ArticlePrion2012
Domain swapping and amyloid fibril conformation.
Article in Prion, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed.
- Protein Self-Interaction in Cellular Function and Network Evolution: Molecular Mechanisms, AI-Driven Insights, and Therapeutic Potentials.International journal of molecular sciences · 2026Review
- Understanding domain swapping in the c-Src SH3 domain through hinge-loop mutagenesis.Acta crystallographica. Section D, Structural biology · 2025Article
- Is amyloid fibrillation related to 3D domain swapping for the C-terminal domain of SARS-CoV main protease?International journal of biological macromolecules · 2022Article
- Mycobacterium tuberculosis CarD, an essential global transcriptional regulator forms amyloid-like fibrils.Scientific reports · 2018Article
- Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Solid state nuclear magnetic resonance · 2017Review
- Insights into the mechanism of cystatin C oligomer and amyloid formation and its interaction with β-amyloid.The Journal of biological chemistry · 2017Article
- Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Nature communications · 2017Article
- Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly.Scientific reports · 2017Article
- Structural Interface Forms and Their Involvement in Stabilization of Multidomain Proteins or Protein Complexes.International journal of molecular sciences · 2016Article
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- Transient misfolding dominates multidomain protein folding.Nature communications · 2015Article
- Engineered Domain Swapping as an On/Off Switch for Protein Function.Chemistry & biology · 2015Article
- Role of domain swapping in the hetero-oligomeric cytochrome b6f lipoprotein complex.Biochemistry · 2015Article
- Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.Biochemistry · 2014Article
- Optical control of protein-protein interactions via blue light-induced domain swapping.Biochemistry · 2014Article
- The quaternary structure of the recombinant bovine odorant-binding protein is modulated by chemical denaturants.PloS one · 2014Article
- Article
- Foldon unfolding mediates the interconversion between M(pro)-C monomer and 3D domain-swapped dimer.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For several different proteins an apparent correlation has been observed between the propensity for dimerization by domain-swapping and the ability to aggregate into amyloid-like fibrils. Examples include the disease-related proteins β 2-microglobulin and transthyretin. This has led to proposals that the amyloid-formation pathway may feature extensive domain swapping. One possible consequence of such an aggregation pathway is that the resulting fibrils would incorporate structural elements that resemble the domain-swapped forms of the protein and, thus, reflect certain native-like structures or domain-interactions. In magic angle spinning solid-state NMR-based and other structural studies of such amyloid fibrils, it appears that many of these proteins form fibrils that are not native-like. Several fibrils, instead, have an in-register, parallel conformation, which is a common amyloid structural motif and is seen, for instance, in various prion fibrils. Such a lack of native structure in the fibrils suggests that the apparent connection between domain-swapping ability and amyloid-formation may be more subtle or complex than may be presumed at first glance.
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Registered trials
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.