The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity

A wide variety of oligomeric structures are formed during the aggregation of proteins associated with neurodegenerative diseases. Such soluble oligomers are believed to be key toxic species in the related disorders; therefore, identification of the structural determinants of toxicity is of upmost im...
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Autor*in:	Catherine K. Xu [verfasserIn] Marta Castellana-Cruz [verfasserIn] Serene W. Chen [verfasserIn] Zhen Du [verfasserIn] Georg Meisl [verfasserIn] Aviad Levin [verfasserIn] Benedetta Mannini [verfasserIn] Laura S. Itzhaki [verfasserIn] Tuomas P. J. Knowles [verfasserIn] Christopher M. Dobson [verfasserIn] Nunilo Cremades [verfasserIn] Janet R. Kumita [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	α-synuclein toxic oligomers Parkinson’s disease familial mutations α-helical structure

Übergeordnetes Werk:	In: Molecules - MDPI AG, 2003, 27(2022), 4, p 1293
Übergeordnetes Werk:	volume:27 ; year:2022 ; number:4, p 1293

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/molecules27041293

Katalog-ID:	DOAJ016419219

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allfieldsSound	10.3390/molecules27041293 doi (DE-627)DOAJ016419219 (DE-599)DOAJ22de59ffd416471b9dbd2a4adc27aee5 DE-627 ger DE-627 rakwb eng QD241-441 Catherine K. Xu verfasserin aut The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier A wide variety of oligomeric structures are formed during the aggregation of proteins associated with neurodegenerative diseases. Such soluble oligomers are believed to be key toxic species in the related disorders; therefore, identification of the structural determinants of toxicity is of upmost importance. Here, we analysed toxic oligomers of α-synuclein and its pathological variants in order to identify structural features that could be related to toxicity and found a novel structural polymorphism within G51D oligomers. These G51D oligomers can adopt a variety of β-sheet-rich structures with differing degrees of α-helical content, and the helical structural content of these oligomers correlates with the level of induced cellular dysfunction in SH-SY5Y cells. This structure–function relationship observed in α-synuclein oligomers thus presents the α-helical structure as another potential structural determinant that may be linked with cellular toxicity in amyloid-related proteins. α-synuclein toxic oligomers Parkinson’s disease familial mutations α-helical structure Organic chemistry Marta Castellana-Cruz verfasserin aut Serene W. Chen verfasserin aut Zhen Du verfasserin aut Georg Meisl verfasserin aut Aviad Levin verfasserin aut Benedetta Mannini verfasserin aut Laura S. Itzhaki verfasserin aut Tuomas P. J. Knowles verfasserin aut Christopher M. Dobson verfasserin aut Nunilo Cremades verfasserin aut Janet R. Kumita verfasserin aut In Molecules MDPI AG, 2003 27(2022), 4, p 1293 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:27 year:2022 number:4, p 1293 https://doi.org/10.3390/molecules27041293 kostenfrei https://doaj.org/article/22de59ffd416471b9dbd2a4adc27aee5 kostenfrei https://www.mdpi.com/1420-3049/27/4/1293 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 27 2022 4, p 1293
language	English
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callnumber-first	Q - Science
author	Catherine K. Xu
spellingShingle	Catherine K. Xu misc QD241-441 misc α-synuclein misc toxic oligomers misc Parkinson’s disease misc familial mutations misc α-helical structure misc Organic chemistry The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity
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topic_title	QD241-441 The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity α-synuclein toxic oligomers Parkinson’s disease familial mutations α-helical structure
topic	misc QD241-441 misc α-synuclein misc toxic oligomers misc Parkinson’s disease misc familial mutations misc α-helical structure misc Organic chemistry
topic_unstemmed	misc QD241-441 misc α-synuclein misc toxic oligomers misc Parkinson’s disease misc familial mutations misc α-helical structure misc Organic chemistry
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title	The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity
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title_full	The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity
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author_browse	Catherine K. Xu Marta Castellana-Cruz Serene W. Chen Zhen Du Georg Meisl Aviad Levin Benedetta Mannini Laura S. Itzhaki Tuomas P. J. Knowles Christopher M. Dobson Nunilo Cremades Janet R. Kumita
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title_sort	pathological g51d mutation in alpha-synuclein oligomers confers distinct structural attributes and cellular toxicity
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title_auth	The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity
abstract	A wide variety of oligomeric structures are formed during the aggregation of proteins associated with neurodegenerative diseases. Such soluble oligomers are believed to be key toxic species in the related disorders; therefore, identification of the structural determinants of toxicity is of upmost importance. Here, we analysed toxic oligomers of α-synuclein and its pathological variants in order to identify structural features that could be related to toxicity and found a novel structural polymorphism within G51D oligomers. These G51D oligomers can adopt a variety of β-sheet-rich structures with differing degrees of α-helical content, and the helical structural content of these oligomers correlates with the level of induced cellular dysfunction in SH-SY5Y cells. This structure–function relationship observed in α-synuclein oligomers thus presents the α-helical structure as another potential structural determinant that may be linked with cellular toxicity in amyloid-related proteins.
abstractGer	A wide variety of oligomeric structures are formed during the aggregation of proteins associated with neurodegenerative diseases. Such soluble oligomers are believed to be key toxic species in the related disorders; therefore, identification of the structural determinants of toxicity is of upmost importance. Here, we analysed toxic oligomers of α-synuclein and its pathological variants in order to identify structural features that could be related to toxicity and found a novel structural polymorphism within G51D oligomers. These G51D oligomers can adopt a variety of β-sheet-rich structures with differing degrees of α-helical content, and the helical structural content of these oligomers correlates with the level of induced cellular dysfunction in SH-SY5Y cells. This structure–function relationship observed in α-synuclein oligomers thus presents the α-helical structure as another potential structural determinant that may be linked with cellular toxicity in amyloid-related proteins.
abstract_unstemmed	A wide variety of oligomeric structures are formed during the aggregation of proteins associated with neurodegenerative diseases. Such soluble oligomers are believed to be key toxic species in the related disorders; therefore, identification of the structural determinants of toxicity is of upmost importance. Here, we analysed toxic oligomers of α-synuclein and its pathological variants in order to identify structural features that could be related to toxicity and found a novel structural polymorphism within G51D oligomers. These G51D oligomers can adopt a variety of β-sheet-rich structures with differing degrees of α-helical content, and the helical structural content of these oligomers correlates with the level of induced cellular dysfunction in SH-SY5Y cells. This structure–function relationship observed in α-synuclein oligomers thus presents the α-helical structure as another potential structural determinant that may be linked with cellular toxicity in amyloid-related proteins.
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title_short	The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity
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The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity

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