ArticleProtein science : a publication of the Protein Society2010
Amyloidogenic sequences in native protein structures.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.
What it found
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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
31 citing papers in PubMed, 1 synthesis or guideline pooled it, 81 citations in OpenAlex.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- Bioinformatic assessment of the potential amyloidogenicity of the human and evolutionarily more ancient proteomes.The Biochemical journal · 2026Article
- Highly sensitive chemiluminescence imaging of misfolded proteins in neurodegenerative models.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Isolated atrial amyloidosis from atrial natriuretic peptide - a common but overlooked cardiac condition.Upsala journal of medical sciences · 2026Review
- Chemical Evolution of Early Macromolecules: From Prebiotic Oligopeptides to Self-Organizing Biosystems via Amyloid Formation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Solvent induced amyloid polymorphism and the uncovering of the elusive class 3 amyloid topology.Communications biology · 2024Article
- Bioengineered amyloid peptide for rapid screening of inhibitors against main protease of SARS-CoV-2.Nature communications · 2024Article
- Role of the mechanisms for antibody repertoire diversification in monoclonal light chain deposition disorders: when a friend becomes foe.Frontiers in immunology · 2023Review
- Protein Based Biomaterials for Therapeutic and Diagnostic Applications.Progress in biomedical engineering (Bristol, England) · 2022Article
- Far-Off Resonance: Multiwavelength Raman Spectroscopy Probing Amide Bands of Amyloid-β-(37-42) Peptide.Molecules (Basel, Switzerland) · 2020Article
- Tau and TDP-43 proteinopathies: kindred pathologic cascades and genetic pleiotropy.Laboratory investigation; a journal of technical methods and pathology · 2019Review
- Microbial functional amyloids serve diverse purposes for structure, adhesion and defence.Biophysical reviews · 2019Review
- The CDR1 and Other Regions of Immunoglobulin Light Chains are Hot Spots for Amyloid Aggregation.Scientific reports · 2019Article
- Comparing the Folds of Prions and Other Pathogenic Amyloids.Pathogens (Basel, Switzerland) · 2018Review
- The Relation between α-Helical Conformation and Amyloidogenicity.Biophysical journal · 2018Article
- Protein misfolding in neurodegenerative diseases: implications and strategies.Translational neurodegeneration · 2017Review
- Article
- X-ray Crystallographic Structures of Oligomers of Peptides Derived from β2-Microglobulin.Journal of the American Chemical Society · 2015Article
- C-terminal sequence of amyloid-resistant type F apolipoprotein A-II inhibits amyloid fibril formation of apolipoprotein A-II in mice.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Peptide-Induced Amyloid-Like Conformational Transitions in Proteins.International journal of peptides · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Numerous short peptides have been shown to form beta-sheet amyloid aggregates in vitro. Proteins that contain such sequences are likely to be problematic for a cell, due to their potential to aggregate into toxic structures. We investigated the structures of 30 proteins containing 45 sequences known to form amyloid, to see how the proteins cope with the presence of these potentially toxic sequences, studying secondary structure, hydrogen-bonding, solvent accessible surface area and hydrophobicity. We identified two mechanisms by which proteins avoid aggregation: Firstly, amyloidogenic sequences are often found within helices, despite their inherent preference to form beta structure. Helices may offer a selective advantage, since in order to form amyloid the sequence will presumably have to first unfold and then refold into a beta structure. Secondly, amyloidogenic sequences that are found in beta structure are usually buried within the protein. Surface exposed amyloidogenic sequences are not tolerated in strands, presumably because they lead to protein aggregation via assembly of the amyloidogenic regions. The use of alpha-helices, where amyloidogenic sequences are forced into helix, despite their intrinsic preference for beta structure, is thus a widespread mechanism to avoid protein aggregation.
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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.