Evidence map›Paper›PMID 32079362›Full record

ArticleBiomolecules2020

The Relevance of Thimet Oligopeptidase in the Regulation of Energy Metabolism and Diet-Induced Obesity.

Mayara C F Gewehr, Alexandre A S Teixeira, Bruna A C Santos, Luana A Biondo, Fábio C Gozzo, Amanda M Cordibello, Rosangela A S Eichler, Patrícia Reckziegel, Renée N.O. Da Silva, Nilton B Dos Santos and 13 more

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Neurolysin Knockout Mice in a Diet-Induced Obesity Model.International journal of molecular sciences · 2023
    Article
  3. Article
  4. Article
  5. Probing the Conformational States of Thimet Oligopeptidase in Solution.International journal of molecular sciences · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. 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

23 authors at 4 institutions in 1 country.

Mayara C F GewehrDepartment of Pharmacology, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Alexandre A S TeixeiraDepartment of Cell Biology and Development, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Bruna A C SantosDepartment of Pharmacology, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Luana A BiondoDepartment of Cell Biology and Development, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Fábio C GozzoInstitute of Chemistry, State University of Campinas, 13083-862 Campinas, SP, Brazil.
Amanda M CordibelloInstitute of Chemistry, State University of Campinas, 13083-862 Campinas, SP, Brazil.
Rosangela A S EichlerDepartment of Pharmacology, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Patrícia ReckziegelDepartment of Pharmacology, Federal University of São Paulo, 04023-062 São Paulo, SP, Brazil.
Renée N.O. Da SilvaDepartment of Pharmacology, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Nilton B Dos SantosDepartment of Pharmacology, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Niels O S CamaraDepartment of Immunology, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Angela CastoldiDepartment of Immunology, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Maria L M Barreto-ChavesDepartment of Anatomy, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Camila S DaleDepartment of Anatomy, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Nathalia SengerDepartment of Anatomy, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Joanna D C C LimaDepartment of Cell Biology and Development, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Marilia C L SeelaenderDepartment of Cell Biology and Development, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Aline C InadaDepartment of Pharmacology, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Eliana H AkamineDepartment of Pharmacology, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Leandro M CastroBiosciences Institute, São Paulo State University, 11330-900 São Vicente, SP, Brazil.
Alice C RodriguesDepartment of Pharmacology, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
José C Rosa NetoDepartment of Cell Biology and Development, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Emer S FerroDepartment of Pharmacology, Biomedical Sciences Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil.
Universidade de São Paulo · BRUniversidade Estadual de Campinas (UNICAMP) · BRUniversidade Estadual Paulista (Unesp) · BRUniversidade Federal de São Paulo · BR

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 445363/2014-2; 400944/2014-6; 400944/2014-6; 302809/2016-3Fundação de Amparo à Pesquisa do Estado de São Paulo 2016/04000-3; 2004/04933-2; 2015/20657-0
6 · The paper itself

Abstract

Thimet oligopeptidase (EC 3.4.24.15; EP24.15; THOP1) is a potential therapeutic target, as it plays key biological functions in processing biologically functional peptides. The structural conformation of THOP1 provides a unique restriction regarding substrate size, in that it only hydrolyzes peptides (optimally, those ranging from eight to 12 amino acids) and not proteins. The proteasome activity of hydrolyzing proteins releases a large number of intracellular peptides, providing THOP1 substrates within cells. The present study aimed to investigate the possible function of THOP1 in the development of diet-induced obesity (DIO) and insulin resistance by utilizing a murine model of hyperlipidic DIO with both C57BL6 wild-type (WT) and THOP1 null (THOP1

Indexed as

Energy MetabolismAdipogenesisAdipose TissueAnimalsDiet, High-FatFemaleGene DeletionInsulin ResistanceLipolysisMaleMetalloendopeptidasesMiceMice, Inbred C57BLObesityMetalloendopeptidasesthimet oligopeptidasediet-induced obesityinsulin resistancemass spectrometryobesitypeptidasespeptidomeproteasesproteasome

Identifiers

PMID32079362
PMCPMC7072564
OpenAlexW3006269376

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.