Evidence map›Paper›PMID 30282802›Full record

ArticleThe Journal of biological chemistry2018

OTUB1 non-catalytically stabilizes the E2 ubiquitin-conjugating enzyme UBE2E1 by preventing its autoubiquitination.

Nagesh Pasupala, Marie E Morrow, Lauren T Que, Barbara A Malynn, Averil Ma, Cynthia Wolberger

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

28 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. OTU deubiquitinases in disease: roles and targeting.Trends in molecular medicine · 2026
    Review
  4. Article
  5. Review
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  12. Review
  13. Article
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  15. Article
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  17. Article
  18. The Deubiquitinase OTUB1 Is a Key Regulator of Energy Metabolism.International journal of molecular sciences · 2022
    Article
  19. Article
  20. Review
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

6 authors at 2 institutions in 1 country.

Nagesh PasupalaFrom the Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205-2185 and.
Marie E MorrowFrom the Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205-2185 and.
Lauren T QueFrom the Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205-2185 and.
Barbara A Malynnthe Department of Medicine, University of California San Francisco, San Francisco, California 94117.
Averil Mathe Department of Medicine, University of California San Francisco, San Francisco, California 94117.
Cynthia WolbergerFrom the Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205-2185 and. Electronic address: cwolberg@jhmi.edu.
Johns Hopkins University · USUniversity of California, San Francisco · US

Funding

REGULATION OF UBIQUITINATION BY DUB-E2 UBIQUITIN CONJUGATING ENZYME COMPLEXESR01GM109102 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WOLBERGER, CYNTHIA · 2014 to 2017
$1.9M
NIGMS NIH HHS R01 GM109102
6 · The paper itself

Abstract

OTUB1 is a deubiquitinating enzyme that cleaves Lys-48-linked polyubiquitin chains and also regulates ubiquitin signaling through a unique, noncatalytic mechanism. OTUB1 binds to a subset of E2 ubiquitin-conjugating enzymes and inhibits their activity by trapping the E2∼ubiquitin thioester and preventing ubiquitin transfer. The same set of E2s stimulate the deubiquitinating activity of OTUB1 when the E2 is not charged with ubiquitin. Previous studies have shown that, in cells, OTUB1 binds to E2-conjugating enzymes of the UBE2D (UBCH5) and UBE2E families, as well as to UBE2N (UBC13). Cellular roles have been identified for the interaction of OTUB1 with UBE2N and members of the UBE2D family, but not for interactions with UBE2E E2 enzymes. We report here a novel role for OTUB1-E2 interactions in modulating E2 protein ubiquitination. We observe that

Indexed as

Amino Acid MotifsAnimalsCysteine EndopeptidasesDeubiquitinating EnzymesMiceMice, Inbred C57BLProtein BindingProtein StabilityUbiquitinUbiquitinationUbiquitin-Conjugating EnzymesCysteine EndopeptidasesDeubiquitinating EnzymesOTUB1 protein, humanOtub1 protein, mouseUBE2E1 protein, humanUbe2e1 protein, mouseUbiquitinUbiquitin-Conjugating Enzymesdeubiquitylation (deubiquitination)histoneUBE2E1ubiquitinubiquitin-conjugating enzyme (E2 enzyme)ubiquitin thioesterase (OTUB1)

Identifiers

PMID30282802
PMCPMC6254341
OpenAlexW2894596463

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.