] prion- mediated phenotypes.Physical and structural basis for polymorphism in amyloid fibrils Prion diseases of yeast: amyloid structure and biology.Molecular chaperone Hsp104 can promote yeast prion generation Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel β-sheet structure.Amyloid polymorphism: structural basis and neurobiological relevance.Prion protein at the crossroads of physiology and disease.[PSI+] Prion transmission barriers protect Saccharomyces cerevisiae from infection: intraspecies 'species barriers'.Discovering protein-based inheritance through yeast genetics.Host Determinants of Prion Strain Diversity Independent of Prion Protein Genotype.Prions in yeast.Solvent-induced tuning of internal structure in a protein amyloid protofibril.Sex, prions, and plasmids in yeast.Computational modeling of the relationship between amyloid and disease.The ZIP-prion connection Molecular structures of amyloid and prion fibrils: consensus versus controversy FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis.The yeast prion protein Ure2: insights into the mechanism of amyloid formation.Modeling ALS and FTLD proteinopathies in yeast: an efficient approach for studying protein aggregation and toxicity.The contribution of different prion protein types and host polymorphisms to clinicopathological variations in Creutzfeldt-Jakob disease.Human prion diseases: molecular, cellular and population biology.Yeast and Fungal Prions.SUP35 expression is enhanced in yeast containing [ISP+], a prion form of the transcriptional regulator Sfp1.Reconstructing the fungal tree of life using phylogenomics and a preliminary investigation of the distribution of yeast prion-like proteins in the fungal kingdom.Septin-containing barriers control the differential inheritance of cytoplasmic elements.Functional amyloids: interrelationship with other amyloids and therapeutic assessment to treat neurodegenerative diseases.Allelic variants of hereditary prions: The bimodularity principle.Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities.What Does Solid-State NMR Tell Us about Amyloid Structures?

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P2860

Prion amyloid structure explains templating: how proteins can be genes.

http://www.wikidata.org/entity/Q30392820

description

2010 nî lūn-bûn

@nan

2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

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2010年论文

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name

Prion amyloid structure explains templating: how proteins can be genes.

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Prion amyloid structure explains templating: how proteins can be genes.

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Prion amyloid structure explains templating: how proteins can be genes.

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Prion amyloid structure explains templating: how proteins can be genes.

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Prion amyloid structure explains templating: how proteins can be genes.

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Prion amyloid structure explains templating: how proteins can be genes.

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J.1567-1364.2010.00666.X

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FEMS Yeast Research

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Prion amyloid structure explains templating: how proteins can be genes.

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Chia-Lin Winchester

http://www.w3.org/2001/XMLSchema#string

David Bateman

http://www.w3.org/2001/XMLSchema#string

Dmitry Kryndushkin

http://www.w3.org/2001/XMLSchema#string

Frank Shewmaker

http://www.w3.org/2001/XMLSchema#string

Herman Edskes

http://www.w3.org/2001/XMLSchema#string

Julie Nemecek

http://www.w3.org/2001/XMLSchema#string

Ryan McGlinchey

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P2860

Prion switching in response to environmental stress

Amyloid aggregates of the HET-s prion protein are infectious.

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

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

Structure of the cross-beta spine of amyloid-like fibrils

Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast

Generating a prion with bacterially expressed recombinant prion protein.

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

Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure

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20726897

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Prion protein family

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