ArticlePloS one2013
The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- A3DyDB: exploring structural aggregation propensities in the yeast proteome.Microbial cell factories · 2023Article
- Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association.Computational and structural biotechnology journal · 2021Article
- Computational prediction of protein aggregation: Advances in proteomics, conformation-specific algorithms and biotechnological applications.Computational and structural biotechnology journal · 2020Review
- A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation.Redox biology · 2018Article
- Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions.The Journal of biological chemistry · 2014Article
- Conformational distribution and α-helix to β-sheet transition of human amylin fragment dimer.Biomacromolecules · 2014Article
- Trifluoroethanol modulates amyloid formation by the all α-helical URN1 FF domain.International journal of molecular sciences · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundProtein aggregation is linked to the onset of an increasing number of human nonneuropathic (either localized or systemic) and neurodegenerative disorders. In particular, misfolding of native α-helical structures and their self-assembly into nonnative intermolecular β-sheets has been proposed to trigger amyloid fibril formation in Alzheimer's and Parkinson's diseases.
methodsHere, we use a battery of biophysical techniques to elucidate the conformational conversion of native α-helices into amyloid fibrils using an all-α FF domain as a model system.
resultsWe show that under mild denaturing conditions at low pH this FF domain self-assembles into amyloid fibrils. Theoretical and experimental dissection of the secondary structure elements in this domain indicates that the helix 1 at the N-terminus has both the highest α-helical and amyloid propensities, controlling the transition between soluble and aggregated states of the protein.
conclusionsThe data illustrates the overlap between the propensity to form native α-helices and amyloid structures in protein segments. SIGNIFICANCE: The results presented contribute to explain why proteins cannot avoid the presence of aggregation-prone regions and indeed use stable α-helices as a strategy to neutralize such potentially deleterious stretches.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.