Evidence map›Paper›PMID 27977168›Full record

ArticleAnalytical chemistry2017

Spectral and Hydrodynamic Analysis of West Nile Virus RNA-Protein Interactions by Multiwavelength Sedimentation Velocity in the Analytical Ultracentrifuge.

Jin Zhang, Joseph Z Pearson, Gary E Gorbet, Helmut Cölfen, Markus W Germann, Margo A Brinton, Borries Demeler

Abstract read
In one paragraph

Article in Analytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

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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

7 authors.

Jin ZhangGeorgia State University , Department of Chemistry, 50 Decatur St. SE, Atlanta, Georgia 30303, United States.
Joseph Z PearsonUniversity of Konstanz , Department of Chemistry, Physical Chemistry, Universitätsstraße 10, Box 714, D-78457 Konstanz, Germany.
Gary E GorbetThe University of Texas Health Science Center at San Antonio , 7703 Floyd Curl Drive, MC 7760, San Antonio, Texas 78229-3901, United States.
Helmut CölfenUniversity of Konstanz , Department of Chemistry, Physical Chemistry, Universitätsstraße 10, Box 714, D-78457 Konstanz, Germany.
Markus W GermannGeorgia State University , Department of Chemistry, 50 Decatur St. SE, Atlanta, Georgia 30303, United States.
Margo A BrintonGeorgia State University , Department of Biology, P.O. 4010, Atlanta, Georgia 30303, United States.
Borries DemelerThe University of Texas Health Science Center at San Antonio , 7703 Floyd Curl Drive, MC 7760, San Antonio, Texas 78229-3901, United States.ORCID 0000-0002-2414-9518

Funding

Development of an UltraScan Meta-Scheduler for HPC Job SubmissionR01GM120600 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Emre H. Brookes, BORRIES DEMELER · 2016 to 2026
$3.6M
Regulation of West Nile Virus ReplicationR01AI048088 · NIAID · GEORGIA STATE UNIVERSITY · PI BRINTON, MARGO A · 2003 to 2012
$2.3M
NIAID NIH HHS R01 AI048088NIGMS NIH HHS R01 GM120600
6 · The paper itself

Abstract

Interactions between nucleic acids and proteins are critical for many cellular processes, and their study is of utmost importance to many areas of biochemistry, cellular biology, and virology. Here, we introduce a new analytical method based on sedimentation velocity (SV) analytical ultracentrifugation, in combination with a novel multiwavelength detector to characterize such interactions. We identified the stoichiometry and molar mass of a complex formed during the interaction of a West Nile virus RNA stem loop structure with the human T cell-restricted intracellular antigen-1 related protein. SV has long been proven as a powerful technique for studying dynamic assembly processes under physiological conditions in solution. Here, we demonstrate, for the first time, how the new multiwavelength technology can be exploited to study protein-RNA interactions, and show how the spectral information derived from the new detector complements the traditional hydrodynamic information from analytical ultracentrifugation. Our method allows the protein and nucleic acid signals to be separated by spectral decomposition such that sedimentation information from each individual species, including any complexes, can be clearly identified based on their spectral signatures. The method presented here extends to any interacting system where the interaction partners are spectrally separable.

Indexed as

HydrodynamicsUltracentrifugationHumansRNA, ViralT-Cell Intracellular Antigen-1West Nile virusRNA, ViralT-Cell Intracellular Antigen-1TIA1 protein, human

Identifiers

PMID27977168
PMCPMC5505516

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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.