ArticleChemistry (Weinheim an der Bergstrasse, Germany)2017
An Iridium(III) Complex as a Photoactivatable Tool for Oxidation of Amyloidogenic Peptides with Subsequent Modulation of Peptide Aggregation.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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.
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Who cites it
10 citing papers in PubMed.
- 2-Phenylbenzothiazolyl iridium complexes as inhibitors and probes of amyloid β aggregation.Dalton transactions (Cambridge, England : 2003) · 2024Article
- Oxidative Damages on the Alzheimer's Related-Aβ Peptide Alters Its Ability to Assemble.Antioxidants (Basel, Switzerland) · 2023Article
- Excited-State Intramolecular Hydrogen Transfer of Compact Molecules Controls Amyloid Aggregation Profiles.JACS Au · 2022Article
- Modification of amyloid-beta peptide aggregationChemical science · 2021Article
- Multiple reactivities of flavonoids towards pathological elements in Alzheimer's disease: structure-activity relationship.Chemical science · 2020Article
- Investigating in Vitro Amyloid Peptide 1-42 Aggregation: Impact of Higher Molecular Weight Stable Adducts.ACS omega · 2019Article
- Chemical strategies to modify amyloidogenic peptides using iridium(iii) complexes: coordination and photo-induced oxidation.Chemical science · 2019Article
- A cationic polymethacrylate-copolymer acts as an agonist for β-amyloid and an antagonist for amylin fibrillation.Chemical science · 2019Article
- Platinum(II)International journal of molecular sciences · 2019Article
- DFT Investigation of Ligand Photodissociation in [RuInorganic chemistry · 2018Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Aggregates of amyloidogenic peptides are involved in the pathogenesis of several degenerative disorders. Herein, an iridium(III) complex, Ir-1, is reported as a chemical tool for oxidizing amyloidogenic peptides upon photoactivation and subsequently modulating their aggregation pathways. Ir-1 was rationally designed based on multiple characteristics, including 1) photoproperties leading to excitation by low-energy radiation; 2) generation of reactive oxygen species responsible for peptide oxidation upon photoactivation under mild conditions; and 3) relatively easy incorporation of a ligand on the Ir
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