Evidence map›Paper›PMID 25346733›Full record

ReviewFrontiers in immunology2014

Tryptophan-catabolizing enzymes - party of three.

Helen J Ball, Felicita F Jusof, Supun M Bakmiwewa, Nicholas H Hunt, Hajime J Yuasa

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Frontiers in immunology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed, 2 pooled it
5.7field-weighted citation impact, top 3% of its field
1 · What the graph read from 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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

101 citing papers in PubMed, 2 syntheses or guidelines pooled it, 172 citations in OpenAlex.

  1. Pooled it
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  6. Review
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  12. Metabolomics of HIV in the Modern cART Era.Advances in experimental medicine and biology · 2026
    Review
  13. Tryptophan's Journey Through Pregnancy: The Role of Serotonin.International journal of tryptophan research : IJTR · 2026
    Review
  14. Article
  15. Article
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41 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 3 countries.

Helen J BallMolecular Immunopathology Unit, School of Medical Sciences and Bosch Institute, University of Sydney , Sydney, NSW , Australia.
Felicita F JusofMolecular Immunopathology Unit, School of Medical Sciences and Bosch Institute, University of Sydney , Sydney, NSW , Australia ; Department of Physiology, Faculty of Medicine, University of Malaya , Kuala Lumpur , Malaysia.
Supun M BakmiwewaMolecular Immunopathology Unit, School of Medical Sciences and Bosch Institute, University of Sydney , Sydney, NSW , Australia.
Nicholas H HuntMolecular Immunopathology Unit, School of Medical Sciences and Bosch Institute, University of Sydney , Sydney, NSW , Australia.
Hajime J YuasaLaboratory of Biochemistry, Faculty of Science, Department of Applied Science, National University Corporation Kochi University , Kochi , Japan.
University of Sydney · AUKōchi University · JPUniversity of Malaya · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that have independently evolved to catalyze the first step in tryptophan catabolism via the kynurenine pathway (KP). The depletion of tryptophan and formation of KP metabolites modulates the activity of the mammalian immune, reproductive, and central nervous systems. IDO and TDO enzymes can have overlapping or distinct functions depending on their expression patterns. The expression of TDO and IDO enzymes in mammals differs not only by tissue/cellular localization but also by their induction by distinct stimuli. To add to the complexity, these genes also have undergone duplications in some organisms leading to multiple isoforms of IDO or TDO. For example, many vertebrates, including all mammals, have acquired two IDO genes via gene duplication, although the IDO1-like gene has been lost in some lower vertebrate lineages. Gene duplications can allow the homologs to diverge and acquire different properties to the original gene. There is evidence for IDO enzymes having differing enzymatic characteristics, signaling properties, and biological functions. This review analyzes the evolutionary convergence of IDO and TDO enzymes as tryptophan-catabolizing enzymes and the divergent evolution of IDO homologs to generate an enzyme family with diverse characteristics not possessed by TDO enzymes, with an emphasis on the immune system.

Indexed as

convergent evolutiondivergent evolutiongene duplicationimmunoregulationindoleamine 2,3-dioxygenasetryptophan 2,3-dioxygenase

Identifiers

PMID25346733
PMCPMC4191572
OpenAlexW2169306316

What OpenQuestion holds

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Registered trials

None linked

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.