Evidence map›Paper›PMID 31409143›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2019

Kinetic and thermodynamic characterisation of HIV-protease inhibitors against E35D↑G↑S mutant in the South African HIV-1 subtype C protease.

Sibusiso Maseko, Eden Padayachee, Siyabonga Maphumulo, Thavendran Govender, Yasien Sayed, Glenn Maguire, Johnson Lin, Tricia Naicker, Sooraj Baijnath, Kruger Hendrik Gerhardus

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

Article in Journal of enzyme inhibition and medicinal chemistry, 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
0.7field-weighted citation impact, top 30% 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, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. Peptides, Antibodies, Peptide Antibodies and More.International journal of molecular sciences · 2019
    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.

Sibusiso Masekoa Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal , Durban , South Africa.ORCID http://orcid.org/0000-0001-7025-6106
Eden Padayacheea Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal , Durban , South Africa.
Siyabonga Maphumuloa Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal , Durban , South Africa.
Thavendran Govendera Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal , Durban , South Africa.
Yasien Sayedb Protein Structure-Function Research Unit, School of Molecular and Cell Biology, University of the Witwatersrand , Wits , South Africa.
Glenn Maguirea Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal , Durban , South Africa.
Johnson Lind School of Life Sciences, University of KwaZulu-Natal , Durban , South Africa.
Tricia Naickera Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal , Durban , South Africa.
Sooraj Baijnatha Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal , Durban , South Africa.
Kruger Hendrik Gerhardusa Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal , Durban , South Africa.ORCID http://orcid.org/0000-0003-0606-2053
University of KwaZulu-Natal · ZAUniversity of the Witwatersrand · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herein, we report the effect of nine FDA approved protease inhibitor drugs against a new HIV-1 subtype C mutant protease, E35D↑G↑S. The mutant has five mutations, E35D, two insertions, position 36 (G and S), and D60E. Kinetics, inhibition constants, vitality, Gibbs free binding energies are reported. The variant showed a decreased affinity for substrate and low catalytic efficiency compared to the wild type. There was a significant decrease in the binding of seven FDA approved protease inhibitors against the mutant (

Indexed as

ThermodynamicsHIV-1HIV ProteaseHIV Protease InhibitorsInhibitory Concentration 50KineticsMolecular Docking SimulationMutationHIV ProteaseHIV Protease Inhibitorsp16 protease, Human immunodeficiency virus 1HIVinhibitormutantProteasethermodynamics

Identifiers

PMID31409143
PMCPMC6713120
OpenAlexW2967653239

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.