ArticleThe Journal of biological chemistry2020
A single amino acid substitution uncouples catalysis and allostery in an essential biosynthetic enzyme in
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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
8 citing papers in PubMed, 18 citations in OpenAlex.
- An integrated in silico and in vitro approach to decipher the anti-tubercular potential of novel thiazetidine scaffolds.Journal of computer-aided molecular design · 2026Article
- Structural basis of allosteric activation of Mycobacterium tuberculosis isocitrate lyase 2.Communications biology · 2026Article
- Retracing the path of evolution: polymorphisms ofEmerging microbes & infections · 2025Article
- Prediction and confirmation of a switch-like region within the N-terminal domain of hSIRT1.Biochemistry and biophysics reports · 2022Article
- Point mutations that boost aromatic amino acid production and COScience advances · 2022Article
- Design and engineering of allosteric communications in proteins.Current opinion in structural biology · 2022Review
- Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021Review
- Evolving the naturally compromised chorismate mutase from Mycobacterium tuberculosis to top performance.The Journal of biological chemistry · 2020Article
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
No grant is acknowledged in the PubMed record.
Abstract
Allostery exploits the conformational dynamics of enzymes by triggering a shift in population ensembles toward functionally distinct conformational or dynamic states. Allostery extensively regulates the activities of key enzymes within biosynthetic pathways to meet metabolic demand for their end products. Here, we have examined a critical enzyme, 3-deoxy-d-
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.