Evidence map›Paper›PMID 31935541›Full record

ReviewCurrent opinion in structural biology2020

Evolving understanding of HIV-1 reverse transcriptase structure, function, inhibition, and resistance.

Francesc Xavier Ruiz, Eddy Arnold

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.3field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 80 citations in OpenAlex.

  1. Mechanism of HIV-1 Capsid Rupture and Uncoating by Reverse Transcription.bioRxiv : the preprint server for biology · 2026
    Article
  2. Protease-mediated maturation of M-PMV reverse transcriptase into a functional heterodimer.Protein science : a publication of the Protein Society · 2026
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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

2 authors at 1 institution in 1 country.

Francesc Xavier RuizCenter for Advanced Biotechnology and Medicine, and Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, 08854, NJ, USA.
Eddy ArnoldCenter for Advanced Biotechnology and Medicine, and Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, 08854, NJ, USA. Electronic address: arnold@cabm.rutgers.edu.
Rutgers, The State University of New Jersey · US

Funding

X-ray Crystallographic Fragment Screening CoreU54AI150472 · NIAID · SEATTLE CHILDREN'S HOSPITAL · PI SARAFIANOS, STEFAN G, TORBETT, BRUCE EDWARD · 2019 to 2021
$15.7M
STRUCTURES OF HIV REVERSE TRANSCRIPTASE WITH SUBSTRATESR37AI027690 · NIAID · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI ARNOLD, EDWARD · 1999 to 2018
$14.4M
X-ray Crystallographic Fragment Screening CoreU54GM103368 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SARAFIANOS, STEFAN G, TORBETT, BRUCE EDWARD · 2017 to 2018
$11.1M
STRUCTURES OF HIV REVERSE TRANSCRIPTASE WITH SUBSTRATESR01AI027690 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI EDWARD ARNOLD · 1989 to 2026
$4.3M
NIAID NIH HHS R01 AI027690NIAID NIH HHS R37 AI027690NIAID NIH HHS U54 AI150472NIGMS NIH HHS U54 GM103368
6 · The paper itself

Abstract

The essential role of reverse transcription in the HIV life cycle is illustrated by the fact that half of the ∼30 FDA-approved drugs for HIV treatment target HIV-1 reverse transcriptase (RT). Even though more than 160 structures of RT deposited in the Protein Data Bank (PDB) have revealed the molecular architecture of RT in great detail, some key states of RT function and inhibition remain still unknown. Recent structures of RT initiation complexes, RT poised for RNA hydrolysis, and RT with approved drugs and investigational compounds have provided a deeper understanding of RT function and inhibition, suggesting novel avenues for targeting this central enzyme of HIV.

Indexed as

Models, MolecularProtein ConformationAnti-HIV AgentsCryoelectron MicroscopyCrystallography, X-RayDrug Resistance, ViralHIV-1HIV Reverse TranscriptaseHumansMacromolecular SubstancesMolecular StructureMutationProtein BindingReverse Transcriptase InhibitorsStructure-Activity RelationshipAnti-HIV AgentsHIV Reverse TranscriptaseMacromolecular Substancesreverse transcriptase, Human immunodeficiency virus 1Reverse Transcriptase Inhibitors

Identifiers

PMID31935541
PMCPMC7596924
OpenAlexW2999016136

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.