Evidence map›Paper›PMID 40363675›Full record

ArticleMolecules (Basel, Switzerland)2025

Design, Synthesis and Biological Evaluation of 3-Hydrazonoindolin-2-one Derivatives as Novel HIV-1 RNase H Inhibitors.

Yiying Zhang, Rao Wang, Yueyue Bu, Angela Corona, Laura Dettori, Enzo Tramontano, Christophe Pannecouque, Erik De Clercq, Shuai Wang, Ge Meng and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2025. 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
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.

  1. 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

11 authors.

Yiying ZhangEngineering Center of Catalysis and Synthesis for Chiral Molecules, Department of Chemistry, Fudan University, Shanghai 200433, China.
Rao WangHenan Key Laboratory of Nanomedicine for Targeting Diagnosis and Treatment, School of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450001, China.
Yueyue BuHenan Key Laboratory of Nanomedicine for Targeting Diagnosis and Treatment, School of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450001, China.
Angela CoronaDepartment of Life and Environmental Sciences, University of Cagliari, 09042 Monserrato, Italy.ORCID 0000-0002-6630-8636
Laura DettoriDepartment of Life and Environmental Sciences, University of Cagliari, 09042 Monserrato, Italy.ORCID 0009-0005-5101-4992
Enzo TramontanoDepartment of Life and Environmental Sciences, University of Cagliari, 09042 Monserrato, Italy.ORCID 0000-0002-4849-0980
Christophe PannecouqueRega Institute for Meical Research, KU Leuven, Herestraat 49, B-3000 Leuven, Belgium.ORCID 0000-0002-1254-4473
Erik De ClercqRega Institute for Meical Research, KU Leuven, Herestraat 49, B-3000 Leuven, Belgium.ORCID 0000-0002-2985-8890
Shuai WangEngineering Center of Catalysis and Synthesis for Chiral Molecules, Department of Chemistry, Fudan University, Shanghai 200433, China.ORCID 0000-0003-0718-1820
Ge MengEngineering Center of Catalysis and Synthesis for Chiral Molecules, Department of Chemistry, Fudan University, Shanghai 200433, China.
Fen-Er ChenEngineering Center of Catalysis and Synthesis for Chiral Molecules, Department of Chemistry, Fudan University, Shanghai 200433, China.

Funding

National Natural Science Foundation of China 21871055
6 · The paper itself

Abstract

Targeting ribonuclease H (RNase H) has emerged as a highly promising strategy for treating HIV-1. In this study, a series of novel 3-hydrazonoindolin-2-one derivatives were designed and synthesized as potential inhibitors of HIV-1 RNase H. Notably, several of these derivatives displayed micromolar inhibitory activity. Among the compounds examined, the hit compound demonstrated potent inhibition of HIV-1 RNase H, boasting a Ki value of 2.31 μM. Additionally, the most potent compound of this general structure exhibited remarkable inhibitory activity, with Ki values of 0.55 μM. Through docking studies, the key interactions of this ligand within the active site of RNase H were uncovered. This novel chemical structure can be regarded as a prospective scaffold for the future development of RNase H inhibitors.

Indexed as

Anti-HIV AgentsDrug DesignEnzyme InhibitorsHIV-1HydrazonesIndolesRibonuclease H, Human Immunodeficiency VirusCatalytic DomainHumansMolecular Docking SimulationMolecular StructureStructure-Activity RelationshipAnti-HIV AgentsEnzyme InhibitorsHydrazonesIndolesRibonuclease H, Human Immunodeficiency Virus3-hydrazonoindolin-2-oneAIDSHIVRNase H

Identifiers

PMID40363675
PMCPMC12073785

What OpenQuestion holds

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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.