Evidence map›Paper›PMID 26397892›Full record

ReviewJournal of Huntington's disease2015

Indoleamine 2,3 Dioxygenase as a Potential Therapeutic Target in Huntington's Disease.

Gelareh Mazarei, Blair R Leavitt

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

Review in Journal of Huntington's disease, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

27 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  5. Vitamin B3 Biotech · 2023
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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

2 authors at 2 institutions in 1 country.

Gelareh MazareiCentre for Molecular Medicine & Therapeutics and Department of Medical Genetics, University of British Columbia, Vancouver, BC, Canada.
Blair R LeavittCentre for Molecular Medicine & Therapeutics and Department of Medical Genetics, University of British Columbia, Vancouver, BC, Canada.
University of British Columbia · CAUniversity of British Columbia Hospital · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Within the past decade, there has been increasing interest in the role of tryptophan (Trp) metabolites and the kynurenine pathway (KP) in diseases of the brain such as Huntington's disease (HD). Evidence is accumulating to suggest that this pathway is imbalanced in neurologic disease states. The KP diverges into two branches that can lead to production of either neuroprotective or neurotoxic metabolites. In one branch, kynurenine (Kyn) produced as a result of tryptophan (Trp) catabolism is further metabolized to neurotoxic metabolites such as 3-hydroxykunurenine (3-HK) and quinolinic acid (QA). In the other branch, Kyn is converted to the neuroprotective metabolite kynurenic acid (KA). The enzyme Indoleamine 2,3 dioxygenase (IDO1) catalyzes the conversion of Trp into Kyn, the first and rate-limiting enzymatic step of the KP. This reaction takes place throughout the body in multiple cell types as a required step in the degradation of the essential amino acid Trp. Studies of IDO1 in brain have focused primarily on a potential role in depression, immune tolerance associated with brain tumours, and multiple sclerosis; however the role of this enzyme in neurodegenerative disease has garnered significant attention in recent years. This review will provide a summary of the current understanding of the role of IDO1 in Huntington's disease and will assess this enzyme as a potential therapeutic target for HD.

Indexed as

Alzheimer DiseaseAnimalsHumansHuntington DiseaseIndoleamine-Pyrrole 2,3,-DioxygenaseKynurenineParkinson DiseaseSignal TransductionTryptophanIDO1 protein, humanIDO2 protein, humanIndoleamine-Pyrrole 2,3,-DioxygenaseKynurenineTryptophanhuntingtinHuntington’s diseaseindoleamine 2,3 dioxygenasekynurenine pathwayquinolinic acidtryptophan

Identifiers

PMID26397892
PMCPMC4923717
OpenAlexW2292886270

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.