α-Synuclein aggregation and modulating factors.

Katerina E. Paleologou, Omar Ali El-Agnaf

Research output: Contribution to journalReview article

14 Citations (Scopus)

Abstract

Aggregated a-synuclein is the major component of inclusions in Parkinson's disease and other synucleinopathy brains indicating that a-syn aggregation is associated with the pathogenesis of neurodegenerative disorders. Although the mechanisms underlying a-syn aggregation and toxicity are not fully elucidated, it is clear that a-syn undergoes post-translational modifications and interacts with numerous proteins and other macromolecules, metals, hormones, neurotransmitters, drugs and poisons that can all modulate its aggregation propensity. The current and most recent findings regarding the factors modulating a-syn aggregation process are discussed in detail.

Original languageEnglish
Pages (from-to)109-164
Number of pages56
JournalSub-Cellular Biochemistry
Volume65
Publication statusPublished - 2012
Externally publishedYes

Fingerprint

Synucleins
Poisons
Post Translational Protein Processing
Neurodegenerative Diseases
Neurotransmitter Agents
Parkinson Disease
Agglomeration
Metals
Hormones
Brain
Pharmaceutical Preparations
Proteins
Macromolecules
Toxicity
cell aggregation factors

ASJC Scopus subject areas

  • Medicine(all)

Cite this

α-Synuclein aggregation and modulating factors. / Paleologou, Katerina E.; Ali El-Agnaf, Omar.

In: Sub-Cellular Biochemistry, Vol. 65, 2012, p. 109-164.

Research output: Contribution to journalReview article

@article{2a2a8f0f15cc4135b6212d44adadac70,
title = "α-Synuclein aggregation and modulating factors.",
abstract = "Aggregated a-synuclein is the major component of inclusions in Parkinson's disease and other synucleinopathy brains indicating that a-syn aggregation is associated with the pathogenesis of neurodegenerative disorders. Although the mechanisms underlying a-syn aggregation and toxicity are not fully elucidated, it is clear that a-syn undergoes post-translational modifications and interacts with numerous proteins and other macromolecules, metals, hormones, neurotransmitters, drugs and poisons that can all modulate its aggregation propensity. The current and most recent findings regarding the factors modulating a-syn aggregation process are discussed in detail.",
author = "Paleologou, {Katerina E.} and {Ali El-Agnaf}, Omar",
year = "2012",
language = "English",
volume = "65",
pages = "109--164",
journal = "Sub-Cellular Biochemistry",
issn = "0306-0225",
publisher = "Plenum Publishers",

}

TY - JOUR

T1 - α-Synuclein aggregation and modulating factors.

AU - Paleologou, Katerina E.

AU - Ali El-Agnaf, Omar

PY - 2012

Y1 - 2012

N2 - Aggregated a-synuclein is the major component of inclusions in Parkinson's disease and other synucleinopathy brains indicating that a-syn aggregation is associated with the pathogenesis of neurodegenerative disorders. Although the mechanisms underlying a-syn aggregation and toxicity are not fully elucidated, it is clear that a-syn undergoes post-translational modifications and interacts with numerous proteins and other macromolecules, metals, hormones, neurotransmitters, drugs and poisons that can all modulate its aggregation propensity. The current and most recent findings regarding the factors modulating a-syn aggregation process are discussed in detail.

AB - Aggregated a-synuclein is the major component of inclusions in Parkinson's disease and other synucleinopathy brains indicating that a-syn aggregation is associated with the pathogenesis of neurodegenerative disorders. Although the mechanisms underlying a-syn aggregation and toxicity are not fully elucidated, it is clear that a-syn undergoes post-translational modifications and interacts with numerous proteins and other macromolecules, metals, hormones, neurotransmitters, drugs and poisons that can all modulate its aggregation propensity. The current and most recent findings regarding the factors modulating a-syn aggregation process are discussed in detail.

UR - http://www.scopus.com/inward/record.url?scp=84894412233&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84894412233&partnerID=8YFLogxK

M3 - Review article

VL - 65

SP - 109

EP - 164

JO - Sub-Cellular Biochemistry

JF - Sub-Cellular Biochemistry

SN - 0306-0225

ER -