Electrostatic Interactions at N- and C-Termini Determine Fibril Polymorphism in Serum Amyloid A Fragments-Reference-Cited by-同舟云学术

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Electrostatic Interactions at N- and C-Termini Determine Fibril Polymorphism in Serum Amyloid A Fragments

Published:2016-09-26 Issue:39 Volume:120 Page:10258-10268
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Jannone Justine M.¹,Grigg James I.¹,Aguirre Lauren M.¹,Jones Eric M.¹

Affiliation:

1. Department of Chemistry and Biochemistry, California Polytechnic State University San Luis Obispo, California 93407 United States

Funder

College of Science and Mathematics, California Polytechnic State University

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.6b07672

Reference80 articles.

1. Protein Misfolding, Functional Amyloid, and Human Disease

2. Biology of Amyloid: Structure, Function, and Regulation

3. The Amyloid State of Proteins in Human Diseases

4. Possibilities for ‘smart’ materials exploiting the self-assembly of polypeptides into fibrils

5. Amyloids: Not Only Pathological Agents but Also Ordered Nanomaterials

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1. Key charged residues influence the amyloidogenic propensity of the helix-1 region of serum amyloid A;Biochimica et Biophysica Acta (BBA) - General Subjects;2024-11

2. Influences of amino-terminal modifications on amyloid fibril formation of human serum amyloid A;Archives of Biochemistry and Biophysics;2023-07

3. Presence of a SARS-CoV-2 Protein Enhances Amyloid Formation of Serum Amyloid A;The Journal of Physical Chemistry B;2021-08-09

4. Presence of a SARS-COV-2 protein enhances Amyloid Formation of Serum Amyloid A;2021-05-19

5. Atomic-level differences between brain parenchymal- and cerebrovascular-seeded Aβ fibrils;Scientific Reports;2021-01-08

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