Evidence map›Paper›PMID 24359751›Full record

ArticleBiophysical journal2013

Single-molecule force spectroscopy study on the mechanism of RNA disassembly in tobacco mosaic virus.

Ningning Liu, Ying Chen, Bo Peng, Yuan Lin, Qian Wang, Zhaohui Su, Wenke Zhang, Hongbin Li, Jiacong Shen

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

5 citing papers in PubMed, 20 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 6 institutions in 3 countries.

Ningning LiuState Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun, P. R. China; School of Chemistry and Material Science, Liaoning Shihua University, Fushun, P. R. China.
Ying ChenState Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun, P. R. China.
Bo PengState Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, P. R. China.
Yuan LinState Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, P. R. China.
Qian WangState Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, P. R. China; Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina. Electronic address: wang@mail.chem.sc.edu.
Zhaohui SuState Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, P. R. China.
Wenke ZhangState Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun, P. R. China. Electronic address: zhangwk@jlu.edu.cn.
Hongbin LiState Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun, P. R. China; Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada.
Jiacong ShenState Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun, P. R. China.
Jilin University · CNState Key Laboratory of Polymer Physics and Chemistry · CNState Key Laboratory of Supramolecular Structure and MaterialsChangchun Institute of Applied Chemistry · CNChinese Academy of Sciences · CNLiaoning Shihua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To explore the disassembly mechanism of tobacco mosaic virus (TMV), a model system for virus study, during infection, we have used single-molecule force spectroscopy to mimic and follow the process of RNA disassembly from the protein coat of TMV by the replisome (molecular motor) in vivo, under different pH and Ca(2+) concentrations. Dynamic force spectroscopy revealed the unbinding free-energy landscapes as that at pH 4.7 the disassembly process is dominated by one free-energy barrier, whereas at pH 7.0 the process is dominated by one barrier and that there exists a second barrier. The additional free-energy barrier at longer distance has been attributed to the hindrance of disordered loops within the inner channel of TMV, and the biological function of those protein loops was discussed. The combination of pH increase and Ca(2+) concentration drop could weaken RNA-protein interactions so much that the molecular motor replisome would be able to pull and disassemble the rest of the genetic RNA from the protein coat in vivo. All these facts provide supporting evidence at the single-molecule level, to our knowledge for the first time, for the cotranslational disassembly mechanism during TMV infection under physiological conditions.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceCalciumCapsid ProteinsDNA-Directed DNA PolymeraseHydrogen-Ion ConcentrationMicroscopy, Atomic ForceMolecular Sequence DataMultienzyme ComplexesProtein BindingReplisomesRNA, ViralSpectrum AnalysisTobacco Mosaic VirusCalciumCapsid ProteinsDNA-Directed DNA PolymeraseMultienzyme ComplexesReplisomesRNA, Viral

Identifiers

PMID24359751
PMCPMC3882505
OpenAlexW1984596171

What OpenQuestion holds

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Registered trials

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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.