ArticleeLife2016
Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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.
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Who cites it
48 citing papers in PubMed, 79 citations in OpenAlex.
- 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
- How ATP and dATP reposition class III ribonucleotide reductase cone domains to regulate enzyme activity.Science advances · 2025Article
- Identification of Fibrillarin and Cajal Bodies Under DNA Replication Stress Conditions in Root Meristem Cells ofInternational journal of molecular sciences · 2025Article
- Metabolic Origin, Role and Fate of the Denaturant Guanidine.Microbial biotechnology · 2025Article
- Resolving early embryonic metabolism in Drosophila through single-embryo metabolomics and transcriptomics.Nature metabolism · 2025Article
- Profile of Catherine Drennan.Proceedings 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 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
- How ATP and dATP Act as Molecular Switches to Regulate Enzymatic Activity in the Prototypical Bacterial Class Ia Ribonucleotide Reductase.Biochemistry · 2024Article
- Structural insights into the initiation of free radical formation in the Class Ib ribonucleotide reductases in Mycobacteria.Current research in structural biology · 2024Article
- dATP elevation induces myocardial metabolic remodeling to support improved cardiac function.Journal of molecular and cellular cardiology · 2023Article
- Allosteric crosstalk in modular proteins: Function fine-tuning and drug design.Computational and structural biotechnology journal · 2023Review
- Analysis of insertions and extensions in the functional evolution of the ribonucleotide reductase family.Protein science : a publication of the Protein Society · 2022Article
- Comprehensive phylogenetic analysis of the ribonucleotide reductase family reveals an ancestral clade.eLife · 2022Article
- Article
- Inhibitors of the Cancer Target Ribonucleotide Reductase, Past and Present.Biomolecules · 2022Review
- 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
- Article
- Structural and Biochemical Investigation of Class I Ribonucleotide Reductase from the HyperthermophileBiochemistry · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Ribonucleotide reductase (RNR) converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair. This enzyme is responsible for reducing all four ribonucleotide substrates, with specificity regulated by the binding of an effector to a distal allosteric site. In all characterized RNRs, the binding of effector dATP alters the active site to select for pyrimidines over purines, whereas effectors dGTP and TTP select for substrates ADP and GDP, respectively. Here, we have determined structures of Escherichia coli class Ia RNR with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how RNR 'reads' the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell.
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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.