Evidence map›Paper›PMID 28188294›Full record

ArticleThe Journal of biological chemistry2017

Understanding the FRET Signatures of Interacting Membrane Proteins.

Christopher King, Valerica Raicu, Kalina Hristova

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

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  16. Interactions between Ligand-Bound EGFR and VEGFR2.Journal of molecular biology · 2021
    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

3 authors.

Christopher Kingthe Program in Molecular Biophysics, Johns Hopkins University, Baltimore, Maryland 21218 and.
Valerica Raicuthe Department of Physics, University of Wisconsin, Milwaukee, Wisconsin 53211.
Kalina Hristovathe Program in Molecular Biophysics, Johns Hopkins University, Baltimore, Maryland 21218 and kh@jhu.edu.

Funding

Seeking the Physical Basis of AchondroplasiaR01GM068619 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2004 to 2022
$5.4M
NIGMS NIH HHS R01 GM068619
6 · The paper itself

Abstract

FRET is an indispensable experimental tool for studying membrane proteins. Currently, two models are available for researchers to determine the oligomerization state of membrane proteins in a static quenching FRET experiment: the model of Veatch and Stryer, derived in 1977, and the kinetic theory-based model for intraoligomeric FRET, derived in 2007. Because of confinement in two dimensions, a substantial amount of FRET is generated by energy transfer between fluorophores located in separate oligomers in the two-dimensional bilayer. This interoligomeric FRET (also known as stochastic, bystander, or proximity FRET) is not accounted for in either model. Here, we use the kinetic theory formalism to describe the dependence of the FRET efficiency measured in an experiment (

Indexed as

Models, ChemicalAnimalsCell MembraneFluorescence Resonance Energy TransferHumansKineticsMembrane ProteinsProtein Interaction MappingProtein MultimerizationMembrane Proteinscell surface receptorfluorescence resonance energy transfer (FRET)mathematical modelingmembrane biophysicsmembrane protein

Identifiers

PMID28188294
PMCPMC5392676

What OpenQuestion holds

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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.