(Q44341966)

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The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils

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1 reference

Europe PubMed Central

2 December 2017

The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils (English)

1 reference

Europe PubMed Central

2 December 2017

4

object named as

Ronald Melki

1 reference

Europe PubMed Central

2 December 2017

author name string

Luc Bousset

1

1 reference

Europe PubMed Central

2 December 2017

Fatma Briki

2

1 reference

Europe PubMed Central

2 December 2017

Jean Doucet

3

1 reference

Europe PubMed Central

2 December 2017

publication date

1 February 2003

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Europe PubMed Central

2 December 2017

Journal of Structural Biology

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Europe PubMed Central

2 December 2017

141

1 reference

Europe PubMed Central

2 December 2017

2

1 reference

Europe PubMed Central

2 December 2017

132-142

1 reference

Europe PubMed Central

2 December 2017

An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid

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Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix

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Identification, characterization, and crystal structure of the Omega class glutathione transferases

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Identification of a protein that purifies with the scrapie prion.

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

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Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds

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Similar and divergent features in mammalian and yeast prions

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The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Conformational changes and disease--serpins, prions and Alzheimer's.

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Ψ, A cytoplasmic suppressor of super-suppressor in yeast

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

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Protein misfolding, evolution and disease

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The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments

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The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele

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Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae.

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Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing

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The protofilament structure of insulin amyloid fibrils

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Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro

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Is Congo red an amyloid-specific dye?

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X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation

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Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain

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Betabellins 15D and 16D, de Novo Designed β-Sandwich Proteins That Have Amyloidogenic Properties

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Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells

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Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro

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Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants.

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Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques.

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

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Identifiers

10.1016/S1047-8477(02)00606-8

1 reference

Europe PubMed Central

2 December 2017

1 reference

Europe PubMed Central

2 December 2017

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