ReviewInternational journal of molecular sciences2020
Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins.
Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
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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
11 citing papers in PubMed, 25 citations in OpenAlex.
- Sensing and Filtering Environmental Fluctuations: The Case of Biomolecular Condensates in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Membrane charge primes the necroptotic kinase RIPK3 for amyloid assembly.Communications chemistry · 2025Article
- Functional constraints of wtf killer meiotic drivers.PLoS genetics · 2025Article
- Functional constraints ofbioRxiv : the preprint server for biology · 2025Article
- Characterization of acrosin and acrosin binding protein as novel CRISP2 interacting proteins in boar spermatozoa.Andrology · 2023Article
- Amyloid-like RIP1/RIP3 RHIM Fragments' Characterization and Application as a Drug Depot.Molecules (Basel, Switzerland) · 2023Article
- The fate of porcine sperm CRISP2 from the perinuclear theca before and after in vitro fertilization†.Biology of reproduction · 2022Article
- Synucleinopathy in Amyotrophic Lateral Sclerosis: A Potential Avenue for Antisense Therapeutics?International journal of molecular sciences · 2022Review
- Genome-Wide Characterization and Expression Analysis of Pathogenesis-Related 1 (International journal of molecular sciences · 2022Article
- Review
- The less conserved metal-binding site in human CRISP1 remains sensitive to zinc ions to permit protein oligomerization.Scientific reports · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The idea that amyloid fibrils and other types of protein aggregates are toxic for cells has been challenged by the discovery of a variety of functional aggregates. However, an identification of crucial differences between pathological and functional aggregation remains to be explored. Functional protein aggregation is often reversible by nature in order to respond properly to changing physiological conditions of the cell. In addition, increasing evidence indicates that fast fibril growth is a feature of functional amyloids, providing protection against the long-term existence of potentially toxic oligomeric intermediates. It is becoming clear that functional protein aggregation is a complexly organized process that can be mediated by a multitude of biomolecular factors. In this overview, we discuss the roles of diverse biomolecules, such as lipids/membranes, glycosaminoglycans, nucleic acids and metal ions, in regulating functional protein aggregation. Our studies on the protein GAPR-1 revealed that several of these factors influence the amyloidogenic properties of this protein. These observations suggest that GAPR-1, as well as the cysteine-rich secretory proteins, antigen 5 and pathogenesis-related proteins group 1 (CAP) superfamily of proteins that it belongs to, require the assembly into an amyloid state to exert several of their functions. A better understanding of functional aggregate formation may also help in the prevention and treatment of amyloid-related diseases.
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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.