ReviewNeurobiology of aging2016
What amyloid ligands can tell us about molecular polymorphism and disease.
Review in Neurobiology of aging, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Tracking of Neuroinflammation Dynamics During Combined Anti-β-Amyloid Therapy (AAT) and Immunomodulation in a Preclinical Alzheimer's Disease Model.International journal of molecular sciences · 2026Article
- Ligands for Protein Fibrils of Amyloid-β, α-Synuclein, and Tau.Chemical reviews · 2025Review
- Ligand Profiling to Characterize Different Polymorphic Forms of α-Synuclein Aggregates.Journal of the American Chemical Society · 2023Article
- Discovery of High-Affinity Amyloid Ligands Using a Ligand-Based Virtual Screening Pipeline.Journal of the American Chemical Society · 2023Article
- Small molecule induced toxic human-IAPP species characterized by NMR.Chemical communications (Cambridge, England) · 2020Article
- Repurposing Triphenylmethane Dyes to Bind to Trimers Derived from Aβ.Journal of the American Chemical Society · 2018Article
- Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate.eLife · 2017Article
- Generation of Clickable Pittsburgh Compound B for the Detection and Capture of β-Amyloid in Alzheimer's Disease Brain.Bioconjugate chemistry · 2017Article
- Anionic Oligothiophenes Compete for Binding of X-34 but not PIB to Recombinant Aβ Amyloid Fibrils and Alzheimer's Disease Brain-Derived Aβ.Chemistry (Weinheim an der Bergstrasse, Germany) · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Brain-penetrant positron emission tomography imaging ligands selective for amyloid pathology in living subjects have sparked a revolution in presymptomatic biomarkers for Alzheimer's disease progression. As additional chemical structures were investigated, the heterogeneity of ligand-binding sites became apparent, as did discrepancies in binding of some ligands between human disease and animal models. These differences and their implications have received little attention. This review discusses the impact of different ligand-binding sites and misfolded protein conformational polymorphism on the interpretation of imaging data acquired with different ligands. Investigation of the differences in binding in animal models may identify pathologic processes informing improvements to these models for more faithful recapitulation of this uniquely human disease. The differential selectivity for binding of particular ligands to different conformational states could potentially be harnessed to better define disease progression and improve the prediction of clinical outcomes.
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.