ArticleThe Journal of biological chemistry2018
Aggregation-phase diagrams of β
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 41 citations in OpenAlex.
- Small bites for big problems: stepwise aggregate degradation by autophagy.Biochemical Society transactions · 2026Review
- Quantitative Analysis of Amyloid Fibril Nucleation by Linking Folding and Nucleation Pathways Using a Robust Ultrasonic Assay.ACS omega · 2026Article
- Production of Distinct Fibrillar, Oligomeric, and Other Aggregation States from Network Models of Multibody Interaction.Journal of chemical theory and computation · 2024Article
- Chemical Modification of the Amino Groups of Human Insulin: Investigating Structural Properties and Amorphous Aggregation of Acetylated Species.The protein journal · 2023Article
- Disease-relevant βNature communications · 2023Article
- A constant domain mutation in a patient-derived antibody light chain reveals principles of AL amyloidosis.Communications biology · 2023Article
- The influence of cations on α-lactalbumin amyloid aggregation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022Review
- Polyphenol-solubility alters amyloid fibril formation of α-synuclein.Protein science : a publication of the Protein Society · 2021Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Breakdown of supersaturation barrier links protein folding to amyloid formation.Communications biology · 2021Article
- Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods.Molecules (Basel, Switzerland) · 2020Review
- Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism.Current research in structural biology · 2020Article
- Heating during agitation of βThe Journal of biological chemistry · 2019Article
- Polyphosphates diminish solubility of a globular protein and thereby promote amyloid aggregation.The Journal of biological chemistry · 2019Article
- Possible mechanisms of polyphosphate-induced amyloid fibril formation of βProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several serious diseases are associated with crystal-like amyloid fibrils or glass-like amorphous aggregates of denatured proteins. However, protein aggregation involving both types of aggregates has not yet been elucidated in much detail. Using a protein associated with dialysis-related amyloidosis, β
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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.