Evidence map›Paper›PMID 20549504›Full record

ArticleMammalian genome : official journal of the International Mammalian Genome Society2010

USP32 is an active, membrane-bound ubiquitin protease overexpressed in breast cancers.

Shiva Akhavantabasi, Hesna B Akman, Aysegul Sapmaz, Jennifer Keller, Elizabeth M Petty, Ayse E Erson

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Mammalian genome : official journal of the International Mammalian Genome Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

37 citing papers in PubMed, 70 citations in OpenAlex.

  1. Deubiquitination of Vangl by USP6 and USP32 Regulates Planar Cell Polarity Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Regulation of Deubiquitinating Enzymes by Post-Translational Modifications.International journal of molecular sciences · 2020
    Review
  18. Review
  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

6 authors at 2 institutions in 2 countries.

Shiva AkhavantabasiDepartment of Biological Sciences, Inonu Bulvari, M.E.T.U, Ankara, Turkey.
Hesna B Akman
Aysegul Sapmaz
Jennifer Keller
Elizabeth M Petty
Ayse E Erson
Inonu University · TRRegional West Medical Center · US

Funding

The role of SEPT9 in cell proliferation and oncogenesisR01CA072877 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PETTY, ELIZABETH M. · 1997 to 2010
$2.4M
NCI NIH HHS R01 CA72877-01A1
6 · The paper itself

Abstract

USP32, on chromosomal band 17q23.1-17q23.2, is a highly conserved but uncharacterized gene that gave rise during evolution to a well-known hominoid-specific proto-oncogene, USP6. We investigated the expression profile of USP32 in human tissues and examined its functions to gain insight into this novel member of the well-conserved ubiquitination system. We detected ubiquitous USP32 expression across tissues and confirmed the predicted deubiquitination function owing to the presence of conserved peptidase signature aspargine, cysteine, histidine, and aspartic acid domains of ubiquitin-specific proteases. A Golgi localization of GFP-fused USP32 was detected by fluorescent protection assay and BODIPY-TR staining. In addition, stable silencing of USP32 caused a significant decrease in the proliferation and migration rate of cells. Based on these and the fact that USP32 maps to 17q23, which is commonly amplified in breast cancers, we analyzed USP32 expression in breast cancer cells. We detected high expression of USP32 in 50% (9 of 18) of breast cancer cell lines and 22% (9 of 41) of primary breast tumors compared to mammary epithelial cells. In summary, we report the preliminary characterization of this novel deubiquitinating enzyme on 17q23 and demonstrate its functional role in the ubiquitin system and its potential involvement in tumorigenesis.

Indexed as

Amino Acid SequenceBreast NeoplasmsCarcinomaCell Line, TumorCell MembraneEndopeptidasesEnzyme ActivationFemaleGene Expression Regulation, NeoplasticHeLa CellsHumansMolecular Sequence DataProto-Oncogene MasSequence Homology, Amino AcidUbiquitin-Specific ProteasesUbiquitin ThiolesteraseEndopeptidasesMAS1 protein, humanProto-Oncogene MasUbiquitin-Specific ProteasesUbiquitin ThiolesteraseUSP10 protein, human

Identifiers

PMID20549504
OpenAlexW2010315416

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.