ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2023
Structure, mechanism and inhibition of anthranilate phosphoribosyltransferase.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 15 citations in OpenAlex.
- Integrating image-based phenotyping and GWAS to map resistance to spittlebug nymphs in interspecific Urochloa grasses.G3 (Bethesda, Md.) · 2026Article
- Structure-Based Virtual Screening of Potential Inhibitors Targeting the Prolyl-tRNA Synthetase (PRS) inMolecules (Basel, Switzerland) · 2025Article
- Article
- Fermentative aminopyrrolnitrin production by metabolically engineered Corynebacterium glutamicum.Microbial cell factories · 2024Article
- Phosphoribosyltransferases and Their Roles in Plant Development and Abiotic Stress Response.International journal of molecular sciences · 2023Review
- Reactivity and mechanism in chemical and synthetic biology.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Article
- Path Integral-Free Energy Perturbation (PI-FEP) Simulations: Kinetic Isotope Effects of Proton/Deuteron Transfer Reactions in Aqueous Solution.Wiley interdisciplinary reviews. Computational molecular scienceArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Anthranilate phosphoribosyltransferase catalyses the second reaction in the biosynthesis of tryptophan from chorismate in microorganisms and plants. The enzyme is homodimeric with the active site located in the hinge region between two domains. A range of structures in complex with the substrates, substrate analogues and inhibitors have been determined, and these have provided insights into the catalytic mechanism of this enzyme. Substrate 5-phospho-d-ribose 1-diphosphate (PRPP) binds to the C-terminal domain and coordinates to Mg
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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.