Evidence map›Paper›PMID 25341667›Full record

ReviewViruses2014

The lysine 65 residue in HIV-1 reverse transcriptase function and in nucleoside analog drug resistance.

Scott J Garforth, Chisanga Lwatula, Vinayaka R Prasad

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

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  8. 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

3 authors at 1 institution in 1 country.

Scott J GarforthDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. scott.garforth@einstein.yu.edu.
Chisanga LwatulaDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. scott.garforth@einstein.yu.edu.
Vinayaka R PrasadDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. vinayaka.prasad@einstein.yu.edu.
Albert Einstein College of Medicine · US

Funding

Immunology/Pathology CoreP30AI051519 · NIAID · YESHIVA UNIVERSITY · PI GOLDSTEIN, HARRIS · 2003 to 2013
$18.6M
The role of viral and cellular proteins in early events of HIV-1 replicationR37AI030861 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI PRASAD, VINAYAKA R. · 2007 to 2016
$4.4M
NIAID NIH HHS P30 AI051519NIAID NIH HHS R37 AI030861
6 · The paper itself

Abstract

Mutations in HIV-1 reverse transcriptase (RT) that confer nucleoside analog RT inhibitor resistance have highlighted the functional importance of several active site residues (M184, Q151 and K65) in RT catalytic function. Of these, K65 residue is notable due to its pivotal position in the dNTP-binding pocket, its involvement in nucleoside analog resistance and polymerase fidelity. This review focuses on K65 residue and summarizes a substantial body of biochemical and structural studies of its role in RT function and the functional consequences of the K65R mutation.

Indexed as

Amino Acid SubstitutionCatalytic DomainDrug Resistance, ViralHIV-1HIV Reverse TranscriptaseHumansLysineModels, MolecularMutation, MissenseReverse Transcriptase InhibitorsHIV Reverse TranscriptaseLysinereverse transcriptase, Human immunodeficiency virus 1Reverse Transcriptase Inhibitors

Identifiers

PMID25341667
PMCPMC4213578
OpenAlexW2081613607

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.