ArticleBiochemistry2019
Selenocysteine Substitution in a Class I Ribonucleotide Reductase.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 14 citations in OpenAlex.
- Chemical modification of selenium-containing amino acids caused by non-thermal dielectric-barrier discharge atmospheric-pressure plasma.RSC advances · 2024Article
- Non-standard amino acid incorporation into thiol dioxygenases.Methods in enzymology · 2024Article
- Role of Water in Proton-Coupled Electron Transfer between Tyrosine and Cysteine in Ribonucleotide Reductase.Journal of the American Chemical Society · 2022Article
- Selenocysteine substitutions in thiyl radical enzymes.Methods in enzymology · 2022Article
- Using selenocysteine-specific reporters to screen for efficient tRNAMethods in enzymology · 2022Article
- Radicals in Biology: Your Life Is in Their Hands.Journal of the American Chemical Society · 2021Article
- Diversity of structures and functions of oxo-bridged non-heme diiron proteins.Archives of biochemistry and biophysics · 2021Review
- Selective cysteine-to-selenocysteine changes in a [NiFe]-hydrogenase confirm a special position for catalysis and oxygen tolerance.Proceedings of the National Academy of Sciences of the United States of America · 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
3 authors at 3 institutions in 1 country.
Funding
Abstract
Ribonucleotide reductases (RNRs) employ a complex radical-based mechanism during nucleotide reduction involving multiple active site cysteines that both activate the substrate and reduce it. Using an engineered allo-tRNA, we substituted two active site cysteines with distinct function in the class Ia RNR of
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.