Structural mechanisms of oligomer and amyloid fibril formation by the prion protein-Reference-Cited by-同舟云学术

Structural mechanisms of oligomer and amyloid fibril formation by the prion protein

Published:2018 Issue:49 Volume:54 Page:6230-6242
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Sengupta Ishita¹²³⁴^ORCID,Udgaonkar Jayant B.⁵⁶⁴^ORCID

Affiliation:

1. National Centre for Biological Sciences

2. Tata Institute of Fundamental Research

3. Bengaluru 560065

4. India

5. Indian Institute of Science Education and Research Pune

6. Pune 411008

Abstract

The aggregation mechanism of the prion protein is highly heterogeneous.

Funder

Department of Biotechnology, Ministry of Science and Technology

Tata Institute of Fundamental Research

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/C8CC03053G

Reference153 articles.

1. Nobel Lecture: Prions

2. The cellular prion protein binds copper in vivo

3. Prion Protein Selectively Binds Copper(II) Ions

4. The AGAAAAGA Palindrome in PrP Is Required to Generate a Productive PrPSc-PrPC Complex That Leads to Prion Propagation

5. Role of the Highly Conserved Middle Region of Prion Protein (PrP) in PrP−Lipid Interaction

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