The degree of unsaturation of fatty acids in phosphatidylserine alters the rate of insulin aggregation and the structure and toxicity of amyloid aggregates-Reference-Cited by-同舟云学术

The degree of unsaturation of fatty acids in phosphatidylserine alters the rate of insulin aggregation and the structure and toxicity of amyloid aggregates

Published:2022-05-13 Issue:11 Volume:596 Page:1424-1433
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Letters

Author:

Matveyenka Mikhail¹,Rizevsky Stanislav¹²,Kurouski Dmitry¹³^ORCID

Affiliation:

1. Department of Biochemistry and Biophysics Texas A&M University College Station TX USA

2. Department of Biotechnology Binh Duong University Thu Dau Mot Vietnam

3. Department of Biomedical Engineering Texas A&M University College Station TX USA

Funder

National Institute of General Medical Sciences

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.14369

Reference51 articles.

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

2. The amyloid state and its association with protein misfolding diseases

3. A new era for understanding amyloid structures and disease

4. Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation

5. Unravelling the Structural Organization of Individual α-Synuclein Oligomers Grown in the Presence of Phospholipids

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