Targeting misfolding and aggregation of the amyloid-β peptide and mutant p53 protein using multifunctional molecules-Reference-Cited by-同舟云学术

Targeting misfolding and aggregation of the amyloid-β peptide and mutant p53 protein using multifunctional molecules

Published:2024 Issue:11 Volume:60 Page:1372-1388
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Grcic Lauryn¹,Leech Grace¹,Kwan Kalvin¹^ORCID,Storr Tim¹^ORCID

Affiliation:

1. Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada

Abstract

We highlight recent advances in the development of multifunctional molecules designed to limit misfolding and aggregation of intrinsically disordered biomolecules, with a focus on the amyloid-beta peptide in AD and the mutant p53 protein in cancer.

Funder

Natural Sciences and Engineering Research Council of Canada

Simon Fraser University

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/CC/D3CC05834D

Reference187 articles.

1. Structural Studies of Amyloid Proteins at the Molecular Level

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