Evidence map›Paper›PMID 35806299›Full record

ArticleInternational journal of molecular sciences2022

Probing the Conformational States of Thimet Oligopeptidase in Solution.

Marcelo F M Marcondes, Gabriel S Santos, Fellipe Bronze, Mauricio F M Machado, Kátia R Perez, Renske Hesselink, Marcel P de Vries, Jaap Broos, Vitor Oliveira

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 88% 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

1 citing paper in PubMed, 0 citations in OpenAlex.

  1. 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

9 authors at 2 institutions in 2 countries.

Marcelo F M MarcondesDepartment of Biophysics, Universidade Federal de São Paulo, Rua Pedro de Toledo, 669, 7º Floor, São Paulo 04039-032, Brazil.
Gabriel S SantosDepartment of Biophysics, Universidade Federal de São Paulo, Rua Pedro de Toledo, 669, 7º Floor, São Paulo 04039-032, Brazil.ORCID 0000-0002-9069-2690
Fellipe BronzeDepartment of Biophysics, Universidade Federal de São Paulo, Rua Pedro de Toledo, 669, 7º Floor, São Paulo 04039-032, Brazil.
Mauricio F M MachadoDepartment of Biophysics, Universidade Federal de São Paulo, Rua Pedro de Toledo, 669, 7º Floor, São Paulo 04039-032, Brazil.ORCID 0000-0003-0313-0866
Kátia R PerezDepartment of Biophysics, Universidade Federal de São Paulo, Rua Pedro de Toledo, 669, 7º Floor, São Paulo 04039-032, Brazil.
Renske HesselinkDepartment of Molecular Genetics, Groningen Biomolecular Science and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
Marcel P de VriesInterfaculty Mass Spectrometry Center, University of Groningen, A. Deusinglaan 1, 9713 AV Groningen, The Netherlands.
Jaap BroosDepartment of Molecular Genetics, Groningen Biomolecular Science and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
Vitor OliveiraDepartment of Biophysics, Universidade Federal de São Paulo, Rua Pedro de Toledo, 669, 7º Floor, São Paulo 04039-032, Brazil.ORCID 0000-0002-4662-1377
Universidade Federal de São Paulo · BRUniversity of Groningen · NL

Funding

Coordenação de Aperfeicoamento de Pessoal de Nível Superior nuffic 011/09São Paulo Research Foundation 2011/20941-9São Paulo Research Foundation 2011/51989-7São Paulo Research Foundation 2014/00661-0São Paulo Research Foundation 2014/20847-0São Paulo Research Foundation 2018/09158-0São Paulo Research Foundation 2020/09678-3
6 · The paper itself

Abstract

Thimet oligopeptidase (TOP) is a metallopeptidase involved in the metabolism of oligopeptides inside and outside cells of various tissues. It has been proposed that substrate or inhibitor binding in the TOP active site induces a large hinge-bending movement leading to a closed structure, in which the bound ligand is enclosed. The main goal of the present work was to study this conformational change, and fluorescence techniques were used. Four active TOP mutants were created, each equipped with a single-Trp residue (fluorescence donor) and a

Indexed as

MetalloendopeptidasesOligopeptidesCatalytic DomainLigandsSubstrate SpecificityLigandsMetalloendopeptidasesOligopeptidesthimet oligopeptidaseenzyme kineticsmetallopeptidasenon-canonical amino acidpeptidase family M3zinc-dependent peptidase

Identifiers

PMID35806299
PMCPMC9266445
OpenAlexW4283738239

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.