ReviewJournal of molecular biology2012
Selective molecular recognition in amyloid growth and transmission and cross-species barriers.
Review in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
40 citing papers in PubMed, 81 citations in OpenAlex.
- Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025Review
- Effect of Cross-Seeding of Wild-Type Amyloid-βThe journal of physical chemistry. B · 2023Article
- Higher-order interactions of Bcr-Abl can broaden chronic myeloid leukemia (CML) drug repertoire.Protein science : a publication of the Protein Society · 2023Article
- Repurposing of intestinal defensins as multi-target, dual-function amyloid inhibitorsChemical science · 2022Article
- Cross-seeding between Aβ and SEVI indicates a pathogenic link and gender difference between alzheimer diseases and AIDS.Communications biology · 2022Article
- Species-barrier on the cross-species oral transmission of bovine AA amyloidosis in mice.The Journal of veterinary medical science · 2021Article
- Multistep Changes in Amyloid Structure Induced by Cross-Seeding on a Rugged Energy Landscape.Biophysical journal · 2021Article
- Review
- Article
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Protein Supramolecular Structures: From Self-Assembly to Nanovaccine Design.Nanomaterials (Basel, Switzerland) · 2020Review
- Binding-induced folding under unfolding conditions: Switching between induced fit and conformational selection mechanisms.The Journal of biological chemistry · 2019Article
- Protein ensembles link genotype to phenotype.PLoS computational biology · 2019Review
- Molecular Recognition between Aβ-Specific Single-Domain Antibody and Aβ Misfolded Aggregates.Antibodies (Basel, Switzerland) · 2018Article
- Structure and energetic basis of overrepresented λ light chain in systemic light chain amyloidosis patients.Biochimica et biophysica acta. Molecular basis of disease · 2018Article
- Experimental and Computational Protocols for Studies of Cross-Seeding Amyloid Assemblies.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Mechanisms of recognition of amyloid-β (Aβ) monomer, oligomer, and fibril by homologous antibodies.The Journal of biological chemistry · 2017Article
- Key aromatic/hydrophobic amino acids controlling a cross-amyloid peptide interactionThe Journal of biological chemistry · 2017Article
- Familial Mutations May Switch Conformational Preferences in α-Synuclein Fibrils.ACS chemical neuroscience · 2017Article
- Amylin-Aβ oligomers at atomic resolution using molecular dynamics simulations: a link between Type 2 diabetes and Alzheimer's disease.Physical chemistry chemical physics : PCCP · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Mutual conformational selection and population shift followed by minor induced-fit optimization is the key mechanism in biomolecular recognition, and monomers and small oligomers binding to amyloid seeds in fibril growth is a molecular recognition event. Here, we describe amyloid aggregation, preferred species, cross-species barriers and transmission within the broad framework of molecular recognition. Cross-seeding of amyloid species is governed by conformational selection of compatible (complementary) states. If the dominant conformations of two species are similar, they can cross-seed each other; on the other hand, if they are sufficiently different, they will grow into different fibrils, reflecting species barriers. Such a scenario has recently been observed for the tau protein, which has four repeats. While a construct consisting of repeats 1, 3 and 4 can serve as a seed for the entire four-repeat tau segment, the inverse does not hold. On the other hand, the tau protein repeats with the characteristic U-turn shape can cross-seed Alzheimer's amyloid β and, similarly, the islet amyloid polypeptide. Within this framework, we suggest that the so-called "central dogma" of amyloid formation, where aggregation takes place through nonspecific backbone hydrogen bonding interactions, which are common to all peptides and proteins, is a simple reflection of the heterogeneous, polymorphic free-energy landscape of amyloid species. Here, we review available data and make some propositions addressing this key problem. In particular, we argue that recent theoretical and experimental observations support the key role of selective molecular recognition in amyloidosis and in determining cross-species barriers and transmission.
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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.