Evidence map›Paper›PMID 33870216›Full record

ArticleCurrent research in structural biology2020

Integrative structural biology studies of HIV-1 reverse transcriptase binding to a high-affinity DNA aptamer.

Steve Tuske, Jie Zheng, Erik D Olson, Francesc X Ruiz, Bruce D Pascal, Anthony Hoang, Joseph D Bauman, Kalyan Das, Jeffrey J DeStefano, Karin Musier-Forsyth and 2 more

Open access · goldAbstract read
In one paragraph

Article in Current research in structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

13 citing papers in PubMed, 17 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

12 authors at 4 institutions in 1 country.

Steve TuskeCenter for Advanced Biotechnology and Medicine, And Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ, 08854, USA.
Jie ZhengDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL, 33458, USA.
Erik D OlsonDepartment of Chemistry and Biochemistry, Center for RNA Biology, And Center for Retrovirus Research, The Ohio State University, Columbus, OH, 43210, USA.
Francesc X RuizCenter for Advanced Biotechnology and Medicine, And Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ, 08854, USA.
Bruce D PascalDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL, 33458, USA.
Anthony HoangCenter for Advanced Biotechnology and Medicine, And Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ, 08854, USA.
Joseph D BaumanCenter for Advanced Biotechnology and Medicine, And Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ, 08854, USA.
Kalyan DasCenter for Advanced Biotechnology and Medicine, And Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ, 08854, USA.
Jeffrey J DeStefanoDepartment of Cell Biology and Molecular Genetics, University of Maryland College Park, College Park, MD, 20740, USA.
Karin Musier-ForsythDepartment of Chemistry and Biochemistry, Center for RNA Biology, And Center for Retrovirus Research, The Ohio State University, Columbus, OH, 43210, USA.
Patrick R GriffinDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL, 33458, USA.
Eddy ArnoldCenter for Advanced Biotechnology and Medicine, And Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ, 08854, USA.
Rutgers, The State University of New Jersey · USScripps Research Institute · USThe Ohio State University · USUniversity of Maryland, College Park · US

Funding

Project 9P50GM103368 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI OLSON, ARTHUR J. · 2012 to 2016
$20.0M
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
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
CHEMISTRY/BIOLOGY TRAINING GRANTT32GM008512 · NIGMS · OHIO STATE UNIVERSITY · PI PEI, DEHUA · 1996 to 2016
$3.9M
MINOS (Macromolecular Insights on Nucleic acids Optimized by Scattering)R01GM105404 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 2012 to 2015
$2.1M
Cellular Factors Critical for Initiation of HIV-1 Reverse TranscriptaseR01AI150493 · NIAID · OHIO STATE UNIVERSITY · PI MUSIER-FORSYTH, KARIN M · 2020 to 2022
$1.2M
Biochemistry of HIV reverse transcriptase fidelity and inhibitor interactionsR01AI150480 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI DESTEFANO, JEFFREY J · 2019 to 2019
$294k
Mechanism of HIV-1 gRNA-Gag interaction leading to selective genome packagingF31AI120868 · NIAID · OHIO STATE UNIVERSITY · PI OLSON, ERIK DAVID · 2016 to 2017
$64k
NIAID NIH HHS F31 AI120868NIAID NIH HHS R01 AI027690NIAID NIH HHS R01 AI150480NIAID NIH HHS R01 AI150493NIAID NIH HHS R37 AI027690NIAID NIH HHS U54 AI150472NIGMS NIH HHS P50 GM103368NIGMS NIH HHS R01 GM105404NIGMS NIH HHS T32 GM008512
6 · The paper itself

Abstract

The high-resolution crystal structure of HIV-1 reverse transcriptase (RT) bound to a 38-mer DNA hairpin aptamer with low pM affinity was previously described. The high-affinity binding aptamer contained 2'-O-methyl modifications and a seven base-pair GC-rich tract and the structure of the RT-aptamer complex revealed specific contacts between RT and the template strand of the aptamer. Similar to all crystal structures of RT bound to nucleic acid template-primers, the aptamer bound RT with a bend in the duplex DNA. To understand the structural basis for the ultra-high-affinity aptamer binding, an integrative structural biology approach was used. Hydrogen-deuterium exchange coupled to liquid chromatography-mass spectrometry (HDX-MS) was used to examine the structural dynamics of RT alone and in the presence of the DNA aptamer. RT was selectively labeled with

Indexed as

HDX-MS high-Affinity DNA aptamerHIV-1 reverse transcriptaseIntegrative structural biologySELEXSubunit-specific 15N-labeling

Identifiers

PMID33870216
PMCPMC8052095
OpenAlexW3039291480

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.