ArticleNature structural & molecular biology2023
Human PRPS1 filaments stabilize allosteric sites to regulate activity.
Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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
21 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.
- Age-Dependent Progression of Neurological Involvement in PRPP Deficiency: Insights from a Four-Generation Family and Systematic Review.Biomolecules · 2026Pooled it
- The molecular basis of ADP-ribose pyrophosphorylation by a phage PRPS-like enzyme in NAD+ reconstitution.Nucleic acids research · 2026Article
- Large-scale quaternary structural transitions underlie gain of function of SPOP cancer mutations.Molecular cell · 2026Article
- Article
- Structural basis for a filamentous morpheein model of human cystathionine beta-synthase.Nature communications · 2026Article
- Enterocytes rely on purine biosynthesis/salvage pathway to facilitate dietary fat absorption.Nature communications · 2026Article
- Rate-limiting enzymes in nucleotide metabolism synchronize nucleotide biosynthesis and chromatin formation.Molecular cell · 2025Article
- The role of gene duplication and paralog specialisation in the evolution of the mammalian PRPS complex.Nature communications · 2025Article
- Product-stabilized filamentation by human glutamine synthetase allosterically tunes metabolic activity.bioRxiv : the preprint server for biology · 2025Article
- PRPS2 enhances RNA mNature communications · 2025Article
- Depletion of nuclear cytoophidia in Alzheimer's disease.Free neuropathology · 2025Article
- Structural basis for allosteric regulation of human phosphofructokinase-1.Nature communications · 2024Article
- Two-metal ion mechanism of DNA cleavage by activated, filamentous SgrAI.The Journal of biological chemistry · 2024Article
- Light-sensitive phosphorylation regulates retinal IMPDH1 activity and filament assembly.The Journal of cell biology · 2024Article
- Structural basis for allosteric regulation of human phosphofructokinase-1.bioRxiv : the preprint server for biology · 2024Article
- A three-level regulatory mechanism of the aldo-keto reductase subfamily AKR12D.Nature communications · 2024Article
- Filament formation drives catalysis by glutaminase enzymes important in cancer progression.Nature communications · 2024Article
- Direct stimulation of de novo nucleotide synthesis by O-GlcNAcylation.Nature chemical biology · 2024Article
- Neurodevelopmental disorder mutations in the purine biosynthetic enzyme IMPDH2 disrupt its allosteric regulation.The Journal of biological chemistry · 2023Article
- Structural basis of human PRPS2 filaments.Cell & bioscience · 2023Article
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 1 country.
Funding
Abstract
The universally conserved enzyme phosphoribosyl pyrophosphate synthetase (PRPS) assembles filaments in evolutionarily diverse organisms. PRPS is a key regulator of nucleotide metabolism, and mutations in the human enzyme PRPS1 lead to a spectrum of diseases. Here we determine structures of human PRPS1 filaments in active and inhibited states, with fixed assembly contacts accommodating both conformations. The conserved assembly interface stabilizes the binding site for the essential activator phosphate, increasing activity in the filament. Some disease mutations alter assembly, supporting the link between filament stability and activity. Structures of active PRPS1 filaments turning over substrate also reveal coupling of catalysis in one active site with product release in an adjacent site. PRPS1 filaments therefore provide an additional layer of allosteric control, conserved throughout evolution, with likely impact on metabolic homeostasis. Stabilization of allosteric binding sites by polymerization adds to the growing diversity of assembly-based enzyme regulatory mechanisms.
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.