(Q44840918)

6 December 2017

title

Simulation studies on the stabilities of aggregates formed by fibril-forming segments of alpha-Synuclein (English)

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6 December 2017

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Jeseong Yoon

1

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6 December 2017

Soonmin Jang

series ordinal

2

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6 December 2017

Kyunghee Lee

series ordinal

3

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6 December 2017

Seokmin Shin

series ordinal

4

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6 December 2017

publication date

1 December 2009

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Journal of Biomolecular Structure and Dynamics

6 December 2017

published in

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6 December 2017

volume

27

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6 December 2017

issue

3

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6 December 2017

page(s)

259-270

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Protein folding and misfolding

6 December 2017

cites work

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Intrinsically disordered protein

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

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

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

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

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A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein

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Investigation of alpha-synuclein fibril structure by site-directed spin labeling

21 January 2018

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Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy

21 January 2018

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Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems

21 January 2018

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10.1080/07391102.2009.10507314

21 January 2018

Identifiers

DOI

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6 December 2017

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