(Q42022717)

English

Concentration dependence of alpha-synuclein fibril length assessed by quantitative atomic force microscopy and statistical-mechanical theory

scientific article published on August 2008

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

Concentration dependence of alpha-synuclein fibril length assessed by quantitative atomic force microscopy and statistical-mechanical theory (English)

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

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Martijn E van Raaij

1

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

Jeroen van Gestel

2

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

Ine M J Segers-Nolten

3

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

Simon W de Leeuw

4

1 reference

Europe PubMed Central

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15 October 2017

Vinod Subramaniam

5

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Europe PubMed Central

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15 October 2017

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publication date

1 August 2008

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Europe PubMed Central

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15 October 2017

Biophysical Journal

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Europe PubMed Central

PMC publication ID

15 October 2017

95

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Europe PubMed Central

PMC publication ID

15 October 2017

10

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

4871-4878

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

describes a project that uses

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2576393/fullTextXML

based on heuristic

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AFM study of glucagon fibrillation via oligomeric structures resulting in interwoven fibrils

1 reference

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Conformational equilibria in monomeric alpha-synuclein at the single-molecule level

1 reference

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Protein aggregation processes: In search of the mechanism

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Polymorphism in the intermediates and products of amyloid assembly

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Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from alpha-synuclein mutants

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A statistical-mechanical theory of fibril formation in dilute protein solutions

1 reference

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Early events in insulin fibrillization studied by time-lapse atomic force microscopy

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Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy

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alpha-Synuclein locus triplication causes Parkinson's disease

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Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities

1 reference

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A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy

1 reference

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Alpha-synuclein and neurodegenerative diseases

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A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro

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Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation

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Average protein density is a molecular-weight-dependent function.

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The effect of macromolecular crowding on protein aggregation and amyloid fibril formation

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17 August 2018

Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy

1 reference

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Dependence of alpha-synuclein aggregate morphology on solution conditions

1 reference

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Glial cell death induced by overexpression of alpha-synuclein

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Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease?

1 reference

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Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy

1 reference

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12 December 2020

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Enhancement of Protein Crystal Nucleation by Critical Density Fluctuations

1 reference

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Reversible mechanical unzipping of amyloid beta-fibrils

1 reference

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inferred from PubMed ID database lookup

Quantitative characterization of protein nanostructures using atomic force microscopy

1 reference

https://pubmed.ncbi.nlm.nih.gov/18676659

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1529/BIOPHYSJ.107.127464

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

ResearchGate publication ID

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