ArticleProtein science : a publication of the Protein Society2017
Heparin-induced amyloid fibrillation of β
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 26 citations in OpenAlex.
- Cylindracin, a Fruiting Body-Specific Protein ofToxins · 2025Article
- Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy.Protein science : a publication of the Protein Society · 2025Article
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- Mechanisms of polyphosphate-induced amyloid fibril formation triggered by breakdown of supersaturation.Biophysics and physicobiology · 2023Article
- Article
- Pathogenic D76N Variant of βBiology · 2021Article
- Polyphenol-solubility alters amyloid fibril formation of α-synuclein.Protein science : a publication of the Protein Society · 2021Article
- Article
- Possible mechanisms of polyphosphate-induced amyloid fibril formation of βProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism.Biophysical reviews · 2018Review
- Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation.The Journal of biological chemistry · 2017Article
- Modulating protein amyloid aggregation with nanomaterials.Environmental science. Nano · 2017Article
- Molecular Origins of the Compatibility between Glycosaminoglycans and Aβ40 Amyloid Fibrils.Journal of molecular biology · 2017Article
- Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation.Biophysical reviews · 2017Review
- Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibrils are fibrillar deposits of denatured proteins associated with amyloidosis and are formed by a nucleation and growth mechanism. We revisited an alternative and classical view of amyloid fibrillation: amyloid fibrils are crystal-like precipitates of denatured proteins formed above solubility upon breaking supersaturation. Various additives accelerate and then inhibit amyloid fibrillation in a concentration-dependent manner, suggesting that the combined effects of stabilizing and destabilizing forces affect fibrillation. Heparin, a glycosaminoglycan and anticoagulant, is an accelerator of fibrillation for various amyloidogenic proteins. By using β
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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.