Evidence map›Paper›PMID 32265297›Full record

ArticleThe Journal of biological chemistry2020

Activation and selectivity of OTUB-1 and OTUB-2 deubiquitinylases.

Dakshinamurthy Sivakumar, Vikash Kumar, Michael Naumann, Matthias Stein

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

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  16. The Activation and Selectivity of theFrontiers in molecular biosciences · 2021
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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

4 authors at 2 institutions in 1 country.

Dakshinamurthy SivakumarMax Planck Institute for Dynamics of Complex Technical Systems, Molecular Simulations and Design Group, 39106 Magdeburg, Germany.ORCID 0000-0003-2130-1155
Vikash KumarMax Planck Institute for Dynamics of Complex Technical Systems, Molecular Simulations and Design Group, 39106 Magdeburg, Germany.
Michael NaumannInstitute of Experimental Internal Medicine, Medical Faculty, Otto von Guericke University, 39120 Magdeburg, Germany.
Matthias SteinMax Planck Institute for Dynamics of Complex Technical Systems, Molecular Simulations and Design Group, 39106 Magdeburg, Germany matthias.stein@mpi-magdeburg.mpg.de.ORCID 0000-0001-7793-0052
Max Planck Institute for Dynamics of Complex Technical Systems · DEOtto-von-Guericke-Universität Magdeburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ovarian tumor domain (OTU) deubiquitinylating cysteine proteases OTUB1 and OTUB2 (OTU ubiquitin aldehyde binding 1 and 2) are representative members of the OTU subfamily of deubiquitinylases. Deubiquitinylation critically regulates a multitude of important cellular processes, such as apoptosis, cell signaling, and growth. Moreover, elevated OTUB expression has been observed in various cancers, including glioma, endometrial cancer, ovarian cancer, and breast cancer. Here, using molecular dynamics simulation approaches, we found that both OTUB1 and OTUB2 display a catalytic triad characteristic of proteases but differ in their configuration and protonation states. The OTUB1 protein had a prearranged catalytic site, with strong electrostatic interactions between the active-site residues His

Indexed as

Molecular Dynamics SimulationCatalytic DomainCysteine EndopeptidasesDeubiquitinating EnzymesEnzyme ActivationHumansHydrogen BondingThiolester HydrolasesCysteine EndopeptidasesDeubiquitinating EnzymesOTUB1 protein, humanOTUB2 protein, humanThiolester Hydrolasesallosteric regulationcatalytic triadcomputational analysiscysteine proteasedeubiquitylation (deubiquitination)molecular dynamicsOTU deubiquitinase ubiquitin aldehyde bindingovarian cancerubiquitin-dependent proteaseubiquitin thioesterase (OTUB1)

Identifiers

PMID32265297
PMCPMC7242701
OpenAlexW3014590847

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.