(Q34602533)

3 August 2017

Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation (English)

1 reference

3 August 2017

1 reference

1 reference

Bente Vestergaard

4

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Daniel Otzen

object named as

Daniel E Otzen

series ordinal

3

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Dmitri Svergun

object named as

Dmitri I Svergun

series ordinal

2

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author name string

Lise Giehm

series ordinal

1

1 reference

PubMed ID

21300904

3 August 2017

language of work or name

English

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publication date

7 February 2011

1 reference

Proceedings of the National Academy of Sciences of the United States of America

3 August 2017

6

1 reference

based on heuristic

inferred from page(s)

published in

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3 August 2017

108

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3 August 2017

8

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3 August 2017

3246-3251

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Strategies to increase the reproducibility of protein fibrillization in plate reader assays

3 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

Granular assembly of alpha-synuclein leading to the accelerated amyloid fibril formation with shear stress

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

The aggregation and fibrillation of alpha-synuclein

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration".

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

Methionine oxidation, alpha-synuclein and Parkinson's disease

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils.

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

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

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3044375

Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism.

7 July 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

Different species of alpha-synuclein oligomers induce calcium influx and seeding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

A SAXS study of glucagon fibrillation

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

SDS-induced fibrillation of alpha-synuclein: an alternative fibrillation pathway.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

PRIMUS: a Windows PC-based system for small-angle scattering data analysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

Alpha-synuclein: stable compact and extended monomeric structures and pH dependence of dimer formation

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

Neurodegenerative disease: amyloid pores from pathogenic mutations.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

The structure of dopamine induced alpha-synuclein oligomers.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

A new method for purification of recombinant human alpha-synuclein in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

Kinetic partitioning between aggregation and vesicle permeabilization by modified ADan

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1013225108

21 January 2018

Identifiers

DOI

10.1073/PNAS.1013225108

1 reference

3 August 2017

0 references

1 reference

3 August 2017

1 reference

PubMed ID

21300904