(Q48668545)

14 February 2018

title

Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure. (English)

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14 February 2018

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6

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14 February 2018

Jean-Marie Ruysschaert

5

object named as

Jean-Marie Ruysschaert

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14 February 2018

Erik Goormaghtigh

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object named as

Erik Goormaghtigh

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14 February 2018

author name string

María Soledad Celej

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14 February 2018

Rabia Sarroukh

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14 February 2018

Gerardo D Fidelio

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14 February 2018

language of work or name

English

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publication date

1 May 2012

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14 February 2018

published in

Biochemical Journal

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14 February 2018

volume

443

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14 February 2018

issue

3

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14 February 2018

page(s)

719-726

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14 February 2018

Protein misfolding, functional amyloid, and human disease

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Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein

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

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21 January 2018

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21 January 2018

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21 January 2018

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

21 January 2018

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Characterization of alpha-synuclein interactions with selected aggregation-inhibiting small molecules

21 January 2018

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21 January 2018

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Structural and mechanistic basis behind the inhibitory interaction of PcTS on alpha-synuclein amyloid fibril formation

21 January 2018

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Characterization of oligomers during alpha-synuclein aggregation using intrinsic tryptophan fluorescence

21 January 2018

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Pore-forming proteins share structural and functional homology with amyloid oligomers

21 January 2018

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Structural properties of pore-forming oligomers of alpha-synuclein

21 January 2018

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21 January 2018

Identifiers

DOI

10.1042/BJ20111924

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14 February 2018

PubMed ID

22316405

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14 February 2018