Evidence map›Paper›PMID 30560566›Full record

ArticleChemical biology & drug design2019

Design, synthesis, and biologic evaluation of novel galloyl derivatives as HIV-1 RNase H inhibitors.

Ping Gao, Xueshun Wang, Lin Sun, Xiqiang Cheng, Vasanthanathan Poongavanam, Jacob Kongsted, Mar Álvarez, Joanna Luczkowiak, Christophe Pannecouque, Erik De Clercq and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in Chemical biology & drug design, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

3 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
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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

16 authors at 6 institutions in 5 countries.

Ping GaoDepartment of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, China.
Xueshun WangDepartment of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, China.
Lin SunDepartment of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, China.
Xiqiang ChengDepartment of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, China.
Vasanthanathan PoongavanamDepartment of Physics, Chemistry and Pharmacy, University of Southern Denmark, Odense M, Denmark.
Jacob KongstedDepartment of Physics, Chemistry and Pharmacy, University of Southern Denmark, Odense M, Denmark.
Mar ÁlvarezCentro de Biología Molecular "Severo Ochoa" (Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid), Madrid, Spain.
Joanna LuczkowiakCentro de Biología Molecular "Severo Ochoa" (Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid), Madrid, Spain.
Christophe PannecouqueRega Institute for Medical Research, K.U.Leuven, Leuven, Belgium.
Erik De ClercqRega Institute for Medical Research, K.U.Leuven, Leuven, Belgium.
Kuo-Hsiung LeeNatural Products Research Laboratories, Eshelman School of Pharmacy, University of North Carolina, Chapel Hill, North Carolina.
Chin-Ho ChenSurgical Science, Department of Surgery, Duke University Medical Center, Durham, North Carolina.
Huiqing LiuDepartment of Pharmacology, School of Basic Medical Sciences, Shandong University, Jinan, China.
Luis Menéndez-AriasCentro de Biología Molecular "Severo Ochoa" (Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid), Madrid, Spain.ORCID 0000-0002-1251-6640
Xinyong LiuDepartment of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, China.ORCID 0000-0002-7302-2214
Peng ZhanDepartment of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, China.ORCID 0000-0002-9675-6026
Shandong University · CNConsejo Superior de Investigaciones Científicas · ESRega Institute for Medical Research · BEUniversity of Southern Denmark · DKDuke University · USUniversity of North Carolina at Chapel Hill · US

Funding

PLANT ANTIHIV AGENTSR01AI033066 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LEE, KUO-HSIUNG · 1992 to 2018
$8.4M
NIAID NIH HHS R01 AI033066
6 · The paper itself

Abstract

Human immunodeficiency virus (HIV) reverse transcriptase (RT)-associated ribonuclease H (RNase H) remains as the only enzyme encoded within the viral genome not targeted by current antiviral drugs. In this work, we report the design, synthesis, and biologic evaluation of a novel series of galloyl derivatives with HIV-1 RNase H inhibitory activity. Most of them showed IC

Indexed as

Drug DesignAnti-HIV AgentsBenzoic AcidBinding SitesCatalytic DomainHIV-1HumansInhibitory Concentration 50Molecular Docking SimulationRibonuclease H, Human Immunodeficiency VirusStructure-Activity RelationshipTropoloneAnti-HIV AgentsBenzoic Acidbeta-thujaplicinolRibonuclease H, Human Immunodeficiency VirusTropolonegalloyl derivativesHIV-1RNase H inhibitors

Identifiers

PMID30560566
PMCPMC7441570
OpenAlexW2905383849

What OpenQuestion holds

Textmetadata
LicenceTDM
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.