Evidence map›Paper›PMID 28373864›Full record

ArticleFrontiers in microbiology2017

Chelation Motifs Affecting Metal-dependent Viral Enzymes:

Mauro Carcelli, Dominga Rogolino, Anna Gatti, Nicolino Pala, Angela Corona, Alessia Caredda, Enzo Tramontano, Christophe Pannecouque, Lieve Naesens, Francesca Esposito

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

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  4. Inhibition ofIUCrJ · 2022
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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

10 authors at 5 institutions in 2 countries.

Mauro CarcelliDepartment of Chemistry, University of Parma Parma, Italy.
Dominga RogolinoDepartment of Chemistry, University of ParmaParma, Italy; Research Interuniversity Consortium Chemistry of Metals in Biological Systems Parma Unit, University of ParmaParma, Italy.
Anna GattiDepartment of Chemistry, University of ParmaParma, Italy; Research Interuniversity Consortium Chemistry of Metals in Biological Systems Parma Unit, University of ParmaParma, Italy.
Nicolino PalaDepartment of Chemistry and Pharmacy, University of Sassari Sassari, Italy.
Angela CoronaDepartment of Life and Environmental Sciences, University of Cagliari, Cittadella Universitaria di Monserrato Cagliari, Italy.
Alessia CareddaDepartment of Life and Environmental Sciences, University of Cagliari, Cittadella Universitaria di Monserrato Cagliari, Italy.
Enzo TramontanoDepartment of Life and Environmental Sciences, University of Cagliari, Cittadella Universitaria di MonserratoCagliari, Italy; Genetics and Biomedical Research institute, National Research CouncilMonserrato, Italy.
Christophe PannecouqueRega Institute for Medical Research, KU Leuven Leuven, Belgium.
Lieve NaesensRega Institute for Medical Research, KU Leuven Leuven, Belgium.
Francesca EspositoDepartment of Life and Environmental Sciences, University of Cagliari, Cittadella Universitaria di Monserrato Cagliari, Italy.
University of Cagliari · ITUniversity of Parma · ITKU Leuven · BENational Research Council · ITUniversity of Sassari · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human immunodeficiency virus type 1 (HIV-1) infection, still represent a serious global health emergency. The chronic toxicity derived from the current anti-retroviral therapy limits the prolonged use of several antiretroviral agents, continuously requiring the discovery of new antiviral agents with innovative strategies of action. In particular, the development of single molecules targeting two proteins (dual inhibitors) is one of the current main goals in drug discovery. In this contest, metal-chelating molecules have been extensively explored as potential inhibitors of viral metal-dependent enzymes, resulting in some important classes of antiviral agents. Inhibition of HIV Integrase (IN) is, in this sense, paradigmatic. HIV-1 IN and Reverse Transcriptase-associated Ribonuclease H (RNase H) active sites show structural homologies, with the presence of two Mg(II) cofactors, hence it seems possible to inhibit both enzymes by means of chelating ligands with analogous structural features. Here we present a series of

Indexed as

acylhydrazoneantiviral agentschelating pharmacophoredual inhibitorsHIV-1 integraseRNase H

Identifiers

PMID28373864
PMCPMC5357622
OpenAlexW2593402194

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.