Evidence map›Paper›PMID 24900367›Full record

ArticleACS medicinal chemistry letters2012

Proposed Bioactive Conformations of Opiorphin, an Endogenous Dual APN/NEP Inhibitor.

Marta Pinto, Catherine Rougeot, Luis Gracia, Mònica Rosa, Andrés García, Gemma Arsequell, Gregorio Valencia, Nuria B Centeno

Open access · greenAbstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.1field-weighted citation impact, top 48% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

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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

8 authors at 4 institutions in 3 countries.

Marta PintoComputer-Assisted Drug Design Laboratory, Research Programme on Biomedical Informatics (GRIB), IMIM-Universitat Pompeu Fabra , Dr. Aiguader 88, E-08003 Barcelona, Spain.
Catherine RougeotInstitut Pasteur-Unité de Biochimie Structurale et Cellulaire/URA2185-CNRS , 25 rue du Docteur Roux, 75724 Paris Cedex 15, France.
Luis GraciaDepartment of Physiology and Biophysics, Weill Cornell Medical College , 1300 York Avenue, New York, New York 10065, United States.
Mònica RosaUnit of Glycoconjugate Chemistry, Instituto de Química Avanzada de Catalunya (IQAC-CSIC) , Jordi Girona 18-26, E-08034 Barcelona, Spain.
Andrés GarcíaComputer-Assisted Drug Design Laboratory, Research Programme on Biomedical Informatics (GRIB), IMIM-Universitat Pompeu Fabra , Dr. Aiguader 88, E-08003 Barcelona, Spain.
Gemma ArsequellUnit of Glycoconjugate Chemistry, Instituto de Química Avanzada de Catalunya (IQAC-CSIC) , Jordi Girona 18-26, E-08034 Barcelona, Spain.
Gregorio ValenciaUnit of Glycoconjugate Chemistry, Instituto de Química Avanzada de Catalunya (IQAC-CSIC) , Jordi Girona 18-26, E-08034 Barcelona, Spain.
Nuria B CentenoComputer-Assisted Drug Design Laboratory, Research Programme on Biomedical Informatics (GRIB), IMIM-Universitat Pompeu Fabra , Dr. Aiguader 88, E-08003 Barcelona, Spain.
Institute of Advanced Chemistry of Catalonia · ESPompeu Fabra University · ESCentre National de la Recherche Scientifique · FRCornell University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conformational profiles for the endogenous peptide Opiorphin and a set of seven analogues exhibiting different inhibitory activities toward human aminopeptidase N (hAPN) and human neprilysin (hNEP) were independently computed to deduce a bioactive conformation that Opiorphin may adopt when binding these two enzymes. The conformational space was thoroughly sampled using an iterative simulated annealing protocol, and a library of low-energy conformers was generated for each peptide. Bioactive Opiorphin conformations fitting our experimental structure-activity relationship data were identified for hAPN and hNEP using computational pairwise comparisons between each of the unique low-energy conformations of Opiorphin and its analogues. The obtained results provide a structural explanation for the dual hAPN and hNEP inhibitory activity of Opiorphin and show that the inborn flexibility of Opiorphin is essential for its analgesic activity.

Indexed as

bioactive conformationconformational analysisOpiorphin

Identifiers

PMID24900367
PMCPMC4025773
OpenAlexW1976963232

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.