Evidence map›Paper›PMID 20580964›Full record

ArticleMethods in enzymology2010

Analysis of complex single-molecule FRET time trajectories.

Mario Blanco, Nils G Walter

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
10.6field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 174 citations in OpenAlex.

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  19. Using Single-Molecule FRET to Evaluate DNA Nanodevices at Work.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  20. Article

34 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 1 country.

Mario BlancoDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan, USA.
Nils G Walter
Analysis Group (United States) · USUniversity of Michigan–Ann Arbor · US

Funding

CELLULAR AND MOLECULAR BIOLOGY AT MICHIGANT32GM007315 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PUTHENVEEDU, MANOJKUMAR A · 1985 to 2021
$12.8M
U-turn of the Hepatitis Delta Virus RibozymeR01GM062357 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WALTER, NILS G · 2001 to 2019
$5.8M
NIGMS NIH HHS R01 GM062357NIGMS NIH HHS T32 GM007315
6 · The paper itself

Abstract

Single-molecule methods have given researchers the ability to investigate the structural dynamics of biomolecules at unprecedented resolution and sensitivity. One of the preferred methods of studying single biomolecules is single-molecule fluorescence resonance energy transfer (smFRET). The popularity of smFRET stems from its ability to report on dynamic, either intra- or intermolecular interactions in real-time. For example, smFRET has been successfully used to characterize the role of dynamics in functional RNAs and their protein complexes, including ribozymes, the ribosome, and more recently the spliceosome. Being able to reliably extract quantitative kinetic and conformational parameters from smFRET experiments is crucial for the interpretation of their results. The need for efficient, unbiased analysis routines becomes more evident as the systems studied become more complex. In this chapter, we focus on the practical utility of statistical algorithms, particularly hidden Markov models, to aid in the objective quantification of complex smFRET trajectories with three or more discrete states, and to extract kinetic information from the trajectories. Additionally, we present a method for systematically eliminating transitions associated with uncorrelated fluorophore behavior that may occur due to dye anisotropy and quenching effects. We also highlight the importance of data condensation through the use of various transition density plots to fully understand the underlying conformational dynamics and kinetic behavior of the biological macromolecule of interest under varying conditions. Finally, the application of these techniques to studies of pre-mRNA conformational changes during eukaryotic splicing is discussed.

Indexed as

AlgorithmsFluorescence Resonance Energy TransferFluorescent DyesImage Processing, Computer-AssistedMarkov ChainsModels, TheoreticalNucleic Acid ConformationRNA, FungalRNA PrecursorsRNA SplicingTime FactorsFluorescent DyesRNA, FungalRNA Precursors

Identifiers

PMID20580964
PMCPMC3012381
OpenAlexW1572086689

What OpenQuestion holds

Textmetadata
LicenceTDM
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.