Evidence map›Paper›PMID 8622927›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

DUB-1, a deubiquitinating enzyme with growth-suppressing activity.

Y Zhu, M Carroll, F R Papa, M Hochstrasser, A D D'Andrea

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 168 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Multiple functions of USP18.Cell death & disease · 2016
    Review
  5. Decision for cell fate: deubiquitinating enzymes in cell cycle checkpoint.Cellular and molecular life sciences : CMLS · 2016
    Review
  6. Article
  7. Article
  8. Article
  9. The role of deubiquitinating enzymes in apoptosis.Cellular and molecular life sciences : CMLS · 2011
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Inhibitor of kappaB kinase is required to activate a subset of interferon gamma-stimulated genes.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  17. Activity-based ubiquitin-specific protease (USP) profiling of virus-infected and malignant human cells.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  18. Article
  19. Article
  20. Antagonistic regulation of myogenesis by two deubiquitinating enzymes, UBP45 and UBP69.Proceedings of the National Academy of Sciences of the United States of America · 2002
    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 2 institutions in 1 country.

Y ZhuDivision of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.
M Carroll
F R Papa
M Hochstrasser
A D D'Andrea
Dana-Farber Cancer Institute · USHarvard University · US

Funding

STRUCTURE AND FUNCTION OF THE ERYTHROPOIETIN RECEPTORR01DK043889 · NIDDK · DANA-FARBER CANCER INSTITUTE · PI D'ANDREA, ALAN D. · 1992 to 2014
$5.3M
Degradation of Short Lived Regulatory Protein in YeastR37GM046904 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 2009 to 2018
$3.6M
DEGRADTION OF SHORT-LIVED REGULATORY PROTEINS IN YEASTR01GM046904 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 1992 to 2020
$3.6M
NIDDK NIH HHS R01 DK43889-01NIGMS NIH HHS GM46904
6 · The paper itself

Abstract

Cytokines regulate cell growth by inducing the expression of specific target genes. Using the differential display method, we have cloned a cytokine-inducible immediate early gene, DUB-1 (for deubiquitinating enzyme). DUB-1 is related to members of the UBP superfamily of deubiquitinating enzymes, which includes the oncoprotein Tre-2. A glutathione S-transferase-DUB-1 fusion protein cleaved ubiquitin from a ubiquitin-beta-galactosidase protein. When a conserved cysteine residue of DUB-1, required for ubiquitin-specific thiol protease activity, was mutated to serine (C60S), deubiquitinating activity was abolished. Continuous expression of DUB-1 from a steroid-inducible promoter induced growth arrest in the G1 phase of the cell cycle. Cells arrested by DUB-1 expression remained viable and resumed proliferation upon steroid withdrawal. Our results suggest that DUB-1 regulates cellular growth by modulating either the ubiquitin-dependent proteolysis or the ubiquitination state of an unknown growth regulatory factor(s).

Indexed as

EndopeptidasesAmino Acid SequenceAnimalsBase SequenceCell CycleCell LineCloning, MolecularDNA, ComplementaryDNA PrimersGenes, Immediate-EarlyGrowth InhibitorsHematopoiesisImmediate-Early ProteinsInterleukin-3MiceMolecular Sequence DataDNA, ComplementaryDNA PrimersDub1 protein, mouseEndopeptidasesGrowth InhibitorsImmediate-Early ProteinsInterleukin-3RNA, MessengerUbiquitins

Identifiers

PMID8622927
PMCPMC39596
OpenAlexW2003209070

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.