Evidence map›Paper›PMID 23595992›Full record

ArticleThe Journal of biological chemistry2013

Examining the role of the HIV-1 reverse transcriptase p51 subunit in positioning and hydrolysis of RNA/DNA hybrids.

Suhman Chung, Jennifer T Miller, Mikalai Lapkouski, Lan Tian, Wei Yang, Stuart F J Le Grice

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
1.2field-weighted citation impact, top 23% 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, 20 citations in OpenAlex.

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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

6 authors at 3 institutions in 1 country.

Suhman ChungRT Biochemistry Section, HIV Drug Resistance Program, Center for Cancer Research, NCI, National Institutes of Health, Frederick Maryland 21702, USA.
Jennifer T Miller
Mikalai Lapkouski
Lan Tian
Wei Yang
Stuart F J Le Grice
National Institutes of Health · USCenter for Cancer Research · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Viral and Host Proteins as Therapeutic TargetsZIABC010494 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI LE GRICE, STUART F. J. · 2009 to 2021
$9.0M
Single-Molecule Spectroscopy of HIV-1 Replication ComplexesZIABC011443 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI LE GRICE, STUART F. J. · 2012 to 2018
$1.4M
Intramural NIH HHS
6 · The paper itself

Abstract

Recent crystallographic analysis of p66/p51 human immunodeficiency virus (HIV) type 1 reverse transcriptase (RT) complexed with a non-polypurine tract RNA/DNA hybrid has illuminated novel and important contacts between structural elements at the C terminus of the noncatalytic p51 subunit and the nucleic acid duplex in the vicinity of the ribonuclease H (RNase H) active site. In particular, a short peptide spanning residues Phe-416-Pro-421 was shown to interact with the DNA strand, cross the minor groove of the helix, and then form Van der Waals contacts with the RNA strand adjacent to the scissile phosphate. At the base of the adjoining α-helix M', Tyr-427 forms a hydrogen bond with Asn-348, the latter of which, when mutated to Ile, is implicated in resistance to both nucleoside and non-nucleoside RT inhibitors. Based on our structural data, we analyzed the role of the p51 C terminus by evaluating selectively mutated p66/p51 heterodimers carrying (i) p51 truncations that encroach on α-M', (ii) alterations that interrupt the Asn-348-Tyr-427 interaction, and (iii) alanine substitutions throughout the region Phe-416-Pro-421. Collectively, our data support the notion that the p51 C terminus makes an important contribution toward hybrid binding and orienting the RNA strand for catalysis at the RNase H active site.

Indexed as

Amino Acid SubstitutionCatalytic DomainDNA, ViralHIV-1HIV Reverse TranscriptaseHumansHydrolysisMutation, MissenseNucleic Acid HeteroduplexesProtein Structure, SecondaryRNA, ViralDNA, ViralHIV Reverse TranscriptaseNucleic Acid Heteroduplexesreverse transcriptase, Human immunodeficiency virus 1RNA, ViralEnzyme MechanismsEnzyme StructureHIVProtein-Nucleic Acid InteractionReverse Transcription

Identifiers

PMID23595992
PMCPMC3668773
OpenAlexW2021841512

What OpenQuestion holds

Textmetadata
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.