ArticleeLife2018
3.3-Å resolution cryo-EM structure of human ribonucleotide reductase with substrate and allosteric regulators bound.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Who cites it
28 citing papers in PubMed, 54 citations in OpenAlex.
- Full-length structure of the anti-viral and pro-tumor DNA deaminase APOBEC3B.bioRxiv : the preprint server for biology · 2026Article
- How ATP and dATP reposition class III ribonucleotide reductase cone domains to regulate enzyme activity.Science advances · 2025Article
- Genetic dissection of Huntington's disease modification by variation at RRM2B.Human molecular genetics · 2025Article
- Cryo-EM captures the coordination of asymmetric electron transfer through a di-copper site in DPOR.Nature communications · 2025Article
- How ATP and dATP Act as Molecular Switches to Regulate Enzymatic Activity in the Prototypical Bacterial Class Ia Ribonucleotide Reductase.Biochemistry · 2024Article
- Article
- Structural insights into the initiation of free radical formation in the Class Ib ribonucleotide reductases in Mycobacteria.Current research in structural biology · 2024Article
- Metabolic clogging of mannose triggers dNTP loss and genomic instability in human cancer cells.eLife · 2023Article
- Inhibitors of the Cancer Target Ribonucleotide Reductase, Past and Present.Biomolecules · 2022Review
- A nucleotide-sensing oligomerization mechanism that controls NrdR-dependent transcription of ribonucleotide reductases.Nature communications · 2022Article
- Cryo-EM structure of the EBV ribonucleotide reductase BORF2 and mechanism of APOBEC3B inhibition.Science advances · 2022Article
- 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
- Still no Rest for the Reductases: Ribonucleotide Reductase (RNR) Structure and Function: An Update.Sub-cellular biochemistry · 2022Review
- Radicals in Biology: Your Life Is in Their Hands.Journal of the American Chemical Society · 2021Article
- Hydroxyurea-The Good, the Bad and the Ugly.Genes · 2021Review
- Solution Structure of the dATP-Inactivated Class I Ribonucleotide Reductase FromFrontiers in molecular biosciences · 2021Article
- Preventing ATP Degradation by ASO-Mediated Knockdown of CD39 and CD73 Results in A2aR-Independent Rescue of T Cell Proliferation.Molecular therapy. Nucleic acids · 2020Article
- Article
- Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets.Annual review of biochemistry · 2020Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Ribonucleotide reductases (RNRs) convert ribonucleotides into deoxyribonucleotides, a reaction essential for DNA replication and repair. Human RNR requires two subunits for activity, the α subunit contains the active site, and the β subunit houses the radical cofactor. Here, we present a 3.3-Å resolution structure by cryo-electron microscopy (EM) of a dATP-inhibited state of human RNR. This structure, which was determined in the presence of substrate CDP and allosteric regulators ATP and dATP, has three α
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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.