Self-aggregation and coaggregation of the p53 core fragment with its aggregation gatekeeper variant-Reference-Cited by-同舟云学术

Self-aggregation and coaggregation of the p53 core fragment with its aggregation gatekeeper variant

Published:2016 Issue:11 Volume:18 Page:8098-8107
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Lei Jiangtao¹²³⁴⁵,Qi Ruxi¹²³⁴⁵,Wei Guanghong¹²³⁴⁵,Nussinov Ruth⁶⁷⁸⁹¹⁰,Ma Buyong⁶⁷⁸⁹¹⁰

Affiliation:

1. State Key Laboratory of Surface Physics

2. Key Laboratory for Computational Physical Sciences (MOE), and Department of Physics

3. Fudan University

4. Shanghai

5. P. R. China

6. Basic Science Program

7. Leidos Biomedical Research, Inc.

8. Cancer and Inflammation Program

9. National Cancer Institute

10. Frederick

Abstract

The p53 aggregation nucleating²⁵¹ILTIITL²⁵⁷hexamer forms rich β-sheet structure, promotes the aggregation of its gatekeeper I254R mutant peptides in a prion-like process.

Funder

National Cancer Institute

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2016/CP/C5CP06538K

Reference71 articles.

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4. Polymorphic cross-seeding amyloid assemblies of amyloid-β and human islet amyloid polypeptide

5. Initiation of assembly of tau(273-284) and its ΔK280 mutant: an experimental and computational study

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