Evidence map›Paper›PMID 17997580›Full record

ArticleBiochemistry2007

Site-specific variations in RNA folding thermodynamics visualized by 2-aminopurine fluorescence.

Jeff D Ballin, Shashank Bharill, Elizabeth J Fialcowitz-White, Ignacy Gryczynski, Zygmunt Gryczynski, Gerald M Wilson

Open access · greenAbstract readValidation Study
In one paragraph

Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 46 citations in OpenAlex.

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  15. 2-aminopurine as a probe for quadruplex loop structures.Methods in molecular biology (Clifton, N.J.) · 2010
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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

6 authors at 3 institutions in 1 country.

Jeff D BallinDepartment of Biochemistry and Molecular Biology and Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.
Shashank Bharill
Elizabeth J Fialcowitz-White
Ignacy Gryczynski
Zygmunt Gryczynski
Gerald M Wilson
University of Maryland, Baltimore · USUniversity of North Texas Health Science Center · USUniversity of North Texas · US

Funding

Visceral Fat & Lipid & Inflammatory Risk factors: Role of EthnicityP20MD001633 · NIMHD · UNIVERSITY OF NORTH TEXAS HLTH SCI CTR · PI GONZALEZ, ADELA · 2005 to 2009
$7.1M
Mechanisms directing oncoprotein and cytokine mRNA decayR01CA102428 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI WILSON, GERALD M. · 2003 to 2013
$2.8M
Mechanisms directing oncoprotein and cytokine mRNA decayR56CA102428 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI WILSON, GERALD M. · 2008 to 2008
$363k
NCI NIH HHS CA102428NCI NIH HHS R01 CA102428NCI NIH HHS R56 CA102428NIMHD NIH HHS P20 MD001633
6 · The paper itself

Abstract

The fluorescent base analogue 2-aminopurine (2-AP) is commonly used to study specific conformational and protein binding events involving nucleic acids. Here, combinations of steady-state and time-resolved fluorescence spectroscopy of 2-AP were employed to monitor conformational transitions within a model hairpin RNA from diverse structural perspectives. RNA substrates adopting stable, unambiguous secondary structures were labeled with 2-AP at an unpaired base, within the loop, or inside the base-paired stem. Steady-state fluorescence was monitored as the RNA hairpins made the transitions between folded and unfolded conformations using thermal denaturation, urea titration, and cation-mediated folding. Unstructured control RNA substrates permitted the effects of higher-order RNA structures on 2-AP fluorescence to be distinguished from stimulus-dependent changes in intrinsic 2-AP photophysics and/or interactions with adjacent residues. Thermodynamic parameters describing local conformational changes were thus resolved from multiple perspectives within the model RNA hairpin. These data provided energetic bases for construction of folding mechanisms, which varied among different folding-unfolding stimuli. Time-resolved fluorescence studies further revealed that 2-AP exhibits characteristic signatures of component fluorescence lifetimes and respective fractional contributions in different RNA structural contexts. Together, these studies demonstrate localized conformational events contributing to RNA folding and unfolding that could not be observed by approaches monitoring only global structural transitions.

Indexed as

Nucleic Acid Conformation2-AminopurineNucleic Acid DenaturationOligoribonucleotidesRNASpectrometry, FluorescenceThermodynamics2-AminopurineOligoribonucleotidesRNA

Identifiers

PMID17997580
PMCPMC2274907
OpenAlexW2063034066

What OpenQuestion holds

Textmetadata
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.