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The phosphorylation of [alpha]-synuclein: development and implication for the mechanism and therapy of the Parkinson's disease

Parkinson's disease (PD) is cited to be the second most common neuronal degenerative disorders; however, the exact mechanism of PD is still unclear. [alpha]-synuclein is one of the key proteins in PD pathogenesis as it's the main component of the PD hallmark Lewy bodies (LBs). Nowadays, the study of... Full description

Journal Title: Journal of Neurochemistry Oct 2015, Vol.135(1), pp.4-18
Main Author: Xu, Yan
Other Authors: Deng, Yulin , Qing, Hong
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 00223042 ; E-ISSN: 14714159 ; DOI: 10.1111/jnc.13234
Link: http://search.proquest.com/docview/1717432577/?pq-origsite=primo
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title: The phosphorylation of [alpha]-synuclein: development and implication for the mechanism and therapy of the Parkinson's disease
format: Article
creator:
  • Xu, Yan
  • Deng, Yulin
  • Qing, Hong
subjects:
  • Parkinsons Disease
  • Phosphorylation
  • Pharmacology
  • Proteins
  • Pathogenesis
ispartof: Journal of Neurochemistry, Oct 2015, Vol.135(1), pp.4-18
description: Parkinson's disease (PD) is cited to be the second most common neuronal degenerative disorders; however, the exact mechanism of PD is still unclear. [alpha]-synuclein is one of the key proteins in PD pathogenesis as it's the main component of the PD hallmark Lewy bodies (LBs). Nowadays, the study of [alpha]-synuclein phosphorylation mechanism related to the PD pathology has become a research hotspot, given that 90% of [alpha]-synuclein deposition in LBs is phosphorylated at Ser129, whereas in normal brains, only 4% or less of [alpha]-synuclein is phosphorylated at the residue. Here, we review the related study of PD pathological mechanism involving the phosphorylation of [alpha]-synuclein mainly at Ser129, Ser87, and Tyr125 residues in recent years, as well as some explorations relating to potential clinical application, in an attempt to describe the development and implication for the mechanism and therapy of PD. Given that some of the studies have yielded paradoxical results, there is...
language: eng
source:
identifier: ISSN: 00223042 ; E-ISSN: 14714159 ; DOI: 10.1111/jnc.13234
fulltext: fulltext
issn:
  • 00223042
  • 0022-3042
  • 14714159
  • 1471-4159
url: Link


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titleThe phosphorylation of [alpha]-synuclein: development and implication for the mechanism and therapy of the Parkinson's disease
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subjectParkinsons Disease ; Phosphorylation ; Pharmacology ; Proteins ; Pathogenesis
descriptionParkinson's disease (PD) is cited to be the second most common neuronal degenerative disorders; however, the exact mechanism of PD is still unclear. [alpha]-synuclein is one of the key proteins in PD pathogenesis as it's the main component of the PD hallmark Lewy bodies (LBs). Nowadays, the study of [alpha]-synuclein phosphorylation mechanism related to the PD pathology has become a research hotspot, given that 90% of [alpha]-synuclein deposition in LBs is phosphorylated at Ser129, whereas in normal brains, only 4% or less of [alpha]-synuclein is phosphorylated at the residue. Here, we review the related study of PD pathological mechanism involving the phosphorylation of [alpha]-synuclein mainly at Ser129, Ser87, and Tyr125 residues in recent years, as well as some explorations relating to potential clinical application, in an attempt to describe the development and implication for the mechanism and therapy of PD. Given that some of the studies have yielded paradoxical results, there is...
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descriptionParkinson's disease (PD) is cited to be the second most common neuronal degenerative disorders; however, the exact mechanism of PD is still unclear. [alpha]-synuclein is one of the key proteins in PD pathogenesis as it's the main component of the PD hallmark Lewy bodies (LBs). Nowadays, the study of [alpha]-synuclein phosphorylation mechanism related to the PD pathology has become a research hotspot, given that 90% of [alpha]-synuclein deposition in LBs is phosphorylated at Ser129, whereas in normal brains, only 4% or less of [alpha]-synuclein is phosphorylated at the residue. Here, we review the related study of PD pathological mechanism involving the phosphorylation of [alpha]-synuclein mainly at Ser129, Ser87, and Tyr125 residues in recent years, as well as some explorations relating to potential clinical application, in an attempt to describe the development and implication for the mechanism and therapy of PD. Given that some of the studies have yielded paradoxical results, there is...
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abstractParkinson's disease (PD) is cited to be the second most common neuronal degenerative disorders; however, the exact mechanism of PD is still unclear. [alpha]-synuclein is one of the key proteins in PD pathogenesis as it's the main component of the PD hallmark Lewy bodies (LBs). Nowadays, the study of [alpha]-synuclein phosphorylation mechanism related to the PD pathology has become a research hotspot, given that 90% of [alpha]-synuclein deposition in LBs is phosphorylated at Ser129, whereas in normal brains, only 4% or less of [alpha]-synuclein is phosphorylated at the residue. Here, we review the related study of PD pathological mechanism involving the phosphorylation of [alpha]-synuclein mainly at Ser129, Ser87, and Tyr125 residues in recent years, as well as some explorations relating to potential clinical application, in an attempt to describe the development and implication for the mechanism and therapy of PD. Given that some of the studies have yielded paradoxical results, there is...
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pubBlackwell Publishing Ltd.
doi10.1111/jnc.13234
urlhttp://search.proquest.com/docview/1717432577/
date2015-10-01