ArticleThe EMBO journal2000
Nuclear export signal located within theDNA-binding domain of the STAT1transcription factor.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 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.
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.
Who cites it
82 citing papers in PubMed, 197 citations in OpenAlex.
- Selinexor potentiates NK cell activation against multiple myeloma.Clinical and experimental immunology · 2026Article
- HDAC1 and HDAC2 Are Involved in Influenza A Virus-Induced Nuclear Translocation of Ectopically Expressed STAT3-GFP.Viruses · 2024Article
- Review
- Targeting and Monitoring Acute Myeloid Leukaemia with Nucleophosmin-1 (International journal of molecular sciences · 2023Review
- Genetic and Functional Identifying of Novel STAT1 Loss-of-Function Mutations in Patients with Diverse Clinical Phenotypes.Journal of clinical immunology · 2022Article
- Deactivation of the antiviral state by rabies virus through targeting and accumulation of persistently phosphorylated STAT1.PLoS pathogens · 2022Article
- A coherent FOXO3-SNAI2 feed-forward loop in autophagy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Crosstalk between nucleocytoplasmic trafficking and the innate immune response to viral infection.The Journal of biological chemistry · 2021Review
- The Interplay Between Coronavirus and Type I IFN Response.Frontiers in microbiology · 2021Review
- FABP7 Regulates Acetyl-CoA Metabolism Through the Interaction with ACLY in the Nucleus of Astrocytes.Molecular neurobiology · 2020Article
- Protocol for Designing Small-Molecule-Regulated Destabilizing Domains forSTAR protocols · 2020Article
- Phospho-Ser727 triggers a multistep inactivation of STAT3 by rapid dissociation of pY705-SH2 through C-terminal tail modulation.International immunology · 2020Article
- Review
- Too much of a good thing: Detrimental effects of interferon.Seminars in immunology · 2019Review
- Nuclear export signal (NES) of transposases affects the transposition activity of mariner-like elementsMobile DNA · 2019Article
- The Methyltransferase-Like Domain of Chikungunya Virus nsP2 Inhibits the Interferon Response by Promoting the Nuclear Export of STAT1.Journal of virology · 2018Article
- The Molecular Basis of Viral Inhibition of IRF- and STAT-Dependent Immune Responses.Frontiers in immunology · 2018Review
- Importins promote high-frequency NF-κB oscillations increasing information channel capacity.Biology direct · 2016Article
- Response to interferons and antibacterial innate immunity in the absence of tyrosine-phosphorylated STAT1.EMBO reports · 2016Article
- A critical role for CRM1 in regulating HOXA gene transcription in CALM-AF10 leukemias.Leukemia · 2015Article
22 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Latent signal transducers and activators of transcription (STATs) reside in the cytoplasm but rapidly accumulate in the nucleus following cytokine stimulation. Nuclear accumulation requires specific tyrosine phosphorylation and STAT dimerization. The presence of STATs in the nucleus is transient, however, and within hours the STATs reappear in the cytoplasm. Results indicate that STAT1 can be dephosphorylated in the nucleus and actively exported by the chromosome region maintenance 1 (CRM1) export receptor. CRM1 recognizes a specific amino acid sequence located within the DNA-binding domain of STAT1. This region shares sequence and functional properties of characterized nuclear export signals. The location of this sequence within STAT1 suggests that it is not accessible to CRM1 when STAT1 is bound to DNA. Evidence is presented to support a model in which STAT1 is tyrosine dephosphorylated in the nucleus and dissociates from DNA, allowing recognition by CRM1 and nuclear export. The regulated export of STAT1 may contribute to silencing of the signal pathway and/or to re-establish STAT1 in the cytoplasm to monitor activity of receptor-kinase signals.
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What OpenQuestion holds
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 OpenQuestion graph.