Evidence map›Paper›PMID 38138960›Full record

ArticleInternational journal of molecular sciences2023

Endoplasmic Reticulum Protein TXNDC5 Interacts with PRDX6 and HSPA9 to Regulate Glutathione Metabolism and Lipid Peroxidation in the Hepatic AML12 Cell Line.

Seyed Hesamoddin Bidooki, Javier Sánchez-Marco, Roberto Martínez-Beamonte, Tania Herrero-Continente, María A Navarro, María J Rodríguez-Yoldi, Jesús Osada

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

8 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Thioredoxin Domain Containing 5 (TXNDC5): Friend or Foe?Current issues in molecular biology · 2024
    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

7 authors at 2 institutions in 2 countries.

Seyed Hesamoddin BidookiDepartamento de Bioquímica y Biología Molecular y Celular, Facultad de Veterinaria, Instituto de Investigación Sanitaria de Aragón, Universidad de Zaragoza, E-50013 Zaragoza, Spain.ORCID 0000-0002-5612-5000
Javier Sánchez-MarcoDepartamento de Bioquímica y Biología Molecular y Celular, Facultad de Veterinaria, Instituto de Investigación Sanitaria de Aragón, Universidad de Zaragoza, E-50013 Zaragoza, Spain.ORCID 0000-0002-9023-741X
Roberto Martínez-BeamonteDepartamento de Bioquímica y Biología Molecular y Celular, Facultad de Veterinaria, Instituto de Investigación Sanitaria de Aragón, Universidad de Zaragoza, E-50013 Zaragoza, Spain.ORCID 0000-0002-8100-5596
Tania Herrero-ContinenteDepartamento de Bioquímica y Biología Molecular y Celular, Facultad de Veterinaria, Instituto de Investigación Sanitaria de Aragón, Universidad de Zaragoza, E-50013 Zaragoza, Spain.
María A NavarroDepartamento de Bioquímica y Biología Molecular y Celular, Facultad de Veterinaria, Instituto de Investigación Sanitaria de Aragón, Universidad de Zaragoza, E-50013 Zaragoza, Spain.ORCID 0000-0002-0108-1004
María J Rodríguez-YoldiInstituto Agroalimentario de Aragón, CITA-Universidad de Zaragoza, E-50013 Zaragoza, Spain.ORCID 0000-0002-3595-7668
Jesús OsadaDepartamento de Bioquímica y Biología Molecular y Celular, Facultad de Veterinaria, Instituto de Investigación Sanitaria de Aragón, Universidad de Zaragoza, E-50013 Zaragoza, Spain.ORCID 0000-0002-8251-8457
Universidad de Zaragoza · ESCentre National de la Recherche Scientifique · FR

Funding

CIBER Fisiopatología de la Obesidad y Nutrición as initiative of FEDER-ISCIII CIBEROBN, CB06/03/1012Fondo Social Europeo-Gobierno de Aragón B16_23RMinisterio de Ciencia e Innovación-Fondo Europeo de Desarrollo Regional PID2019-104915RB-I00 and PID2022-104915RB-I00The proteomic analysis was performed in the Proteomics Unit of Complutense University of Madrid, a member of ProteoRed PT17/0019, of the PE I+D+i 2013-2016, funded by ISCIII and ERDF." Or "Grant PRB3 (IPT17/0019 - ISCIII-SGEFI / ERDF)
6 · The paper itself

Abstract

Non-alcoholic fatty liver disease or steatosis is an accumulation of fat in the liver. Increased amounts of non-esterified fatty acids, calcium deficiency, or insulin resistance may disturb endoplasmic reticulum (ER) homeostasis, which leads to the abnormal accumulation of misfolded proteins, activating the unfolded protein response. The ER is the primary location site for chaperones like thioredoxin domain-containing 5 (TXNDC5). Glutathione participates in cellular oxidative stress, and its interaction with TXNDC5 in the ER may decrease the disulfide bonds of this protein. In addition, glutathione is utilized by glutathione peroxidases to inactivate oxidized lipids. To characterize proteins interacting with TXNDC5, immunoprecipitation and liquid chromatography-mass spectrometry were used. Lipid peroxidation, reduced glutathione, inducible phospholipase A

Indexed as

Protein Disulfide-IsomerasesThioredoxinsAnimalsCarrier ProteinsCell LineEndoplasmic ReticulumEndoplasmic Reticulum StressGlutathioneHSP70 Heat-Shock ProteinsLipid MetabolismLipid PeroxidationLiverMicePeroxiredoxin VIPhospholipases A2, Calcium-IndependentCarrier ProteinsGlutathioneHSP70 Heat-Shock ProteinsHspa9 protein, mousePeroxiredoxin VIPhospholipases A2, Calcium-IndependentPrdx6 protein, mouseProtein Disulfide-IsomerasesThioredoxinsendoplasmic reticulumglutathioneHSPA9lipid peroxidationliverPRDX6protein interactionTXNDC5

Identifiers

PMID38138960
PMCPMC10743020
OpenAlexW4389346581

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.