Tyrosine-Generated Nanostructures Initiate Amyloid Cross-Seeding in Proteins Leading to a Lethal Aggregation Trap
Author:
Affiliation:
1. Biophysical and Biomaterials Research Laboratory, Room 310, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India
Funder
University Grants Commission
Department of Science and Technology, Ministry of Science and Technology
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b00472
Reference36 articles.
1. Intrinsic property of phenylalanine to trigger protein aggregation and hemolysis has a direct relevance to phenylketonuria
2. Therapeutic implication of L-phenylalanine aggregation mechanism and its modulation by D-phenylalanine in phenylketonuria
3. Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria
4. Extension of the generic amyloid hypothesis to nonproteinaceous metabolite assemblies
5. Cross-seeding effects of amyloid β-protein and α-synuclein
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