ReviewThe Journal of biological chemistry2015
Specific chaperones and regulatory domains in control of amyloid formation.
Review in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 38 citations in OpenAlex.
- Segmental and global amyloid burden and myocardial mechanics: a multimodality imaging comparison.Journal of medicine and life · 2026Article
- Diagnostic Accuracy of Bisphosphonate Scintigraphy in Glu54GlnATTR Cardiomyopathy.Journal of clinical medicine · 2025Article
- Lung endothelium, tau, and amyloids in health and disease.Physiological reviews · 2024Review
- Article
- OAF: a new member of the BRICHOS family.Bioinformatics advances · 2022Article
- Neuroserpin and transthyretin are extracellular chaperones that preferentially inhibit amyloid formation.Science advances · 2021Article
- Spidroin-Based Biomaterials in Tissue Engineering: General Approaches and Potential Stem Cell Therapies.Stem cells international · 2021Review
- Optimization of expression and purification of mitochondrial HSP 40 (Tid1-L) chaperone: Role of mortalin and tid1 in the reactivation and amyloid inhibition of proteins.Saudi journal of biological sciences · 2020Article
- Growth Hormone(s), Testosterone, Insulin-Like Growth Factors, and Cortisol: Roles and Integration for Cellular Development and Growth With Exercise.Frontiers in endocrinology · 2020Review
- Bacterial functional amyloids: Order from disorder.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- The yeast stress inducible Ssa Hsp70 reduces α-synuclein toxicity by promoting its degradation through autophagy.PLoS genetics · 2018Article
- Elevated Surfactant Protein Levels and Increased Flow of Cerebrospinal Fluid in Cranial Magnetic Resonance Imaging.Molecular neurobiology · 2018Article
- Translational Control by Prion-like Proteins.Trends in cell biology · 2018Review
- Article
- Inhibition of Protein Aggregation by Several Antioxidants.Oxidative medicine and cellular longevity · 2018Article
- Antagonistic evolution of an antibiotic and its molecular chaperone: how to maintain a vital ectosymbiosis in a highly fluctuating habitat.Scientific reports · 2017Article
- The amyloid interactome: Exploring protein aggregation.PloS one · 2017Article
- Article
- Introduction to thematic series: protein interactions, structures, and networks.The Journal of biological chemistry · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many proteins can form amyloid-like fibrils in vitro, but only about 30 amyloids are linked to disease, whereas some proteins form physiological amyloid-like assemblies. This raises questions of how the formation of toxic protein species during amyloidogenesis is prevented or contained in vivo. Intrinsic chaperoning or regulatory factors can control the aggregation in different protein systems, thereby preventing unwanted aggregation and enabling the biological use of amyloidogenic proteins. The molecular actions of these chaperones and regulators provide clues to the prevention of amyloid disease, as well as to the harnessing of amyloidogenic proteins in medicine and biotechnology.
Indexed as
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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.