Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects

Chakraborty et al. present biophysical and structural insights into fibril-forming oligomers of alpha-synuclein stabilized by heme. They show that heme targets the His50 residue of the oligomers and locks the protein into a different conformation which leads to non-toxic, non-fibrillating oligomer f...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Ritobrita Chakraborty, Sandip Dey, Pallabi Sil, Simanta Sarani Paul, Dipita Bhattacharyya, Anirban Bhunia, Jayati Sengupta, Krishnananda Chattopadhyay
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/25742eb9b9d54e619cd7385d8ac904d4
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:25742eb9b9d54e619cd7385d8ac904d4
record_format	dspace
spelling	oai:doaj.org-article:25742eb9b9d54e619cd7385d8ac904d42021-12-02T15:38:22ZConformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects10.1038/s42003-021-02026-z2399-3642https://doaj.org/article/25742eb9b9d54e619cd7385d8ac904d42021-05-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02026-zhttps://doaj.org/toc/2399-3642Chakraborty et al. present biophysical and structural insights into fibril-forming oligomers of alpha-synuclein stabilized by heme. They show that heme targets the His50 residue of the oligomers and locks the protein into a different conformation which leads to non-toxic, non-fibrillating oligomer formation, therefore addressing a very important issue in the field of structure of transient oligomers.Ritobrita ChakrabortySandip DeyPallabi SilSimanta Sarani PaulDipita BhattacharyyaAnirban BhuniaJayati SenguptaKrishnananda ChattopadhyayNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Ritobrita Chakraborty Sandip Dey Pallabi Sil Simanta Sarani Paul Dipita Bhattacharyya Anirban Bhunia Jayati Sengupta Krishnananda Chattopadhyay Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects
description	Chakraborty et al. present biophysical and structural insights into fibril-forming oligomers of alpha-synuclein stabilized by heme. They show that heme targets the His50 residue of the oligomers and locks the protein into a different conformation which leads to non-toxic, non-fibrillating oligomer formation, therefore addressing a very important issue in the field of structure of transient oligomers.
format	article
author	Ritobrita Chakraborty Sandip Dey Pallabi Sil Simanta Sarani Paul Dipita Bhattacharyya Anirban Bhunia Jayati Sengupta Krishnananda Chattopadhyay
author_facet	Ritobrita Chakraborty Sandip Dey Pallabi Sil Simanta Sarani Paul Dipita Bhattacharyya Anirban Bhunia Jayati Sengupta Krishnananda Chattopadhyay
author_sort	Ritobrita Chakraborty
title	Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects
title_short	Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects
title_full	Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects
title_fullStr	Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects
title_full_unstemmed	Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects
title_sort	conformational distortion in a fibril-forming oligomer arrests alpha-synuclein fibrillation and minimizes its toxic effects
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/25742eb9b9d54e619cd7385d8ac904d4
work_keys_str_mv	AT ritobritachakraborty conformationaldistortioninafibrilformingoligomerarrestsalphasynucleinfibrillationandminimizesitstoxiceffects AT sandipdey conformationaldistortioninafibrilformingoligomerarrestsalphasynucleinfibrillationandminimizesitstoxiceffects AT pallabisil conformationaldistortioninafibrilformingoligomerarrestsalphasynucleinfibrillationandminimizesitstoxiceffects AT simantasaranipaul conformationaldistortioninafibrilformingoligomerarrestsalphasynucleinfibrillationandminimizesitstoxiceffects AT dipitabhattacharyya conformationaldistortioninafibrilformingoligomerarrestsalphasynucleinfibrillationandminimizesitstoxiceffects AT anirbanbhunia conformationaldistortioninafibrilformingoligomerarrestsalphasynucleinfibrillationandminimizesitstoxiceffects AT jayatisengupta conformationaldistortioninafibrilformingoligomerarrestsalphasynucleinfibrillationandminimizesitstoxiceffects AT krishnanandachattopadhyay conformationaldistortioninafibrilformingoligomerarrestsalphasynucleinfibrillationandminimizesitstoxiceffects
_version_	1718386160580952064

Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects

Ejemplares similares