Kinetics of amyloid aggregation: a study of the GNNQQNY prion sequence (Q34499321)

2 August 2017

Kinetics of amyloid aggregation: a study of the GNNQQNY prion sequence (English)

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2 August 2017

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2

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author name string

Jessica Nasica-Labouze

series ordinal

1

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2 August 2017

29 November 2012

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PLOS Computational Biology

2 August 2017

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2 August 2017

8

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2 August 2017

11

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2 August 2017

e1002782

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Creative Commons Attribution 4.0 International

2 August 2017

start time

29 November 2012

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

A variational model for oligomer-formation process of GNNQQNY peptide from yeast prion protein Sup35

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A multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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

7 July 2018

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

7 July 2018

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Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism

7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants

7 July 2018

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7 July 2018

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The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease

7 July 2018

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7 July 2018

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Conversion of non-fibrillar beta-sheet oligomers into amyloid fibrils in Alzheimer's disease amyloid peptide aggregation

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12 December 2020

The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease?

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Multiple assembly pathways underlie amyloid-beta fibril polymorphisms

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Amyloid fibril polymorphism is under kinetic control

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Stability of single sheet GNNQQNY aggregates analyzed by replica exchange molecular dynamics: Antiparallel versus parallel association

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Thermodynamics and Kinetics of Aggregation for the GNNQQNY Peptide

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Identifiers

DOI

1 reference

journals/ploscb/Nasica-LabouzeM12

2 August 2017

1 reference

DBLP Dataset 2021-01-02

28 January 2021

1 reference

2 August 2017

1 reference

PubMed ID

23209391