Self-assembly of human amylin-derived peptides studied by atomic force microscopy and single molecule force spectroscopy-Reference-Cited by-同舟云学术

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Self-assembly of human amylin-derived peptides studied by atomic force microscopy and single molecule force spectroscopy

Published:2012 Issue:4 Volume:8 Page:1234-1242
ISSN:1744-683X
Container-title:Soft Matter
language:en
Short-container-title:Soft Matter

Author:

Valle-Delgado Juan José,Liepina Inta,Lapidus Dmitrijs,Sabaté Raimon,Ventura Salvador,Samitier Josep,Fernàndez-Busquets Xavier

Publisher

Royal Society of Chemistry (RSC)

Subject

Condensed Matter Physics,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2012/SM/C1SM06764H

Reference103 articles.

1. Protein folding and misfolding

2. High-Resolution Electron Microscopic Analysis of the Amyloid Fibril in Alzheimerʼs Disease

3. Tau protein pathology in neurodegenerative diseases

4. Alzheimer’s amyloid fibrils: structure and assembly

5. Oligomerization and fibril assembly of the amyloid-β protein

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1. Incorporation of phenylcarbonyl groups in the sidechain: A tool to induce ordered assembly of peptides on surfaces;Journal of Peptide Science;2024-06-19

2. Understanding the mechanism of amylin aggregation: From identifying crucial segments to tracing dominant sequential events to modeling potential aggregation suppressors;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2023-01

3. Functional Bacterial Amyloids: Understanding Fibrillation, Regulating Biofilm Fibril Formation and Organizing Surface Assemblies;Molecules;2022-06-24

4. Insights into Mechanism of A β 42 Fibril Growth on Surface of Graphene Oxides: Oxidative Degree Matters;Advanced Healthcare Materials;2021-05-29

5. Characterizing the assembly behaviors of human amylin: a perspective derived from C-terminal variants;Chem. Commun.;2013

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