ArticleMolecular medicine reports2016
Nuclear distribution of eIF3g and its interacting nuclear proteins in breast cancer cells.
Article in Molecular medicine reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- A CRY1 Interactor eIF3G1 Negatively Regulates Root Growth Under Blue Light inPlants (Basel, Switzerland) · 2026Article
- m6A readers, writers, erasers, and the m6A epitranscriptome in breast cancer.Journal of molecular endocrinology · 2023Review
- Long non-coding RNA LINC02446 suppresses the proliferation and metastasis of bladder cancer cells by binding with EIF3G and regulating the mTOR signalling pathway.Cancer gene therapy · 2021Article
- Emerging roles of N6-methyladenosine (mCell & bioscience · 2020Review
- Roles of eIF3m in the tumorigenesis of triple negative breast cancer.Cancer cell international · 2020Article
- High Survivin and Low Zinc Finger of the Cerebellum 1 Expression Indicates Poor Prognosis in Triple-negative Breast Carcinoma.Journal of breast cancer · 2019Article
- Eukaryotic translation initiation factor 3 subunit G promotes human colorectal cancer.American journal of translational research · 2019Article
- Eukaryotic translation initiation factor 3 subunit G (EIF3G) resensitized HCT116/5-Fu to 5-fluorouracil (5-Fu) via inhibition of MRP and MDR1.OncoTargets and therapy · 2018Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic translation initiation factor 3 subunit g (eIF3g) is a core subunit of the eukaryotic translation initiation factor 3 complex, and is important in the initiation of translation. It is also involved in caspase-mediated apoptosis, and is upregulated in multidrug-resistant cancer cells. In the present study, the nuclear distribution of eIF3g was determined by performing co-immunoprecipitation of proteins that potentially interact with eIF3g in the nucleus. Mass spectrometry characterization showed that three proteins, heterogeneous nuclear ribonucleoprotein U/scaffold attachment factor A, HSZFP36/zinc finger protein 823 and β‑actin, were among the candidate eIF3g‑interacting proteins in the nucleus. The protein‑protein interaction was further confirmed by cross‑linking and a glutathione S‑transferase pull‑down assay, followed by western blotting. The co‑localization of these proteins was determined by confocal microscopy. These findings provide novel insight into the possible functions of eIF3g in the nucleus and serves as an important first step for further investigation of the roles of eIF3g in cancer development.
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Registered trials
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 Socratic graph.