A minimal conformational switching-dependent model for amyloid self-assembly.

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Kinetics of spontaneous filament nucleation via oligomers: Insights from theory and simulation.Imaging Aβ(1-42) fibril elongation reveals strongly polarised growth and growth incompetent states.

P2860

Q42697772-E4AFBFC5-3BDD-4579-A77B-8D314E4FF145 Q47449222-C63C33A0-9A84-4FF5-A70B-D2A715E3BA83

P2860

A minimal conformational switching-dependent model for amyloid self-assembly.

Item

http://www.wikidata.org/entity/Q38528499

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

A minimal conformational switching-dependent model for amyloid self-assembly.

@en

type

Item

label

A minimal conformational switching-dependent model for amyloid self-assembly.

@en

prefLabel

A minimal conformational switching-dependent model for amyloid self-assembly.

@en

P1476

A minimal conformational switching-dependent model for amyloid self-assembly

@en

P2093

Dhiman Ghosh

http://www.w3.org/2001/XMLSchema#string

Ranjith Padinhateeri

http://www.w3.org/2001/XMLSchema#string

P2860

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

Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils

Protein misfolding, functional amyloid, and human disease

Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.

Amyloid fibril formation by an SH3 domain.

Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity.

Direct measurement of force generation by actin filament polymerization using an optical trap

Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: the Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth.

Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.

Fitting yeast and mammalian prion aggregation kinetic data with the Finke-Watzky two-step model of nucleation and autocatalytic growth.

P2888

srep21103

P304

21103

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1038/SREP21103

http://www.w3.org/2001/XMLSchema#string

P407

English

P478

http://www.w3.org/2001/XMLSchema#string

P50

Srivastav Ranganathan

Samir K Maji

P577

2016-02-17T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

294884081

http://www.w3.org/2001/XMLSchema#string

P6179

1011244223

http://www.w3.org/2001/XMLSchema#string

P698

26883720

http://www.w3.org/2001/XMLSchema#string

P921

self-assembly

P932

4756677

http://www.w3.org/2001/XMLSchema#string

A minimal conformational switching-dependent model for amyloid self-assembly.

about

P2860

P2860

A minimal conformational switching-dependent model for amyloid self-assembly.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P5875

P6179

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P5875

P6179

P698

P921

P932