(Q46703068)

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Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases

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Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases (English)

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Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

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Hisashi Yagi

1

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

Eiko Kusaka

2

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Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

Kunihiro Hongo

3

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Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

Tomohiro Mizobata

4

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Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

Yasushi Kawata

5

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Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

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14 September 2005

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Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

280

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Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

46

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Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

38609-38616

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

Neurodegenerative disorders of protein aggregation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Conformational disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

The structural basis of protein folding and its links with human disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Amyloid fibrils from the viewpoint of protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Conformational constraints for amyloid fibrillation: the importance of being unfolded

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Biochemical characterization of the core structure of alpha-synuclein filaments

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Pesticides directly accelerate the rate of alpha-synuclein fibril formation: a possible factor in Parkinson's disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Trimethylamine-N-oxide-induced folding of alpha-synuclein.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Evidence for a partially folded intermediate in alpha-synuclein fibril formation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Nitration inhibits fibrillation of human α‐synuclein in vitro by formation of soluble oligomers

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Alpha-synuclein and Parkinson's disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Tau and alpha-synuclein pathology in amygdala of Parkinsonism-dementia complex patients of Guam

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Alpha-synuclein, Abeta and Alzheimer's disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

The relationship between amyloid and tau.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Amyloid-like fibril formation of co-chaperonin GroES: nucleation and extension prefer different degrees of molecular compactness.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

The protofilament structure of insulin amyloid fibrils

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Alpha-synuclein in Lewy bodies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Dependence of alpha-synuclein aggregate morphology on solution conditions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Strong growth polarity of yeast prion fiber revealed by single fiber imaging

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Protein misfolding, evolution and disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Structure of the cross-beta spine of amyloid-like fibrils

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Correlation of structural elements and infectivity of the HET-s prion

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Protein folding and misfolding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Tubulin seeds alpha-synuclein fibril formation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Seeding specificity in amyloid growth induced by heterologous fibrils

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Seeding-dependent maturation of beta2-microglobulin amyloid fibrils at neutral pH.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Main-chain dominated amyloid structures demonstrated by the effect of high pressure

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Stimulation of insulin fibrillation by urea-induced intermediates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Conformational variations in an infectious protein determine prion strain differences

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Generation of prion transmission barriers by mutational control of amyloid conformations

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

The structure of amyloid fibrils by electron microscopy and X-ray diffraction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

In-situ atomic force microscopy study of β-amyloid fibrillization

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508623200

21 January 2018

Identifiers

10.1074/JBC.M508623200

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 December 2017

http://europepmc.org/abstract/MED/16162499

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