ArticleMethods in molecular biology (Clifton, N.J.)2016
Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins.
Article in Methods in molecular biology (Clifton, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Physics of Protein Aggregation in Normal and Accelerated Brain Aging.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Heterosubstituted Derivatives of PtPFPP for OBioconjugate chemistry · 2022Article
- Characterization of Amyloidogenic Peptide Aggregability in Helical Subspace.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The protein-surfactant stoichiometry governs the conformational switching and amyloid nucleation kinetics of tau K18.European biophysics journal : EBJ · 2020Article
- Long-range Regulation of Partially Folded Amyloidogenic Peptides.Scientific reports · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Amyloid formation and aberrant protein aggregation are hallmarks of more than 30 different human diseases. The proteins that form amyloid can be divided into two structural classes: those that form compact, well-ordered, globular structures in their unaggregated state and those that are intrinsically disordered in their unaggregated states. The latter include the Aβ peptide of Alzheimer's disease, islet amyloid polypeptide (IAPP, amylin) implicated in type 2 diabetes and α-synuclein, which is linked to Parkinson's disease. Work in the last 10 years has highlighted the potential role of pre-amyloid intermediates in cytotoxicity and has focused attention on their properties. A number of intrinsically disordered proteins appear to form helical intermediates during amyloid formation. We discuss the spectroscopic methods employed to detect and characterize helical intermediates in homogenous solution and in membrane-catalyzed amyloid formation, with the emphasis on the application of circular dichroism (CD). IAPP is used as an example, but the methods are generally applicable.
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.