Evidence map›Paper›PMID 35891446›Full record

ArticleViruses2022

Multi-Substituted Quinolines as HIV-1 Integrase Allosteric Inhibitors.

Long Phi Dinh, Jian Sun, Courtney D Glenn, Krunal Patel, Julie A Pigza, Matthew G Donahue, Larry Yet, Jacques J Kessl

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Viruses, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. HIV-1 Integrase Inhibition Activity by Spiroketals Derived fromPharmaceuticals (Basel, Switzerland) · 2023
    Article
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 2 institutions in 1 country.

Long Phi DinhDepartment of Chemistry, University of South Alabama, Mobile, AL 36688, USA.ORCID 0000-0002-4600-6374
Jian SunDepartment of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg, MS 39406, USA.
Courtney D GlennDepartment of Chemistry, University of South Alabama, Mobile, AL 36688, USA.ORCID 0000-0002-0508-2573
Krunal PatelDepartment of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg, MS 39406, USA.
Julie A PigzaDepartment of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg, MS 39406, USA.
Matthew G DonahueDepartment of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg, MS 39406, USA.ORCID 0000-0002-2608-1529
Larry YetDepartment of Chemistry, University of South Alabama, Mobile, AL 36688, USA.
Jacques J KesslDepartment of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg, MS 39406, USA.ORCID 0000-0001-8103-6678
University of Southern Mississippi · USUniversity of South Alabama · US

Funding

Training and Mentoring Core P20GM103476 · NIGMS · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI MICHAEL R GARRETT · 2012 to 2026
$60.2M
New Inhibitors Targeting HIV-1 Integrase During Viral MaturationR01AI140985 · NIAID · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI Jacques J. Kessl · 2019 to 2026
$2.2M
Asymmetric Synthesis of Bioactive Nitrogen HeterocyclesR15GM129751 · NIGMS · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI DONAHUE, MATTHEW GARRETT · 2018 to 2018
$439k
NIAID NIH HHS R01 AI140985NIGMS NIH HHS P20 GM103476NIH HHS AI140985NIH HHS GM129751NIH HHS P20GM103476
6 · The paper itself

Abstract

Allosteric HIV-1 integrase (IN) inhibitors, or ALLINIs, are a new class of antiviral agents that bind at the dimer interface of the IN, away from the enzymatic catalytic site and block viral replication by triggering an aberrant multimerization of the viral enzyme. To further our understanding of the important binding features of multi-substituted quinoline-based ALLINIs, we have examined the IN multimerization and antiviral properties of substitution patterns at the 6 or 8 position. We found that the binding properties of these ALLINIs are negatively impacted by the presence of bulky substitutions at these positions. In addition, we have observed that the addition of bromine at either the 6 (6-bromo) or 8 (8-bromo) position conferred better antiviral properties. Finally, we found a significant loss of potency with the 6-bromo when tested with the ALLINI-resistant IN A128T mutant virus, while the 8-bromo analog retained full effectiveness.

Indexed as

HIV-1HIV IntegraseHIV Integrase InhibitorsQuinolinesAllosteric RegulationAntiviral AgentsVirus ReplicationAntiviral AgentsHIV IntegraseHIV Integrase Inhibitorsp31 integrase protein, Human immunodeficiency virus 1QuinolinesALLINIHIV-1integrasemultimerizationquinolines

Identifiers

PMID35891446
PMCPMC9324412
OpenAlexW4283814020

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.