ArticleJournal of medicinal chemistry2026
Discovery of Sulfonamide Pantothenate Kinase Activators and Elucidation of the Role of Isoform Selectivity in Cellular Pantothenate Kinase Activation.
Article in Journal of medicinal chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Therapeutic Advances in Major NBIA Disorders: Current Strategies and Translational Challenges.Neurology international · 2026Review
- Probing Allosteric Kinase Modulators as Next Game-Changers in Fighting Neurodegeneration.Journal of medicinal chemistry · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
Coenzyme A (CoA) biosynthesis is controlled by the four isoforms of the rate-limiting enzyme pantothenate kinase (PANK), whose tissue expression and subcellular localization regulate CoA homeostasis. Pantazines are positive allosteric modulators of PANK that increase cellular CoA levels by disrupting feedback inhibition by acyl-CoA esters. In this study, a structure-guided design was used to modify the Pantazine scaffold near the ATP-binding site to address metabolic liabilities of earlier leads. Replacement of a metabolically labile cyclopropyl group with a sulfonamide introduced a new hydrogen-bonding interaction with the γ-phosphate of ATP in the PANK3•ATP•Pantazine complex. This interaction improved ligand affinity, solubility, and metabolic stability. Analysis of isoform-specific inhibition revealed that cellular CoA elevation correlates with the difference in affinity between PANK3 and PANK1β, defining an "activation window" for CoA induction. Lead sulfonamide Pantazines were metabolically stable and increased hepatic CoA levels, supporting their potential for treating metabolic CoA deficiencies.
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.