Evidence map›Paper›PMID 22937016›Full record

ArticlePloS one2012

Systematic analysis of the physiological importance of deubiquitinating enzymes.

Wei-Ling Tsou, Michael J Sheedlo, Marie E Morrow, Jessica R Blount, Kelly M McGregor, Chittaranjan Das, Sokol V Todi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Expression and Role of Ubiquitin-Specific Peptidases in Osteoblasts.International journal of molecular sciences · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Unanchored Ubiquitin Chains, Revisited.Frontiers in cell and developmental biology · 2020
    Review
  11. Article
  12. Article
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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

7 authors at 3 institutions in 1 country.

Wei-Ling TsouDepartment of Pharmacology, Wayne State University School of Medicine, Detroit, Michigan, United States of America.
Michael J Sheedlo
Marie E Morrow
Jessica R Blount
Kelly M McGregor
Chittaranjan Das
Sokol V Todi
Michigan United · USPurdue University West Lafayette · USWayne State University · US

Funding

Nonlinear Optical Imaging for Guiding Protein Structure DeterminationR01RR026273 · NCRR · PURDUE UNIVERSITY · PI SIMPSON, GARTH JASON · 2010 to 2011
$745k
Posttranslational Modification of Deubiquitinating Enzymes in NeurodegenerationR00NS064097 · NINDS · WAYNE STATE UNIVERSITY · PI TODI, SOKOL · 2011 to 2013
$724k
NCRR NIH HHS 1R01RR026273NCRR NIH HHS R01 RR026273NINDS NIH HHS R00 NS064097NINDS NIH HHS R00NS064097
6 · The paper itself

Abstract

Deubiquitinating enzymes (DUBs) are proteases that control the post-translational modification of proteins by ubiquitin and in turn regulate diverse cellular pathways. Despite a growing understanding of DUB biology at the structural and molecular level, little is known about the physiological importance of most DUBs. Here, we systematically identify DUBs encoded by the genome of Drosophila melanogaster and examine their physiological importance in vivo. Through domain analyses we uncovered 41 Drosophila DUBs, most of which have human orthologues. Systematic knockdown of the vast majority of DUBs throughout the fly or in specific cell types had dramatic consequences for Drosophila development, adult motility or longevity. Specific DUB subclasses proved to be particularly necessary during development, while others were important in adults. Several DUBs were indispensable in neurons or glial cells during developmental stages; knockdown of others perturbed the homeostasis of ubiquitinated proteins in adult flies, or had adverse effects on wing positioning as a result of neuronal requirements. We demonstrate the physiological significance of the DUB family of enzymes in intact animals, find that there is little functional redundancy among members of this family of proteases, and provide insight for future investigations to understand DUB biology at the molecular, cellular and organismal levels.

Indexed as

AnimalsDrosophila melanogasterDrosophila ProteinsEndopeptidasesHumansUbiquitinUbiquitinationDrosophila ProteinsEndopeptidasesUbiquitin

Identifiers

PMID22937016
PMCPMC3427330
OpenAlexW1998684648

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.