ArticleACS omega2017
Substituent, Charge, and Size Effects on the Fluorogenic Performance of Amyloid Ligands: A Small-Library Screening Study.
Article in ACS omega, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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.
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Who cites it
7 citing papers in PubMed.
- Fluorogenic Hyaluronan Nanogels Track Individual Early Protein Aggregates Originated under Oxidative Stress.ACS applied materials & interfaces · 2024Article
- Selective In Vitro and Ex Vivo Staining of Brain Neurofibrillary Tangles and Amyloid Plaques by Novel Ethylene Ethynylene-Based Optical Sensors.Biosensors · 2023Article
- Controlled and Selective Photo-oxidation of Amyloid-β Fibrils by OligomericACS applied materials & interfaces · 2022Article
- A Portrait of the OPE as a Biological Agent.Molecules (Basel, Switzerland) · 2021Review
- Highly Effective Inactivation of SARS-CoV-2 by Conjugated Polymers and Oligomers.ACS applied materials & interfaces · 2020Article
- Computational Investigation of the Binding Dynamics of OligoACS chemical neuroscience · 2020Article
- Nanomedical Relevance of the Intermolecular Interaction Dynamics-Examples from Lysozymes and Insulins.ACS omega · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Developing new molecular ligands for the direct detection and tracking of amyloid protein aggregates is key to understanding and defeating myriad neurodegenerative and other disorders including Alzheimer's and Parkinson's diseases. A crucial factor in the performance of an amyloid dye is its ability to detect the amyloid structural motif independent of the sequence of the amyloid-forming protomer. The current study investigates structure-function relationships of a class of novel phenyleneethynylene (PPE)-based dyes and fluorescent polymers using amyloid fibrils formed by two model proteins: lysozyme and insulin. A small library of 18 PPE compounds that vary in molecular weights, charge densities, water solubilities, and types and geometries of functional groups was tested. One compound, the small anionic oligo(
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Registered trials
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