Open Access
Alpha-Synuclein Misfolding and Aggregation in Parkinson's Disease
Michael White
- Vol. 3, Iss: 1, pp 27
TLDR
Eukaryon is published by students at Lake Forest College and is part of the Molecular and Cellular Neuroscience Commons, Molecular Biology Commons, molecular Genetics Commons, and the Nervous System Diseases Commons.Abstract:
Follow this and additional works at: http://publications.lakeforest.edu/eukaryon Part of the Molecular and Cellular Neuroscience Commons, Molecular Biology Commons, Molecular Genetics Commons, and the Nervous System Diseases Commons Disclaimer: Eukaryon is published by students at Lake Forest College, who are solely responsible for its content. The views expressed in Eukaryon do not necessarily reflect those of the College. Articles published within Eukaryon should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.read more
Citations
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Journal ArticleDOI
The remarkable conformational plasticity of alpha-synuclein: blessing or curse?
TL;DR: The ways in which aggregated α-SYN mediates toxicity and might lead to PD are addressed, and possible therapeutic strategies are proposed.
Journal ArticleDOI
Hederagenin and α-hederin promote degradation of proteins in neurodegenerative diseases and improve motor deficits in MPTP-mice
An-Guo Wu,Wu Zeng,Vincent Kam Wai Wong,Yi-Zhun Zhu,Amy C. Y. Lo,Liang Liu,Betty Yuen Kwan Law +6 more
TL;DR: The neuroprotective effect of the purified Hedera helix (HH) fraction containing both hederagenin and &agr;‐hederin, is confirmed by the improvement of motor deficits in PD mice model, suggesting the therapeutic roles of HH in neurodegenerative disorders.
Journal ArticleDOI
The ubiquitin proteasome system as a potential therapeutic target for treatment of neurodegenerative diseases.
TL;DR: The pathogenic role and intracellular fate of the candidate molecules associated with onset and progression of AD and PD, the protein tau and α-synuclein in context with the function of ubiquitin proteasome system are discussed.
Journal ArticleDOI
Function and Dysfunction of α-Synuclein: Probing Conformational Changes and Aggregation by Single Molecule Fluorescence
TL;DR: The current literature featuring single-molecule fluorescence studies of α-synuclein are reviewed and how these studies have contributed to the authors' understanding of both its function and its role in disease are discussed.
Experimental and computational analysis of the synucleins
TL;DR: This study led to the development of a proposed evolutionary model for the synucleins, which hypothesized that P-synuclein, encoded by seven exons, is the oldest o f theSynuclein proteins, whose structure and function have been resolved.
References
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Mutation in the α-synuclein gene identified in families with Parkinson's disease
Mihael H. Polymeropoulos,Christian Lavedan,Elisabeth Leroy,Susan E. Ide,Anindya Dehejia,Amalia Dutra,Brian L. Pike,Holly Root,Jeffrey Rubenstein,Rebecca Boyer,Edward S. Stenroos,Settara C. Chandrasekharappa,Aglaia Athanassiadou,Theodore Papapetropoulos,William G. Johnson,Alice Lazzarini,Roger C. Duvoisin,Giuseppe Di Iorio,Lawrence I. Golbe,Robert L. Nussbaum +19 more
TL;DR: A mutation was identified in the α-synuclein gene, which codes for a presynaptic protein thought to be involved in neuronal plasticity, in the Italian kindred and in three unrelated families of Greek origin with autosomal dominant inheritance for the PD phenotype.
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Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Tohru Kitada,Shuichi Asakawa,Nobutaka Hattori,Hiroto Matsumine,Yasuhiro Yamamura,Shinsei Minoshima,Masayuki Yokochi,Yoshikuni Mizuno,Nobuyoshi Shimizu +8 more
TL;DR: Mutations in the newly identified gene appear to be responsible for the pathogenesis of Autosomal recessive juvenile parkinsonism, and the protein product is named ‘Parkin’.
Journal ArticleDOI
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
Eriza Maria Valente,Patrick M. Abou-Sleiman,Viviana Caputo,Miratul M. K. Muqit,Kirsten Harvey,Suzana Gispert,Zeeshan Ali,Domenico Del Turco,Anna Rita Bentivoglio,Daniel G. Healy,Alberto Albanese,Robert L. Nussbaum,Rafael González-Maldonado,Thomas Deller,S Salvi,Pietro Cortelli,William P. Gilks,David S. Latchman,Roberk J. Harvey,Bruno Dallapiccola,Georg Auburger,Nicholas W. Wood +21 more
TL;DR: The identification of two homozygous mutations affecting the PINK1 kinase domain in three consanguineous PARK6 families provide a direct molecular link between mitochondria and the pathogenesis of PD.
Journal ArticleDOI
α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies
TL;DR: It is shown thatLewy bodies and Lewy neurites from Parkinson’s disease and dementia with Lewy bodies are stained strongly by antibodies directed against amino- terminal and carboxyl-terminal sequences of α-synuclein, showing the presence of full- length or close to full-length α- synuclein.
Journal ArticleDOI
The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia.
Juan J. Zarranz,Javier Alegre,Juan Carlos Gómez-Esteban,Elena Lezcano,Raquel Ros,Israel Ampuero,Lídice Vidal,Janet Hoenicka,Olga Rodriguez,Begoña Atarés,Verónica Llorens,Estrella Gomez Tortosa,Teodoro del Ser,David G. Munoz,Justo García de Yébenes +14 more
TL;DR: Dementia with Lewy bodies is related to mutation of α‐synuclein, and the novel mutation, that substitutes a dicarboxylic amino acid, glutamic acid, with a basic amino acid in a much conserved area of the protein, is likely to produce severe disturbance of protein function.