Evidence map›Paper›PMID 33333923›Full record

ReviewInternational journal of molecular sciences2020

Large Multidomain Protein NMR: HIV-1 Reverse Transcriptase Precursor in Solution.

Tatiana V Ilina, Zhaoyong Xi, Teresa Brosenitsch, Nicolas Sluis-Cremer, Rieko Ishima

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 50% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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 1 institution in 1 country.

Tatiana V IlinaDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.ORCID 0000-0002-9985-5978
Zhaoyong XiDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Teresa BrosenitschDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Nicolas Sluis-CremerDepartment of Medicine, Division of Infectious Diseases, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA.
Rieko IshimaDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.ORCID 0000-0002-3418-0922
University of Pittsburgh · US

Funding

Technology Development 2: MAS NMR and dynamic nuclear polarization for HIV-1 structural biologyP50AI150481 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GRONENBORN, ANGELA M. · 2019 to 2021
$14.1M
NIAID NIH HHS P50 AI150481NIH HHS AI150481
6 · The paper itself

Abstract

NMR studies of large proteins, over 100 kDa, in solution are technically challenging and, therefore, of considerable interest in the biophysics field. The challenge arises because the molecular tumbling of a protein in solution considerably slows as molecular mass increases, reducing the ability to detect resonances. In fact, the typical

Indexed as

Magnetic Resonance SpectroscopyProtein Interaction Domains and MotifsBinding SitesHIV-1HIV InfectionsHIV Reverse TranscriptaseHumansModels, MolecularProtein BindingProtein ConformationProtein MultimerizationSolubilitySolutionsHIV Reverse Transcriptasereverse transcriptase, Human immunodeficiency virus 1SolutionsHIVisotope labelingNMRproteinreverse transcriptaseribonuclease H

Identifiers

PMID33333923
PMCPMC7765405
OpenAlexW3112287447

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.