Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities-Reference-Cited by-同舟云学术

Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities

Published:2018 Issue:29 Volume:54 Page:3605-3608
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Bhattacharyya Dipita¹²³,Kumar Rakesh⁴⁵³,Mehra Surabhi⁴⁵³,Ghosh Anirban¹²³,Maji Samir K.⁴⁵³,Bhunia Anirban¹²³^ORCID

Affiliation:

1. Department of Biophysics, Bose Institute

2. Kolkata 700 054

3. India

4. Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay

5. Mumbai 400 076

Abstract

Familial mutations in α-synuclein affect the immediate chemical environment of the protein's backbone, changing its aggregation kinetics and forming diverse structural and functional intermediates.

Funder

Council of Scientific and Industrial Research

University Grants Commission

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CC/C7CC09597J

Reference24 articles.

1. More than a Rumor Spreads in Parkinson's Disease

2. Implications of peptide assemblies in amyloid diseases

3. Multiple Tight Phospholipid-Binding Modes of α-Synuclein Revealed by Solution NMR Spectroscopy

4. Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation

5. What is the role of protein aggregation in neurodegeneration?

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