Evidence map›Paper›PMID 29103054›Full record

ReviewJournal of Parkinson's disease2017

Is the Enzyme ACMSD a Novel Therapeutic Target in Parkinson's Disease?

Keerthi Thirtamara-Rajamani, Peipei Li, Martha L Escobar Galvis, Viviane Labrie, Patrik Brundin, Lena Brundin

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of Parkinson's disease, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. NADGenes · 2021
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. NADSignal transduction and targeted therapy · 2020
    Review
  16. Review
  17. Article
  18. Article
  19. Review
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

6 authors at 1 institution in 1 country.

Keerthi Thirtamara-RajamaniCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, MI, USA.
Peipei LiCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, MI, USA.
Martha L Escobar GalvisCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, MI, USA.
Viviane LabrieCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, MI, USA.
Patrik BrundinCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, MI, USA.
Lena BrundinCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, MI, USA.
Van Andel Institute · US

Funding

Linking Synucleinopathy and Dysfunction of Olfactory PathwaysR01DC016519 · NIDCD · VAN ANDEL RESEARCH INSTITUTE · PI MOORE, DARREN JOHN, WESSON, DANIEL W · 2017 to 2021
$2.8M
Role of Kynurenine Pathway Metabolites in Perinatal Depression and SuicidalityR01MH104622 · NIMH · VAN ANDEL RESEARCH INSTITUTE · PI BRUNDIN, LENA CECILIA · 2014 to 2016
$1.2M
Does Microglial Activation Influence Propagation of Alpha-synuclein PathologyR21NS093993 · NINDS · VAN ANDEL RESEARCH INSTITUTE · PI BRUNDIN, PATRIK · 2016 to 2017
$523k
NIDCD NIH HHS R01 DC016519NIMH NIH HHS R01 MH104622NINDS NIH HHS R21 NS093993
6 · The paper itself

Abstract

Several large genome wide association studies have identified a locus in close proximity to the gene encoding the enzyme aminocarboxymuconate-semialdehyde-decarboxylase (ACMSD) to be associated with the risk for Parkinson's disease (PD), tentatively suggesting that this enzyme might influence PD pathogenesis. Further support for this comes from the recent identification of a disease-segregating stop codon mutation in ACMSD in a family with Parkinsonism, and a missense mutation in the ACMSD gene predicted to disrupt enzyme function in an individual with typical PD. ACMSD is part of the kynurenine pathway, responsible for the catalytic breakdown of tryptophan into NAD+, generating several neuroactive metabolites in the process. The enzyme is located at a key branch-point of the pathway, limiting the production of the neurotoxin quinolinic acid, which has excitotoxic and inflammatory properties. In this review, we discuss the genetic findings in light of the functions of ACMSD and its potential involvement in PD pathogenesis.

Indexed as

AnimalsBrainCarboxy-LyasesHumansInflammationMutationParkinson DiseaseQuinolinic Acidaminocarboxymuconate-semialdehyde decarboxylaseCarboxy-LyasesQuinolinic AcidACMSDexcitotoxicitykynurenine pathwayneuroinflammationoxidative stressParkinson’s disease

Identifiers

PMID29103054
PMCPMC5676848
OpenAlexW2766855729

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.