Surface effects on functional amyloid formation-Reference-Cited by-同舟云学术

Surface effects on functional amyloid formation

Published:2024 Issue:34 Volume:16 Page:16172-16182
ISSN:2040-3364
Container-title:Nanoscale
language:en
Short-container-title:Nanoscale

Author:

Dear Alexander J.¹²^ORCID,Meisl Georg¹^ORCID,Taylor Christopher G.¹^ORCID,Palmiero Umberto Capasso³,Stubbe Susanne Nordby⁴,Liu Qian⁴,Arosio Paolo³,Linse Sara²,Knowles Tuomas P. J.¹^ORCID,Andreasen Maria⁴^ORCID

Affiliation:

1. Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK

2. Department of Biochemistry and Structural Biology, Lund University, SE-221 00 Lund, Sweden

3. Institute for Chemical and Bioengineering, Department of Chemistry and Applied Biosciences, ETH Zürich, Zürich, Switzerland

4. Department of Biomedicine, Aarhus University, Wilhelm Meyers Allé 3, Aarhus DK-8000, Denmark

Abstract

Fibril nucleation during protein aggregation is a heterogeneous process highly dependent on the surfaces present during the process.

Funder

Natur og Univers, Det Frie Forskningsråd

Aarhus Universitets Forskningsfond

Novo Nordisk Fonden

Vetenskapsrådet

Frances and Augustus Newman Foundation

HORIZON EUROPE European Research Council

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/NR/D4NR01496K

Reference53 articles.

1. Protein Misfolding, Functional Amyloid, and Human Disease

2. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

3. Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules

4. Functional Amyloids Composed of Phenol Soluble Modulins Stabilize Staphylococcus aureus Biofilms

5. Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides