ArticleThe Journal of biological chemistry2018
A glutaredoxin domain fused to the radical-generating subunit of ribonucleotide reductase (RNR) functions as an efficient RNR reductant.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- A Structurally Divergent Class Ia Ribonucleotide Reductase from a Tick-Borne Pathogen.Biochemistry · 2025Article
- Article
- Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction.Nature communications · 2024Article
- A nucleotide-sensing oligomerization mechanism that controls NrdR-dependent transcription of ribonucleotide reductases.Nature communications · 2022Article
- Article
- Solution Structure of the dATP-Inactivated Class I Ribonucleotide Reductase FromFrontiers in molecular biosciences · 2021Article
- A ribonucleotide reductase fromThe Journal of biological chemistry · 2020Article
- Cell-cycle-dependent phosphorylation of RRM1 ensures efficient DNA replication and regulates cancer vulnerability to ATR inhibition.Oncogene · 2020Article
- Class Id ribonucleotide reductase utilizes a MnJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Reannotation of the Ribonucleotide Reductase in a Cyanophage Reveals Life History Strategies Within the Virioplankton.Frontiers in microbiology · 2019Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Class I ribonucleotide reductase (RNR) consists of a catalytic subunit (NrdA) and a radical-generating subunit (NrdB) that together catalyze reduction of ribonucleotides to their corresponding deoxyribonucleotides. NrdB from the firmicute
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Registered trials
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