Evidence map›Paper›PMID 31606878›Full record

ArticleJournal of biomolecular NMR2019

Conformational flexibility of adenine riboswitch aptamer in apo and bound states using NMR and an X-ray free electron laser.

Jienv Ding, Monalisa Swain, Ping Yu, Jason R Stagno, Yun-Xing Wang

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. An overview of structural approaches to study therapeutic RNAs.Frontiers in molecular biosciences · 2022
    Review
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.

Jienv DingProtein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, National Institute of Health, Frederick, MD, 21702, USA. jienyu.ding@nih.gov.
Monalisa SwainProtein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, National Institute of Health, Frederick, MD, 21702, USA.
Ping YuProtein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, National Institute of Health, Frederick, MD, 21702, USA.
Jason R StagnoProtein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, National Institute of Health, Frederick, MD, 21702, USA.
Yun-Xing WangProtein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, National Institute of Health, Frederick, MD, 21702, USA. wangyunx@mail.nih.gov.ORCID http://orcid.org/0000-0002-2175-0148

Funding

NIH HHS Intramural Research
6 · The paper itself

Abstract

Riboswitches are structured cis-regulators mainly found in the untranslated regions of messenger RNA. The aptamer domain of a riboswitch serves as a sensor for its ligand, the binding of which triggers conformational changes that regulate the behavior of its expression platform. As a model system for understanding riboswitch structures and functions, the add adenine riboswitch has been studied extensively. However, there is a need for further investigation of the conformational dynamics of the aptamer in light of the recent real-time crystallographic study at room temperature (RT) using an X-ray free electron laser (XFEL) and femtosecond X-ray crystallography (SFX). Herein, we investigate the conformational motions of the add adenine riboswitch aptamer domain, in the presence or absence of adenine, using nuclear magnetic resonance relaxation measurements and analysis of RT atomic displacement factors (B-factors). In the absence of ligand, the P1 duplex undergoes a fast exchange where the overall molecule exhibits a motion at k

Indexed as

Nuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationRiboswitchAdenineAptamers, NucleotideCrystallography, X-RayModels, MolecularAdenineAptamers, NucleotideRiboswitchAdenine riboswitchAptamerB-factorConformational exchangeCPMG

Identifiers

PMID31606878
PMCPMC6817744

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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.