ArticleJournal of fluorescence2026
Indoleamine-2,3-Dioxygenase 1 Enzyme Inhibition: a Useful Target to Screen Chemicals for their Therapeutic Potential.
Article in Journal of fluorescence, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Phytochemical Modulation of the Kynurenine Pathway (KYNP) and Its Emerging Mechanistic Insights into Cancer Progression: A Systematic Review.International journal of molecular sciences · 2026Pooled it
- Formulation development and preclinical assessment of ethyl acetate fraction of Saraca asoca (EASA) flowers for cataract management.International ophthalmology · 2026Article
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Indoleamine 2,3-dioxygenase 1 (IDO1) is a key immunoregulatory enzyme that catalyzes the oxidative cleavage of L-tryptophan to N-formyl kynurenine, playing a critical role in immune tolerance and various pathological conditions, including cancer, autoimmune diseases, cataractogenesis, and neurodegenerative disorders. In this study, molecular docking was performed using a phytochemical library to identify compounds with strong binding affinity and favorable interactions within the IDO1 active site. Based on these in silico findings, selected compounds were further evaluated using a newly developed and cost-effective optimized fluorescence-based assay employing lens homogenate enzyme preparations to quantitatively assess IDO1 activity. Dose-response experiments revealed that several phytochemicals exhibited significant concentration-dependent inhibition of IDO1, with promising IC₅₀ values. The consistency between docking results and experimental inhibition supports the potential of these compounds as IDO1 inhibitors. This integrated in silico-in vitro approach provides a reliable platform for screening IDO1 modulators and identifies promising natural inhibitors for further development as therapeutics for IDO1-associated diseases.
Indexed as
Identifiers
41055823What 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.