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Amyloid Fibrils

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Related Experiment Video

Updated: May 11, 2026

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
09:27

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

α-Synuclein mutations cluster around a putative protein loop.

Eleanna Kara1, Patrick A Lewis, Helen Ling

  • 1Reta Lila Weston Research Laboratories, Department of Molecular Neuroscience, UCL Institute of Neurology, London WC1N 3BG, UK. eleannakara@gmail.com

Neuroscience Letters
|May 15, 2013
PubMed
Summary
This summary is machine-generated.

Researchers mapped five pathogenic mutations in alpha-synuclein (α-synuclein) protein structure. Four mutations align with a potential protein fold, while A30P mutation significantly alters protein structure, offering insights into disease mechanisms.

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Last Updated: May 11, 2026

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Published on: January 5, 2016

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons
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Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein
12:01

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Published on: May 30, 2015

Area of Science:

  • Structural biology
  • Neuroscience
  • Genetics

Background:

  • Alpha-synuclein (α-synuclein) is implicated in neurodegenerative diseases.
  • Pathogenic mutations in α-synuclein are key to understanding disease mechanisms.

Purpose of the Study:

  • To map known pathogenic mutations of α-synuclein onto structural models.
  • To investigate the structural implications of these mutations and their link to pathogenicity.

Main Methods:

  • Utilized available protein structure models for α-synuclein.
  • Mapped five identified pathogenic mutations onto these structural models.

Main Results:

  • Four of the five pathogenic mutations were localized to a potential fold within the α-synuclein structure.
  • The A30P mutation was identified as an exception, predicted to profoundly impact protein structure.

Conclusions:

  • The structural mapping provides a framework for understanding α-synuclein mutation pathogenicity.
  • Findings suggest distinct structural mechanisms for different α-synuclein mutations.