ArticleThe Journal of biological chemistry2017
Glutamate 52-β at the α/β subunit interface of
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 36 citations in OpenAlex.
- Allosteric gating of radical transport in ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Conformationally gated multisite proton-coupled electron transfer in the ribonucleotide reductaseProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry.Nature communications · 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
- Structural insights into the initiation of free radical formation in the Class Ib ribonucleotide reductases in Mycobacteria.Current research in structural biology · 2024Article
- Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2023Article
- Article
- Effects of chameleon dispense-to-plunge speed on particle concentration, complex formation, and final resolution: A case study using the Neisseria gonorrhoeae ribonucleotide reductase inactive complex.Journal of structural biology · 2022Article
- Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes.Sub-cellular biochemistry · 2022Article
- Article
- Radicals in Biology: Your Life Is in Their Hands.Journal of the American Chemical Society · 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
- Conformational Motions and Water Networks at the α/β Interface inJournal of the American Chemical Society · 2020Article
- Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets.Annual review of biochemistry · 2020Review
- Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex.Science (New York, N.Y.) · 2020Article
- Evidence of Destabilization of the Human Thymidylate Synthase (hTS) Dimeric Structure Induced by the Interface Mutation Q62R.Biomolecules · 2019Article
- Photochemical Rescue of a Conformationally Inactivated Ribonucleotide Reductase.Journal of the American Chemical Society · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Ribonucleotide reductases (RNRs) catalyze the conversion of nucleoside diphosphate substrates (S) to deoxynucleotides with allosteric effectors (e) controlling their relative ratios and amounts, crucial for fidelity of DNA replication and repair.
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.