ArticleProceedings of the National Academy of Sciences of the United States of America2004
Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 136 citations in OpenAlex.
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- SOBA: Development and testing of a soluble oligomer binding assay for detection of amyloidogenic toxic oligomers.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The role of α-sheet structure in amyloidogenesis: characterization and implications.Open biology · 2022Review
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- Metals in ALS TDP-43 Pathology.International journal of molecular sciences · 2021Review
- A critical review of radiotracers in the positron emission tomography imaging of traumatic brain injury: FDG, tau, and amyloid imaging in mild traumatic brain injury and chronic traumatic encephalopathy.European journal of nuclear medicine and molecular imaging · 2021Review
- Edge Strand Dissociation and Conformational Changes in Transthyretin under Amyloidogenic Conditions.Biophysical journal · 2020Article
- Tumorigenic p53 mutants undergo common structural disruptions including conversion to α-sheet structure.Protein science : a publication of the Protein Society · 2020Article
- Aggregation Mechanism of Alzheimer's Amyloid β-Peptide Mediated by α-Strand/α-Sheet Structure.International journal of molecular sciences · 2020Article
- The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations.Frontiers in molecular biosciences · 2020Review
- Protein three-dimensional structures at the origin of life.Interface focus · 2019Review
- α-Sheet secondary structure in amyloid β-peptide drives aggregation and toxicity in Alzheimer's disease.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Computational insights into the role of α-strand/sheet in aggregation of α-synuclein.Scientific reports · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Transthyretin, beta(2)-microglobulin, lysozyme, and the prion protein are four of the best-characterized proteins implicated in amyloid disease. Upon partial acid denaturation, these proteins undergo conformational change into an amyloidogenic intermediate that can self-assemble into amyloid fibrils. Many experiments have shown that pH-mediated changes in structure are required for the formation of the amyloidogeneic intermediate, but it has proved impossible to characterize these conformational changes at high resolution using experimental means. To probe these conformational changes at atomic resolution, we have performed molecular dynamics simulations of these proteins at neutral and low pH. In low-pH simulations of all four proteins, we observe the formation of alpha-pleated sheet secondary structure, which was first proposed by L. Pauling and R. B. Corey [(1951) Proc. Natl. Acad. Sci. USA 37, 251-256]. In all beta-sheet proteins, transthyretin and beta(2)-microglobulin, alpha-pleated sheet structure formed over the strands that are highly protected in hydrogen-exchange experiments probing amyloidogenic conditions. In lysozyme and the prion protein, alpha-sheets formed in the specific regions of the protein implicated in the amyloidogenic conversion. We propose that the formation of alpha-pleated sheet structure may be a common conformational transition in amyloidosis.
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