Evidence map›Paper›PMID 19489724›Full record

ReviewAnnual review of biochemistry2009

Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.

Francisca E Reyes-Turcu, Karen H Ventii, Keith D Wilkinson

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 809 papers.

0numbers the graph read from it
0cells of the map it votes in
809citing papers in PubMed
36.6field-weighted citation impact, top 1% 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

809 citing papers in PubMed, 1,403 citations in OpenAlex.

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  7. bioRxiv : the preprint server for biology · 2026
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749 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

3 authors at 2 institutions in 1 country.

Francisca E Reyes-TurcuLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Karen H Ventii
Keith D Wilkinson
Emory University · USNational Institutes of Health · US

Funding

UBIQUITIN-DEPENDENT PROTEOLYSIS--SPECIFICITY/MECHANISMR01GM030308 · NIGMS · EMORY UNIVERSITY · PI WILKINSON, KEITH D · 1985 to 2010
$3.9M
NIGMS NIH HHS R01 GM030308
6 · The paper itself

Abstract

Deubiquitinating enzymes (DUBs) are proteases that process ubiquitin or ubiquitin-like gene products, reverse the modification of proteins by a single ubiquitin(-like) protein, and remodel polyubiquitin(-like) chains on target proteins. The human genome encodes nearly 100 DUBs with specificity for ubiquitin in five gene families. Most DUB activity is cryptic, and conformational rearrangements often occur during the binding of ubiquitin and/or scaffold proteins. DUBs with specificity for ubiquitin contain insertions and extensions modulating DUB substrate specificity, protein-protein interactions, and cellular localization. Binding partners and multiprotein complexes with which DUBs associate modulate DUB activity and substrate specificity. Quantitative studies of activity and protein-protein interactions, together with genetic studies and the advent of RNAi, have led to new insights into the function of yeast and human DUBs. This review discusses ubiquitin-specific DUBs, some of the generalizations emerging from recent studies of the regulation of DUB activity, and their roles in various cellular processes.

Indexed as

AnimalsEndopeptidasesHumansProtein Structure, TertiaryUbiquitinUbiquitinationEndopeptidasesUbiquitin

Identifiers

PMID19489724
PMCPMC2734102
OpenAlexW2139364069

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.