Evidence map›Paper›PMID 24988342›Full record

ArticleBiophysical journal2014

Quantifying protein-protein interactions of peripheral membrane proteins by fluorescence brightness analysis.

Elizabeth M Smith, Patrick J Macdonald, Yan Chen, Joachim D Mueller

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.1field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

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  11. Eph-ephrin signaling modulated by polymerization and condensation of receptors.Proceedings of the National Academy of Sciences of the United States of America · 2017
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Elizabeth M SmithSchool of Physics and Astronomy, University of Minnesota, Minneapolis, Minnesota.
Patrick J MacdonaldDepartment of Biomedical Engineering, University of Minnesota, Minneapolis, Minnesota.
Yan ChenSchool of Physics and Astronomy, University of Minnesota, Minneapolis, Minnesota; Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota.
Joachim D MuellerSchool of Physics and Astronomy, University of Minnesota, Minneapolis, Minnesota; Department of Biomedical Engineering, University of Minnesota, Minneapolis, Minnesota; Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota. Electronic address: mueller@physics.umn.edu.
University of Minnesota · US

Funding

In vivo Fluorescence Fluctuation Spectroscopy - Administrative SupplementR01GM064589 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI MUELLER, JOACHIM D · 2002 to 2019
$4.6M
NIGMS NIH HHS R01 GM064589NIGMS NIH HHS R01GM064589PHS HHS 5T32A1083196
6 · The paper itself

Abstract

Fluorescently labeled proteins that are found both in the cytoplasm and at the plasma membrane, such as peripheral membrane proteins, create stratified fluorescent layers that present a challenging environment for brightness studies with fluorescence fluctuation spectroscopy. The geometry of each layer along with fluorescence and brightness contributions from adjacent layers generates a convoluted raw brightness that conceals the underlying brightness of each individual layer. Because the brightness at a layer establishes the oligomeric state of the fluorescently labeled protein at said layer, we developed a method that connects the experimental raw brightness with the physical brightness at each layered compartment. The technique determines the oligomerization in each compartment from an axial intensity scan through the sample, followed by a fluorescence fluctuation spectroscopy measurement at each layer. We experimentally verify the technique with H-Ras-EGFP as a model system and determine its oligomeric state at both the plasma membrane and in the cytoplasm. Furthermore, we study the oligomerization of the Gag matrix domain of Human T-lymphotropic virus Type 1. The matrix domain targets the Gag polyprotein to the plasma membrane where, subsequently, viral assembly occurs. We determine the oligomerization of matrix in the cytoplasm and observe the onset of protein-protein interactions at the membrane. These observations shed light on the early assembly steps of the retrovirus.

Indexed as

Protein MultimerizationAlgorithmsCell Line, TumorCell MembraneCytoplasmGene Products, gagHumansHuman T-lymphotropic virus 1Microscopy, FluorescenceProtein BindingProtein Structure, Tertiaryras ProteinsGene Products, gagras Proteins

Identifiers

PMID24988342
PMCPMC4119281
OpenAlexW2088860501

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.