Evidence map›Paper›PMID 27285106›Full record

ReviewCell death and differentiation2016

Regulation of pluripotency and differentiation by deubiquitinating enzymes.

B Suresh, J Lee, H Kim, S Ramakrishna

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell death and differentiation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing 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

62 citing papers in PubMed, 90 citations in OpenAlex.

  1. Review
  2. Article
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  10. Review
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  14. Article
  15. Posttranslational Modifications ofPharmacological reviews · 2024
    Review
  16. Article
  17. Article
  18. [Ubiquitin-specific protease 42 regulates osteogenic differentiation of human adipose-derived stem cells].Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences · 2024
    Article
  19. Article
  20. Role of UBE2C in Brain Cancer Invasion and Dissemination.International journal of molecular sciences · 2023
    Review

2 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

B SureshDepartment of Pharmacology and Brain Korea 21 PLUS Project for Medical Science, Yonsei University College of Medicine, Seoul, South Korea.
J LeeDepartment of Physiology and Brain Korea 21 PLUS Project for Medical Science, Yonsei University College of Medicine, Seoul, South Korea.
H KimDepartment of Pharmacology and Brain Korea 21 PLUS Project for Medical Science, Yonsei University College of Medicine, Seoul, South Korea.
S RamakrishnaGraduate School of Biomedical Science and Engineering, Department of Biomedical Science, Hanyang University, Seoul, South Korea.
Yonsei University · KRHanyang University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modifications (PTMs) of stemness-related proteins are essential for stem cell maintenance and differentiation. In stem cell self-renewal and differentiation, PTM of stemness-related proteins is tightly regulated because the modified proteins execute various stem cell fate choices. Ubiquitination and deubiquitination, which regulate protein turnover of several stemness-related proteins, must be carefully coordinated to ensure optimal embryonic stem cell maintenance and differentiation. Deubiquitinating enzymes (DUBs), which specifically disassemble ubiquitin chains, are a central component in the ubiquitin-proteasome pathway. These enzymes often control the balance between ubiquitination and deubiquitination. To maintain stemness and achieve efficient differentiation, the ubiquitination and deubiquitination molecular switches must operate in a balanced manner. Here we summarize the current information on DUBs, with a focus on their regulation of stem cell fate determination and deubiquitinase inhibition as a therapeutic strategy. Furthermore, we discuss the possibility of using DUBs with defined stem cell transcription factors to enhance cellular reprogramming efficiency and cell fate conversion. Our review provides new insight into DUB activity by emphasizing their cellular role in regulating stem cell fate. This role paves the way for future research focused on specific DUBs or deubiquitinated substrates as key regulators of pluripotency and stem cell differentiation.

Indexed as

AnimalsCell DifferentiationCell Self RenewalDeubiquitinating EnzymesEmbryonic Stem CellsHumansNeoplasmsTranscription FactorsTumor Suppressor ProteinsUbiquitinUbiquitinationDeubiquitinating EnzymesTranscription FactorsTumor Suppressor ProteinsUbiquitin

Identifiers

PMID27285106
PMCPMC4947674
OpenAlexW2414180960

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.