Evidence map›Paper›PMID 29051706›Full record

ArticleInternational journal of tryptophan research : IJTR2017

Investigation of the Tissue Distribution and Physiological Roles of Indoleamine 2,3-Dioxygenase-2.

Felicita F Jusof, Supun M Bakmiwewa, Silvia Weiser, Lay Khoon Too, Richard Metz, George C Prendergast, Stuart T Fraser, Nicholas H Hunt, Helen J Ball

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

Article in International journal of tryptophan research : IJTR, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 33% 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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.

  1. Pooled it
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  19. Novel Selective IDO1 Inhibitors with Isoxazolo[5,4-Pharmaceuticals (Basel, Switzerland) · 2021
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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

9 authors at 3 institutions in 3 countries.

Felicita F JusofMolecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, The University of Sydney, Camperdown, NSW, Australia.
Supun M BakmiwewaMolecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, The University of Sydney, Camperdown, NSW, Australia.
Silvia WeiserMolecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, The University of Sydney, Camperdown, NSW, Australia.
Lay Khoon TooMolecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, The University of Sydney, Camperdown, NSW, Australia.
Richard MetzNewLink Genetics Corporation, Ames, IA, USA.
George C PrendergastLankenau Institute for Medical Research, Wynnewood, PA, USA.
Stuart T FraserDiscipline of Physiology, Bosch Institute and School of Medical Sciences, The University of Sydney, Camperdown, NSW, Australia.
Nicholas H HuntMolecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, The University of Sydney, Camperdown, NSW, Australia.
Helen J BallMolecular Immunopathology Unit, Bosch Institute and School of Medical Sciences, The University of Sydney, Camperdown, NSW, Australia.
University of Sydney · AULankenau Institute for Medical Research · USNewLink Genetics (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Indoleamine 2,3-dioxygenase-2 (IDO2) is 1 of the 3 enzymes that can catalyze the first step in the kynurenine pathway of tryptophan metabolism. Of the 2 other enzymes, tryptophan 2,3-dioxygenase is highly expressed in the liver and has a role in tryptophan homeostasis, whereas indoleamine 2,3-dioxygenase-1 (IDO1) expression is induced by inflammatory stimuli. Indoleamine 2,3-dioxygenase-2 is reportedly expressed comparatively narrow, including in liver, kidney, brain, and in certain immune cell types, and it does not appear to contribute significantly to systemic tryptophan catabolism under normal physiological conditions. Here, we report the identification of an alternative splicing pattern, including the use of an alternative first exon, that is conserved in the mouse

Indexed as

indoleamine 2,3-dioxygenasekynurenineTryptophantryptophan 2,3-dioxygenase

Identifiers

PMID29051706
PMCPMC5638149
OpenAlexW2763160800

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

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.