Evidence map›Paper›PMID 28659380›Full record

ReviewOpen biology2017

Deubiquitylation of deubiquitylases.

Saba Haq, Suresh Ramakrishna

Abstract readReview
In one paragraph

Review in Open biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

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  18. Regulating tumor suppressor genes: post-translational modifications.Signal transduction and targeted therapy · 2020
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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

2 authors.

Saba HaqDepartment of Life Science, College of Natural Sciences, Hanyang University, Seoul, South Korea.
Suresh RamakrishnaGraduate School of Biomedical Science and Engineering, Hanyang University, Seoul, South Korea suri28@hanyang.ac.kr suresh.ramakris@gmail.com.ORCID 0000-0002-4038-1085

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deubiquitylating enzymes (DUBs) reverse the ubiquitylation of target proteins, thereby regulating diverse cellular functions. In contrast to the plethora of research being conducted on the ability of DUBs to counter the degradation of cellular proteins or auto-ubiquitylated E3 ligases, very little is known about the mechanisms of DUB regulation. In this review paper, we summarize a novel possible mechanism of DUB deubiquitylation by other DUBs. The available data suggest the need for further experiments to validate and characterize this notion of 'Dubbing DUBs'. The current studies indicate that the idea of deubiquitylation of DUBs by other DUBs is still in its infancy. Nevertheless, future research holds the promise of validation of this concept.

Indexed as

UbiquitinationDeubiquitinating EnzymesDeubiquitinating Enzymesauto-regulationdeubiquitylating DUBsproteasome degradationself-deubiquitylationubiquitylation

Identifiers

PMID28659380
PMCPMC5493773

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.