Evidence map›Paper›PMID 25924794›Full record

ArticleParasitology research2015

MJD and OTU deubiquitinating enzymes in Schistosoma mansoni.

Roberta Verciano Pereira, Matheus de Souza Gomes, Marcela Pereira Costa, Liana Konovaloff Jannotti Passos, William de Castro Borges, Renata Guerra-Sá

Abstract read
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In one paragraph

Article in Parasitology research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. The emerging role of Deubiquitinases (DUBs) in parasites: A foresight review.Frontiers in cellular and infection microbiology · 2022
    Review
  2. Article
  3. Revealing a Novel Otubain-Like Enzyme fromFrontiers in chemistry · 2017
    Article
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 3 institutions in 1 country.

Roberta Verciano PereiraNúcleo de Pesquisas em Ciências Biológicas, Universidade Federal de Ouro Preto, Ouro Preto, MG, Brazil.
Matheus de Souza Gomes
Marcela Pereira Costa
Liana Konovaloff Jannotti Passos
William de Castro Borges
Renata Guerra-Sá
Universidade Federal de Ouro Preto · BRFundação Oswaldo Cruz · BRUniversidade Federal de Uberlândia · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitination and deubiquitination of proteins can alter diverse cellular processes, such as proteolysis, trafficking, subcellular localisation, DNA repair, apoptosis and signal transduction. Deubiquitinating enzymes (DUBs) are responsible for removing ubiquitin from their target proteins. Previous reports have shown the presence of two subfamilies of DUBs in Schistosoma mansoni: Ub carboxyl-terminal hydrolase (UCH) and Ub-specific protease (USP). In this study, we analysed the ovarian tumour (OTU) and Machado-Joseph disease protein domain (MJD) proteases found in the Schistosoma mansoni genome database. An in silico analysis identified two different MJD subfamily members, SmAtaxin-3 and SmJosephin, and five distinct OTU proteases, SmOTU1, SmOTU3, SmOTU5a, SmOTU6b and SmOtubain. The phylogenetic analysis showed the evolutionary conservation of these proteins. Furthermore, the 3D structures confirmed the similarity of these proteins with human proteins. In addition, we performed quantitative reverse transcription-polymerase chain reaction (qRT-PCR) and observed distinct expression profiles for all of the investigated transcripts between the cercariae, schistosomula and adult worm stages. Taken together, our data suggest that MJD and OTU subfamily members contribute to regulating the activity of the Ub-proteasome system during the life cycle of this parasite.

Indexed as

Gene Expression Regulation, EnzymologicProtein Processing, Post-TranslationalAnimalsCercariaEndopeptidasesFemaleHelminth ProteinsHumansLife Cycle StagesPhylogenyProteasome Endopeptidase ComplexSchistosoma mansoniUbiquitinationEndopeptidasesHelminth ProteinsProteasome Endopeptidase Complex

Identifiers

PMID25924794
OpenAlexW2094941696

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.