Evidence map›Paper›PMID 22247597›Full record

ArticleJournal of clinical biochemistry and nutrition2012

Thioredoxin binding protein (TBP)-2/Txnip and α-arrestin proteins in cancer and diabetes mellitus.

Hiroshi Masutani, Eiji Yoshihara, So Masaki, Zhe Chen, Junji Yodoi

Open access · bronzeAbstract read
In one paragraph

Article in Journal of clinical biochemistry and nutrition, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 67 citations in OpenAlex.

  1. Mutations in the Txnip PPXY motifs protect against myocardial infarction despite enhanced protein stability.American journal of physiology. Heart and circulatory physiology · 2026
    Article
  2. N6-methyladenosine (miScience · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Effects of multi-walled carbon nanotubes on gene and microRNA expression in human hepatocarcinoma HepG2 cells.Materials express : an international journal on multidisciplinary materials research · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Thioredoxin-Interacting Protein in Cancer and Diabetes.Antioxidants & redox signaling · 2022
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Early Predictors in the Onset of Type 2 Diabetes at Different Fasting Blood Glucose Levels.Diabetes, metabolic syndrome and obesity : targets and therapy · 2021
    Article
  19. TXNIP/TBP-2: A Master Regulator for Glucose Homeostasis.Antioxidants (Basel, Switzerland) · 2020
    Review
  20. 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

5 authors at 1 institution in 1 country.

Hiroshi MasutaniInstitute for Virus Research, Graduate School of Biostudies, Kyoto University, 53 Kawahara-cho, Shogoin, Sakyo, Kyoto 606-8507, Japan.
Eiji Yoshihara
So Masaki
Zhe Chen
Junji Yodoi
Kyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thioredoxin binding protein -2/ thioredoxin interacting protein is an α-arrestin protein that has attracted much attention as a multifunctional regulator. Thioredoxin binding protein -2 expression is downregulated in tumor cells and the level of thioredoxin binding protein is correlated with clinical stage of cancer. Mice with mutations or knockout of the thioredoxin binding protein -2 gene are much more susceptible to carcinogenesis than wild-type mice, indicating a role for thioredoxin binding protein -2 in cancer suppression. Studies have also revealed roles for thioredoxin binding protein -2 in metabolic control. Enhancement of thioredoxin binding protein -2 expression causes impairment of insulin sensitivity and glucose-induced insulin secretion, and β-cell apoptosis. These changes are important characteristics of type 2 diabetes mellitus. Thioredoxin binding protein -2 regulates transcription of metabolic regulating genes. Thioredoxin binding protein -2-like inducible membrane protein/ arrestin domain containing 3 regulates endocytosis of receptors such as the β(2)-adrenergic receptor. The α-arrestin family possesses PPXY motifs and may function as an adaptor/scaffold for NEDD family ubiquitin ligases. Elucidation of the molecular mechanisms of α-arrestin proteins would provide a new pharmacological basis for developing approaches against cancer and type 2 diabetes mellitus.

Indexed as

cancerdiabetes mellitusthioredoxin binding protein −2-like inducible membrane protein/ arrestin domain containing 3thioredoxin binding protein −2/ thioredoxin interacting proteinα-arrestin

Identifiers

PMID22247597
PMCPMC3246179
OpenAlexW53103779

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.