Evidence map›Paper›PMID 30314342›Full record

ArticleMolecules (Basel, Switzerland)2018

Aminobenzosuberone Scaffold as a Modular Chemical Tool for the Inhibition of Therapeutically Relevant M1 Aminopeptidases.

Emmanuel Salomon, Marjorie Schmitt, Anil Kumar Marapaka, Athanasios Stamogiannos, Germain Revelant, Céline Schmitt, Sarah Alavi, Isabelle Florent, Anthony Addlagatta, Efstratios Stratikos and 2 more

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.5field-weighted citation impact, top 31% 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

7 citing papers in PubMed, 18 citations in OpenAlex.

  1. Trial
  2. Review
  3. Review
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  7. 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

12 authors at 3 institutions in 3 countries.

Emmanuel SalomonLaboratoire d'Innovation Moléculaire et Applications, Université de Haute-Alsace, Université de Strasbourg, CNRS, 68093 Mulhouse, France. emmanuel.salomon@uha.fr.
Marjorie SchmittLaboratoire d'Innovation Moléculaire et Applications, Université de Haute-Alsace, Université de Strasbourg, CNRS, 68093 Mulhouse, France. marjorie.schmitt@uha.fr.
Anil Kumar MarapakaCentre for Chemical Biology, CSIR-Indian Institute of Chemical Technology, Hyderabad 500007, Telangana, India. anilmarapaka@gmail.com.ORCID 0000-0001-8872-0552
Athanasios StamogiannosProtein Chemistry Laboratory, INRASTES, National Centre for Scientific Research Demokritos, Agia Paraskevi, 15310 Athens, Greece. a.stamogiannos@gmail.com.
Germain RevelantLaboratoire d'Innovation Moléculaire et Applications, Université de Haute-Alsace, Université de Strasbourg, CNRS, 68093 Mulhouse, France. germain.revelant@hotmail.fr.
Céline SchmittLaboratoire d'Innovation Moléculaire et Applications, Université de Haute-Alsace, Université de Strasbourg, CNRS, 68093 Mulhouse, France. celine.schmitt85@gmail.com.
Sarah AlaviLaboratoire d'Innovation Moléculaire et Applications, Université de Haute-Alsace, Université de Strasbourg, CNRS, 68093 Mulhouse, France. SALAVI@esta-groupe.fr.
Isabelle FlorentMolécules de Communication et Adaptation des Micro-organismes, Muséum National d'Histoire Naturelle, CNRS, 75231 Paris, France. isabelle.florent@mnhn.fr.
Anthony AddlagattaCentre for Chemical Biology, CSIR-Indian Institute of Chemical Technology, Hyderabad 500007, Telangana, India. anthonyaddlagatta@gmail.com.
Efstratios StratikosProtein Chemistry Laboratory, INRASTES, National Centre for Scientific Research Demokritos, Agia Paraskevi, 15310 Athens, Greece. stratikos@gmail.com.ORCID 0000-0002-3566-2309
Céline TarnusLaboratoire d'Innovation Moléculaire et Applications, Université de Haute-Alsace, Université de Strasbourg, CNRS, 68093 Mulhouse, France. celine.tarnus@uha.fr.
Sébastien AlbrechtLaboratoire d'Innovation Moléculaire et Applications, Université de Haute-Alsace, Université de Strasbourg, CNRS, 68093 Mulhouse, France. sebastien.albrecht@uha.fr.ORCID 0000-0002-1016-0193
Centre National de la Recherche Scientifique · FRIndian Institute of Chemical Technology · INNational Centre of Scientific Research "Demokritos" · GR

Funding

Agence Nationale de la Recherche ANR-12-BS07-0020-01Department of Science and Technology, New Delhi, India EMR/2015/000461
6 · The paper itself

Abstract

The synthesis of racemic substituted 7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-one hydrochlorides was optimized to enhance reproducibility and increase the overall yield. In order to investigate their specificity, series of enzyme inhibition assays were carried out against a diversity of proteases, covering representative members of aspartic, cysteine, metallo and serine endopeptidases and including eight members of the monometallic M1 family of aminopeptidases as well as two members of the bimetallic M17 and M28 aminopeptidase families. This aminobenzosuberone scaffold indeed demonstrated selective inhibition of M1 aminopeptidases to the exclusion of other tested protease families; it was particularly potent against mammalian APN and its bacterial/parasitic orthologues

Indexed as

AminopeptidasesAnimalsCoumarinsEnzyme ActivationMolecular ConformationMolecular Docking SimulationMolecular Dynamics SimulationMolecular StructureProtease InhibitorsProtein BindingStructure-Activity RelationshipSubstrate SpecificityAminopeptidasesbenzosuberoneCoumarinsProtease Inhibitorsaminobenzosuberone scaffoldM1 aminopeptidasesselective inhibitors

Identifiers

PMID30314342
PMCPMC6222927
OpenAlexW2897996011

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.