Evidence map›Paper›PMID 8756652›Full record

ArticleMolecular and cellular biology1996

Enhancement of antiproliferative activity of gamma interferon by the specific inhibition of tyrosine dephosphorylation of Stat1.

K Shuai, J Liao, M M Song

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

45 citing papers in PubMed, 151 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Inflammaging: Age and Systemic, Cellular, and Nuclear Inflammatory Biology in Older Adults.The journals of gerontology. Series A, Biological sciences and medical sciences · 2019
    Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Protein tyrosine phosphatases in the JAK/STAT pathway.Frontiers in bioscience : a journal and virtual library · 2008
    Review
  18. Article
  19. Article
  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

3 authors at 1 institution in 1 country.

K ShuaiDepartment of Medicine, Molecular Biology Institute, University of California--Los Angeles, 90095-1678, USA.
J Liao
M M Song
University of California, Los Angeles · US

Funding

NIAID NIH HHS AI07126-19
6 · The paper itself

Abstract

Gamma interferon (IFN-gamma) signals to the nucleus through the activation, by tyrosine phosphorylation, of the latent cytoplasmic transcription factor Stat1 (signal transducer and activator of transcription). It has been demonstrated that the activity of Stat1 is dependent on tyrosine phosphorylation which is regulated by Jak tyrosine kinases as well as by the as-yet-unidentified protein tyrosine phosphatase. We report that the N-terminal domain of Stat1, which is highly conserved among all STAT family members, is required for its tyrosine dephosphorylation. A single amino acid substitution (Arg-31 to Ala) in the Stat1 N-terminal domain inhibited Stat1 tyrosine dephosphorylation. The deletion of the Stat1 N-terminal domain resulted in a mutant Stat1 protein which was constitutively phosphorylated on Tyr-701. Upon IFN-gamma stimulation, the tyrosine phosphorylation of this mutant protein was further enhanced but was not down-regulated by protein tyrosine phosphatase in vivo. When expressed in NIH 3T3 cells, this mutant protein greatly enhanced the antiproliferative activity of IFN-gamma. We suggest that the N-terminal domains of STATs are crucial for modulating STAT activities through regulating the tyrosine dephosphorylation of STATs.

Indexed as

3T3 CellsAmino Acid SequenceAnimalsCell DivisionDNA-Binding ProteinsHumansInterferon-gammaMiceMolecular Sequence DataPhosphorylationPhosphotyrosineProtein Processing, Post-TranslationalProtein Tyrosine PhosphatasesRecombinant Fusion ProteinsSequence AlignmentSequence DeletionDNA-Binding ProteinsInterferon-gammaPhosphotyrosineProtein Tyrosine PhosphatasesRecombinant Fusion ProteinsSTAT1 protein, humanStat1 protein, mouseSTAT1 Transcription FactorTrans-Activators

Identifiers

PMID8756652
PMCPMC231495
OpenAlexW2103807332

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.