Evidence map›Paper›PMID 29124681›Full record

ArticleNeurotoxicity research2018

Synergistic Toxicity of the Neurometabolites Quinolinic Acid and Homocysteine in Cortical Neurons and Astrocytes: Implications in Alzheimer's Disease.

Paula Pierozan, Helena Biasibetti-Brendler, Felipe Schmitz, Fernanda Ferreira, Carlos Alexandre Netto, Angela T S Wyse

Abstract read
PubMed Publisher
In one paragraph

Article in Neurotoxicity research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

9 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Homocysteine fibrillar assemblies display cross-talk with Alzheimer's disease β-amyloid polypeptide.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Homocysteine and Gliotoxicity.Neurotoxicity research · 2021
    Review
  8. Article
  9. Article
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.

Paula PierozanLaboratório de Neuroproteção e Doenças Metabólicas, Departamento de Bioquímica, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul, Rua Ramiro Barcelos 2600 anexo, Porto Alegre, RS, 90035-003, Brazil. paula.pierozan@ufrgs.br.ORCID 0000-0002-6111-7435
Helena Biasibetti-BrendlerLaboratório de Neuroproteção e Doenças Metabólicas, Departamento de Bioquímica, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul, Rua Ramiro Barcelos 2600 anexo, Porto Alegre, RS, 90035-003, Brazil.
Felipe SchmitzLaboratório de Neuroproteção e Doenças Metabólicas, Departamento de Bioquímica, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul, Rua Ramiro Barcelos 2600 anexo, Porto Alegre, RS, 90035-003, Brazil.
Fernanda FerreiraLaboratório de Neuroproteção e Doenças Metabólicas, Departamento de Bioquímica, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul, Rua Ramiro Barcelos 2600 anexo, Porto Alegre, RS, 90035-003, Brazil.
Carlos Alexandre NettoPrograma de Pós-Graduação em Ciências Biológicas: Bioquímica, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil.
Angela T S WyseLaboratório de Neuroproteção e Doenças Metabólicas, Departamento de Bioquímica, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul, Rua Ramiro Barcelos 2600 anexo, Porto Alegre, RS, 90035-003, Brazil.
Universidade Federal do Rio Grande do Sul · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The brain of patients affected by Alzheimer's disease (AD) develops progressive neurodegeneration linked to the formation of proteins aggregates. However, their single actions cannot explain the extent of brain damage observed in this disorder, and the characterization of co-adjuvant involved in the early toxic processes evoked in AD is essential. In this line, quinolinic acid (QUIN) and homocysteine (Hcy) appear to be involved in the AD neuropathogenesis. Herein, we investigate the effects of QUIN and Hcy on early toxic events in cortical neurons and astrocytes. Exposure of primary cortical cultures to these neurometabolites for 24 h induced concentration-dependent neurotoxicity. In addition, QUIN (25 μM) and Hcy (30 μM) triggered ROS production, lipid peroxidation, diminished of Na

Indexed as

Analysis of VarianceAnimalsAnnexin A5AstrocytesCells, CulturedCerebral CortexCoculture TechniquesDrug SynergismEmbryo, MammalianFemaleHomocysteineMembrane PotentialsMitochondriaNerve Tissue ProteinsNeuronsNeurotoxinsAnnexin A5HomocysteineNerve Tissue ProteinsNeurotoxinsQuinolinic AcidSodium-Potassium-Exchanging ATPaseThiobarbituric Acid Reactive SubstancesAlzheimer diseaseHomocysteineNa+,K+-ATPaseOxidative stressQuinolinic acid

Identifiers

PMID29124681
OpenAlexW2767838837

What OpenQuestion holds

Textmetadata
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.