α-Synuclein phosphorylation as a therapeutic target in Parkinson’s disease

No abstract is available for this paper.

• Publication year

  2012

• Venue

  Reviews in the Neurosciences

• Publication date

  2012-04-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1515/revneuro-2011-0067PMID 22499677
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  2008cited by this paper
• LRRK2 is a component of granular alpha‐synuclein pathology in the brainstem of Parkinson's disease

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• Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations.

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• Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism.

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• Provided for Non-commercial Research and Educational Use Only. Not for Reproduction, Distribution or Commercial Use. Author's Personal Copy Role of Post-translational Modifications in Modulating the Structure, Function and Toxicity of A-synuclein: Implications for Parkinson's Disease Pathogenesis an

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