ArticleChemical science2016
Radical transfer in
Article in Chemical science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed.
- Asymmetric Connectivity Between Redox-Active Tyrosines and Reaction-Center Chlorophylls in Photosystem II.Plants (Basel, Switzerland) · 2026Article
- Low-barrier hydrogen bond powers long-range radical transfer in the metal-free ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- Conformationally gated multisite proton-coupled electron transfer in the ribonucleotide reductaseProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Real-time assay of ribonucleotide reductase activity with a fluorescent RNA aptamer.FEBS letters · 2026Article
- Biological semiconductors: self-assembled shell proteins as photoactive materials.Chemical science · 2026Article
- Hydrogen Tunneling and Conformational Motions in Nonadiabatic Proton-Coupled Electron Transfer between Interfacial Tyrosines in Ribonucleotide Reductase.Journal of the American Chemical Society · 2025Article
- 2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor NProceedings of the National Academy of Sciences of the United States of America · 2024Article
- 2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor NbioRxiv : the preprint server for biology · 2024Article
- Conformational control over proton-coupled electron transfer in metalloenzymes.Nature reviews. Chemistry · 2024Review
- Spectroscopically Orthogonal Labelling to Disentangle Site-Specific Nitroxide Label Distributions.Applied magnetic resonance · 2024Article
- Exploring Proton-Coupled Electron Transfer at Multiple Scales.Nature computational science · 2023Article
- Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2023Article
- Direct Proton-Coupled Electron Transfer between Interfacial Tyrosines in Ribonucleotide Reductase.Journal of the American Chemical Society · 2023Article
- Article
- Role of Water in Proton-Coupled Electron Transfer between Tyrosine and Cysteine in Ribonucleotide Reductase.Journal of the American Chemical Society · 2022Article
- In-Cell Characterization of the Stable Tyrosyl Radical in E. coli Ribonucleotide Reductase Using Advanced EPR Spectroscopy.Angewandte Chemie (International ed. in English) · 2021Article
- Detection of Water Molecules on the Radical Transfer Pathway of Ribonucleotide Reductase byJournal of the American Chemical Society · 2021Article
- Glutamate Mediates Proton-Coupled Electron Transfer Between Tyrosines 730 and 731 inJournal of the American Chemical Society · 2021Article
- Gated Proton Release during Radical Transfer at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotides to deoxyribonucleotides in all living organisms. The catalytic cycle of
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.