Evidence map›Paper›PMID 21078289›Full record

ArticleAnalytical biochemistry2011

Applications of phasor plots to in vitro protein studies.

Nicholas G James, Justin A Ross, Martin Stefl, David M Jameson

Abstract read
In one paragraph

Article in Analytical biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
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  8. Wide-field time-gated SPAD imager for phasor-based FLIM applications.Methods and applications in fluorescence · 2020
    Article
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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

4 authors.

Nicholas G JamesDepartment of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii, Honolulu, HI 96813, USA.
Justin A Ross
Martin Stefl
David M Jameson

Funding

Dynamin: Ligand Interactions and Conformational DynamicsR01GM076665 · NIGMS · UNIVERSITY OF HAWAII AT MANOA · PI JAMESON, DAVID MICHAEL · 2006 to 2009
$1.2M
NIGMS NIH HHS R01 GM076665NIGMS NIH HHS R01GM076665
6 · The paper itself

Abstract

In a recent article, we described the application of phasor analysis to fluorescence intensity decay data on in vitro samples. As detailed in that article, this method provides researchers with a simple graphical method for viewing lifetime data that can be used to quantify individual components of a mixture as well as to identify excited state reactions. In the current article, we extend the use of in vitro phasor analysis to intrinsic protein fluorescence. We show how alterations in the excited state properties of tryptophan residues are easily visualized using the phasor method. Specifically, we demonstrate that protein-ligand and protein-protein interactions can result in unique shifts in the location of phasor points, indicative of protein conformational changes. Application of the method to a rapid kinetic experiment is also shown. Finally, we show that the unfolding of lysozyme with either urea or guanidine hydrochloride results in different phasor trajectories, indicative of unique denaturation pathways.

Indexed as

Fluorescence Resonance Energy TransferFluorescent DyesHumansHydrogen-Ion ConcentrationKineticsLigandsProtein FoldingProteinsProtein UnfoldingSpectrometry, FluorescenceTemperatureTryptophanFluorescent DyesLigandsProteinsTryptophan

Identifiers

PMID21078289
PMCPMC3021620

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.