Optical structural analysis of individual α-synuclein oligomers.

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Optical structural analysis of individual α-synuclein oligomers.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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Optical structural analysis of individual α-synuclein oligomers.

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Optical structural analysis of individual α-synuclein oligomers.

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Optical structural analysis of individual α-synuclein oligomers.

@en

Optical structural analysis of individual α-synuclein oligomers.

@nl

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Optical Structural Analysis of Individual α‐Synuclein Oligomers

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Optical structural analysis of individual α-synuclein oligomers.

@en

Optical structural analysis of individual α-synuclein oligomers.

@nl

P1476

Optical structural analysis of individual α-synuclein oligomers.

@en

P2860

Molecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-Assemblies

Minimalist design of water-soluble cross-beta architecture.

Alpha-synuclein in Lewy bodies

Protein misfolding, functional amyloid, and human disease

Multi-dimensional super-resolution imaging enables surface hydrophobicity mapping.

The binding of thioflavin-T to amyloid fibrils: localisation and implications.

Direct observation of the interconversion of normal and toxic forms of α-synuclein

Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.

The structural basis for optimal performance of oligothiophene-based fluorescent amyloid ligands: conformational flexibility is essential for spectral assignment of a diversity of protein aggregates.

Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregation

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4886-4890

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scholarly article

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10.1002/ANIE.201710779

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1738c44b723cab2728d51650b0aa41dc4c750ee4

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English

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2018-03-23T00:00:00Z

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29342318

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P921

Synuclein

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5988047

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