Modeling Amyloid Aggregation Kinetics: A Case Study with Sup35NM-Reference-Cited by-同舟云学术

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Modeling Amyloid Aggregation Kinetics: A Case Study with Sup35NM

Published:2021-05-07 Issue:19 Volume:125 Page:4955-4963
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Sharma Aditi¹,McDonald Matthew A.¹^ORCID,Rose Harrison B.¹,Chernoff Yury O.²³,Behrens Sven H.¹⁴,Bommarius Andreas S.¹⁵^ORCID

Affiliation:

1. School of Chemical & Biomolecular Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, United States

2. School of Biological Sciences, Georgia Institute of Technology, Atlanta, Georgia 30332, United States

3. Laboratory of Amyloid Biology, St. Petersburg State University, St. Petersburg 199034, Russia

4. Polymer Science & Materials Chemistry, Exponent, Inc., Atlanta, Georgia 30326, United States

5. School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, United States

Funder

Division of Molecular and Cellular Biosciences

Division of Industrial Innovation and Partnerships

Division of Chemical, Bioengineering, Environmental, and Transport Systems

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.0c11250

Reference42 articles.

1. Ion-specific Effects on Prion Nucleation and Strain Formation

2. Amyloid diseases: Abnormal protein aggregation in neurodegeneration

3. Therapeutic strategies for human amyloid diseases

4. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Prion-like Aggregation of the Heptapeptide GNNQQNY into Amyloid Nanofiber Is Governed by Configuration Entropy;Journal of Chemical Information and Modeling;2023-10-02

2. Global analysis of kinetics reveals the role of secondary nucleation in recombinant spider silk self‐assembly;Protein Science;2023-07-24

3. The interacting rotifer-biopolymers are anti- and disaggregating agents for human-type beta-amyloid in vitro;International Journal of Biological Macromolecules;2022-03

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