Evidence map›Paper›PMID 34419931›Full record

ArticleJournal of molecular graphics & modelling2021

Revertant mutation V48G alters conformational dynamics of highly drug resistant HIV protease PRS17.

Shelley H Burnaman, Daniel W Kneller, Yuan-Fang Wang, Andrey Kovalevsky, Irene T Weber

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

Article in Journal of molecular graphics & modelling, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 58% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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

5 authors at 2 institutions in 1 country.

Shelley H BurnamanDepartment of Biology, Georgia State University, Atlanta, GA, USA.
Daniel W KnellerNeutron Scattering Division, Oak Ridge National Laboratory, 1 Bethel Valley Road, Oak Ridge, TN, 37831, USA.
Yuan-Fang WangDepartment of Biology, Georgia State University, Atlanta, GA, USA.
Andrey KovalevskyNeutron Scattering Division, Oak Ridge National Laboratory, 1 Bethel Valley Road, Oak Ridge, TN, 37831, USA.
Irene T WeberDepartment of Biology, Georgia State University, Atlanta, GA, USA. Electronic address: iweber@gsu.edu.
Georgia State University · USOak Ridge National Laboratory · US

Funding

Inhibition of Resistant Variants of HIV ProteaseU01AI150461 · NIAID · GEORGIA STATE UNIVERSITY · PI HARRISON, ROBERT WILSON, WEBER, IRENE T · 2019 to 2020
$691k
NIAID NIH HHS U01 AI150461
6 · The paper itself

Abstract

Drug resistance is a serious problem for controlling the HIV/AIDS pandemic. Current antiviral drugs show several orders of magnitude worse inhibition of highly resistant clinical variant PRS17 of HIV-1 protease compared with wild-type protease. We have analyzed the effects of a common resistance mutation G48V in the flexible flaps of the protease by assessing the revertant PRS17

Indexed as

HIV Protease InhibitorsPharmaceutical PreparationsCatalytic DomainDrug Resistance, ViralHIV ProteaseMutationProtein ConformationHIV ProteaseHIV Protease InhibitorsPharmaceutical PreparationsDrug resistanceHIV proteaseMolecular mechanism of resistanceStructural dynamics

Identifiers

PMID34419931
PMCPMC8435028
OpenAlexW3196245669

What OpenQuestion holds

Textmetadata
LicenceTDM
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.