ArticleInternational journal of molecular sciences2021
Trypsin Induced Degradation of Amyloid Fibrils.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
13 citing papers in PubMed, 30 citations in OpenAlex.
- Substituent-Based Modulation of Self-Assembly and Immunogenicity of Amphipathic Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Broken but not beaten: Challenge of reducing the amyloids pathogenicity by degradation.Journal of advanced research · 2025Review
- Cathepsin B prevents cell death by fragmentation and destruction of pathological amyloid fibrils.Cell death discovery · 2025Article
- Dietary Strategies to Mitigate Alzheimer's Disease: Insights into Antioxidant Vitamin Intake and Supplementation with Microbiota-Gut-Brain Axis Cross-Talk.Antioxidants (Basel, Switzerland) · 2024Review
- Article
- Correction: Stepanenko et al. Trypsin Induced Degradation of Amyloid Fibrils.International journal of molecular sciences · 2024Article
- A Perspective on How Fibrinaloid Microclots and Platelet Pathology May be Applied in Clinical Investigations.Seminars in thrombosis and hemostasis · 2024Review
- Observations of amyloid breakdown by proteases over time using scanning acoustic microscopy.Scientific reports · 2023Article
- Amyloid Fibrils ofInternational journal of molecular sciences · 2023Article
- Peptide Inhibitors of Insulin Fibrillation: Current and Future Challenges.International journal of molecular sciences · 2023Review
- Amyloid fibrils degradation: the pathway to recovery or aggravation of the disease?Frontiers in molecular biosciences · 2023Article
- Pathological and Functional Amyloid Fibrils-Part I.International journal of molecular sciences · 2022Article
- Is It Possible to Create Antimicrobial Peptides Based on the Amyloidogenic Sequence of Ribosomal S1 Protein ofInternational journal of molecular sciences · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Proteolytic enzymes are known to be involved in the formation and degradation of various monomeric proteins, but the effect of proteases on the ordered protein aggregates, amyloid fibrils, which are considered to be extremely stable, remains poorly understood. In this work we study resistance to proteolytic degradation of lysozyme amyloid fibrils with two different types of morphology and beta-2-microglobulun amyloids. We showed that the proteolytic enzyme of the pancreas, trypsin, induced degradation of amyloid fibrils, and the mechanism of this process was qualitatively the same for all investigated amyloids. At the same time, we found a dependence of efficiency and rate of fibril degradation on the structure of the amyloid-forming protein as well as on the morphology and clustering of amyloid fibrils. It was assumed that the discovered relationship between fibrils structure and the efficiency of their degradation by trypsin can become the basis of a new express method for the analysis of amyloids polymorphism. Unexpectedly lower resistance of both types of lysozyme amyloids to trypsin exposure compared to the native monomeric protein (which is not susceptible to hydrolysis) was attributed to the higher availability of cleavage sites in studied fibrils. Another intriguing result of the work is that the cytotoxicity of amyloids treated with trypsin was not only failing to decline, but even increasing in the case of beta-2-microglobulin fibrils.
Indexed as
Identifiers
What OpenQuestion holds
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.