Evidence map›Paper›PMID 27844253›Full record

ReviewCancer metastasis reviews2016

The role of deubiquitinases in breast cancer.

Zhenna Xiao, Peijing Zhang, Li Ma

Open access · greenAbstract readReview
In one paragraph

Review in Cancer metastasis reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Monoubiquitination in Homeostasis and Cancer.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Deubiquitinase Activity Profiling Identifies UCHL1 as a Candidate Oncoprotein That Promotes TGFβ-Induced Breast Cancer Metastasis.Clinical cancer research : an official journal of the American Association for Cancer Research · 2020
    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 2 institutions in 1 country.

Zhenna XiaoDepartment of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX, 77030, USA.
Peijing ZhangDepartment of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX, 77030, USA.
Li MaDepartment of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX, 77030, USA. lma4@mdanderson.org.
The University of Texas MD Anderson Cancer Center · USThe University of Texas Health Science Center at Houston · US

Funding

Regulation of metastasis and epithelial-mesenchymal transition by microRNAsR01CA166051 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI MA, LI · 2012 to 2023
$3.4M
Epithelial-mesenchymal transition regulators in radioresistance and DNA repairR01CA181029 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI MA, LI · 2014 to 2018
$1.7M
NCI NIH HHS R01 CA166051NCI NIH HHS R01 CA181029
6 · The paper itself

Abstract

Although growing numbers of oncoproteins and pro-metastatic proteins have been extensively characterized, many of these tumor-promoting proteins are not good drug targets, which represent a major barrier to curing breast cancer and other cancers. There is a need, therefore, for alternative therapeutic approaches to destroying cancer-promoting proteins. The human genome encodes approximately 100 deubiquitinating enzymes (DUBs, also called deubiquitinases), which are amenable to pharmacologic inhibition by small molecules. By removing monoubiquitin or polyubiquitin chains from the target protein, DUBs can modulate the degradation, localization, activity, trafficking, and recycling of the substrate, thereby contributing substantially to the regulation of cancer proteins and pathways. Targeting certain DUBs may lead to destabilization or functional inactivation of some key oncoproteins or pro-metastatic proteins, including non-druggable ones, which will provide therapeutic benefits to cancer patients. In breast cancer, growing numbers of DUBs are found to be aberrantly expressed. Depending on their substrates, specific DUBs can either promote or suppress mammary tumors. In this article, we review the role and mechanisms of action of DUBs in breast cancer and discuss the potential of targeting DUBs for cancer treatment.

Indexed as

AnimalsBreast NeoplasmsDeubiquitinating EnzymesFemaleHumansUbiquitinationDeubiquitinating EnzymesBreast cancerDeubiquitinaseDUB inhibitorUbiquitination

Identifiers

PMID27844253
PMCPMC5215973
OpenAlexW2552591484

What OpenQuestion holds

Textmetadata
LicenceTDM
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.