Evidence map›Paper›PMID 36788191›Full record

ArticleMolecular diversity2024

Environmentally benign synthesis of unsymmetrical ureas and their evaluation as potential HIV-1 protease inhibitors via a computational approach.

Tsenbeni N Lotha, Kikoleho Richa, Viphrezolie Sorhie, Ketiyala, Vevosa Nakro, Imkongyanger, Vimha Ritse, Lemzila Rudithongru, Nima D Namsa, Latonglila Jamir

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Article in Molecular diversity, 2024. 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
0.7field-weighted citation impact, top 35% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. Recent Advances in Heterocyclic HIV Protease Inhibitors.International journal of molecular sciences · 2025
    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

10 authors at 2 institutions in 1 country.

Tsenbeni N LothaDepartment of Environmental Science, Nagaland University, Lumami, Nagaland, 798627, India.
Kikoleho RichaDepartment of Chemistry, Nagaland University, Lumami, Nagaland, 798627, India.
Viphrezolie SorhieDepartment of Environmental Science, Nagaland University, Lumami, Nagaland, 798627, India.
KetiyalaDepartment of Environmental Science, Nagaland University, Lumami, Nagaland, 798627, India.
Vevosa NakroDepartment of Environmental Science, Nagaland University, Lumami, Nagaland, 798627, India.
ImkongyangerDepartment of Environmental Science, Nagaland University, Lumami, Nagaland, 798627, India.
Vimha RitseDepartment of Environmental Science, Nagaland University, Lumami, Nagaland, 798627, India.
Lemzila RudithongruDepartment of Environmental Science, Nagaland University, Lumami, Nagaland, 798627, India.
Nima D NamsaDepartment of Molecular Biology and Biotechnology, Tezpur University, Napaam, Assam, 784028, India.
Latonglila JamirDepartment of Environmental Science, Nagaland University, Lumami, Nagaland, 798627, India. latongli.jamir@gmail.com.ORCID http://orcid.org/0000-0003-4039-9426
Nagaland University · INTezpur University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present work reports the cost-effective, high yielding and environmentally acceptable preparation of unsymmetrical ureas from thiocarbamate salts using sodium percarbonate as an oxidant. Efficacy of the unsymmetrical ureas as potential human immune deficiency virus (HIV-1) protease inhibitors has been evaluated via in silico approach. The results revealed interactions of the urea compounds at the active site of the enzyme with favorable binding affinities causing possible mutations hindering the functioning of the enzyme. Further computational assessment of IC50 using known references satisfactorily authenticated the inhibitory action of the selected compounds against HIV-1 protease. Added to the easy synthesis of the ureas following an environmentally benign protocol, this work may be a valuable addition to the ongoing search for drugs with better efficacy profiles and reduced toxicity against HIV.

Indexed as

HIV ProteaseHIV Protease InhibitorsMolecular Docking SimulationUreaGreen Chemistry TechnologyHIV-1HumansStructure-Activity RelationshipHIV ProteaseHIV Protease Inhibitorsp16 protease, Human immunodeficiency virus 1UreaHIV-1 protease inhibitorsIn silicoMolecular dockingUrea

Identifiers

PMID36788191
OpenAlexW4320857240

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.