Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: a quantitative analysis of the effects of pH and buffer system (Q44395829)

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scientific article published in April 2003

Language	Label	Description	Also known as
English	Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: a quantitative analysis of the effects of pH and buffer system	scientific article published in April 2003

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: a quantitative analysis of the effects of pH and buffer system (English)

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Europe PubMed Central

PubMed publication ID

2 December 2017

prion protein family

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author name string

Li Zhu

1

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Europe PubMed Central

PubMed publication ID

2 December 2017

Xu-Jia Zhang

2

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Europe PubMed Central

PubMed publication ID

2 December 2017

Ling-Yun Wang

3

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Europe PubMed Central

PubMed publication ID

2 December 2017

Jun-Mei Zhou

4

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2 December 2017

Sarah Perrett

5

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Europe PubMed Central

PubMed publication ID

2 December 2017

language of work or name

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publication date

1 April 2003

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Europe PubMed Central

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2 December 2017

Journal of Molecular Biology

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Europe PubMed Central

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2 December 2017

328

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Europe PubMed Central

PubMed publication ID

2 December 2017

1

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Europe PubMed Central

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2 December 2017

235-254

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Europe PubMed Central

PubMed publication ID

2 December 2017

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

1 reference

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1 reference

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

1 reference

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The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation

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Prion domain initiation of amyloid formation in vitro from native Ure2p

1 reference

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

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

1 reference

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The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases

1 reference

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

1 reference

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Equilibrium folding properties of the yeast prion protein determinant Ure2

1 reference

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Pressure denaturation of the yeast prion protein Ure2.

1 reference

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Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p

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Folding of the yeast prion protein Ure2: kinetic evidence for folding and unfolding intermediates

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

1 reference

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Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt

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Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure

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Equilibrium dissociation and unfolding of the Arc repressor dimer

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Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation

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Dimeric tyrosyl-tRNA synthetase from Bacillus stearothermophilus unfolds through a monomeric intermediate. A quantitative analysis under equilibrium conditions

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Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1.

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Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism

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Kinetic role of early intermediates in protein folding

1 reference

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7 January 2021

Multiple intermediates and transition states during protein unfolding

1 reference

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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2

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Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?

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Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins

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Mechanisms of amyloidogenesis

1 reference

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7 January 2021

Nucleated conformational conversion and the replication of conformational information by a prion determinant

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Self-replication and scrapie

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Kinetic analysis of amyloid fibril formation

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Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces

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Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH.

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Amyloid fibrillogenesis: themes and variations

1 reference

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Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein

1 reference

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7 January 2021

Prion filament networks in [URE3] cells of Saccharomyces cerevisiae

1 reference

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7 January 2021

Two prion-inducing regions of Ure2p are nonoverlapping

1 reference

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7 January 2021

Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor.

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Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate

1 reference

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Protein Denaturation

2 references

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7 January 2021

based on heuristic

inferred from DOI database lookup

Equilibrium dissociation and unfolding of the dimeric human papillomavirus strain-16 E2 DNA-binding domain

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Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation

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The prion domain of yeast Ure2p induces autocatalytic formation of amyloid fibers by a recombinant fusion protein

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7 January 2021

Identifiers

10.1016/S0022-2836(03)00249-3

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

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