Evidence map›Paper›PMID 33171603›Full record

ArticleViruses2020

Darunavir-Resistant HIV-1 Protease Constructs Uphold a Conformational Selection Hypothesis for Drug Resistance.

Zhanglong Liu, Trang T Tran, Linh Pham, Lingna Hu, Kyle Bentz, Daniel A Savin, Gail E Fanucci

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.2field-weighted citation impact, top 34% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
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  4. Review
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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

7 authors at 2 institutions in 1 country.

Zhanglong LiuDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Trang T TranDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Linh PhamDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Lingna HuDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Kyle BentzDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Daniel A SavinDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.ORCID 0000-0002-9235-517X
Gail E FanucciDepartment of Chemistry, University of Florida, Gainesville, FL 32611, USA.
University of Florida · USLinkedIn (United States) · US

Funding

Upgrade to E500 X- and Q-Band CW EPR Spectrometer for Biomedical ResearchS10RR031603 · NCRR · UNIVERSITY OF FLORIDA · PI FANUCCI, GAIL E · 2011 to 2011
$523k
NIH HHS GM105409NIH HHS S10 OD021758-01NIH HHS S10RR031603
6 · The paper itself

Abstract

Multidrug resistance continues to be a barrier to the effectiveness of highly active antiretroviral therapy in the treatment of human immunodeficiency virus 1 (HIV-1) infection. Darunavir (DRV) is a highly potent protease inhibitor (PI) that is oftentimes effective when drug resistance has emerged against first-generation inhibitors. Resistance to darunavir does evolve and requires 10-20 amino acid substitutions. The conformational landscapes of six highly characterized HIV-1 protease (PR) constructs that harbor up to 19 DRV-associated mutations were characterized by distance measurements with pulsed electron double resonance (PELDOR) paramagnetic resonance spectroscopy, namely double electron-electron resonance (DEER). The results show that the accumulated substitutions alter the conformational landscape compared to PI-naïve protease where the semi-open conformation is destabilized as the dominant population with open-like states becoming prevalent in many cases. A linear correlation is found between values of the DRV inhibition parameter K

Indexed as

Drug Resistance, Multiple, ViralAmino Acid SubstitutionDarunavirGenetic VariationHIVHIV ProteaseHIV Protease InhibitorsMutationProtein ConformationDarunavirHIV ProteaseHIV Protease Inhibitorsp16 protease, Human immunodeficiency virus 1darunavirDEER spectroscopydrug resistancegenetic and phenotypic diversityHIV-1 protease

Identifiers

PMID33171603
PMCPMC7695139
OpenAlexW3097931685

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.