Evidence map›Paper›PMID 28700912›Full record

ArticleBiophysical journal2017

Quantitative Brightness Analysis of Protein Oligomerization in the Nuclear Envelope.

Jared Hennen, Kwang-Ho Hur, Cosmo A Saunders, G W Gant Luxton, Joachim D Mueller

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2017. 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
2.0field-weighted citation impact, top 13% 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, 26 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Jared HennenSchool of Physics and Astronomy, University of Minnesota, Minneapolis, Minnesota.
Kwang-Ho HurSchool of Physics and Astronomy, University of Minnesota, Minneapolis, Minnesota.
Cosmo A SaundersDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota.
G W Gant LuxtonDepartment of Genetics, Cell Biology, and Development, 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. Electronic address: mueller@physics.umn.edu.
University of Minnesota · US

Funding

TRAINING PROGRAM IN MUSCLE RESEARCHT32AR007612 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI JAMES M ERVASTI, DAWN A LOWE · 2001 to 2026
$11.3M
In vivo Fluorescence Fluctuation Spectroscopy - Administrative SupplementR01GM064589 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI MUELLER, JOACHIM D · 2002 to 2019
$4.6M
NIAMS NIH HHS T32 AR007612NIGMS NIH HHS R01 GM064589
6 · The paper itself

Abstract

Brightness analysis of fluorescence fluctuation experiments has been used to successfully measure the oligomeric state of proteins at the plasma membrane, in the nucleoplasm, and in the cytoplasm of living cells. Here we extend brightness analysis to the nuclear envelope (NE), a double membrane barrier separating the cytoplasm from the nucleoplasm. Results obtained by applying conventional brightness analysis to fluorescently tagged proteins within the NE exhibited an unusual concentration dependence. Similarly, the autocorrelation function of the fluorescence fluctuations exhibited unexpected changes with protein concentration. These observations motivated the application of mean-segmented Q analysis, which identified the existence of a fluctuation process distinct from molecular diffusion in the NE. We propose that small changes in the separation of the inner and outer nuclear membrane are responsible for the additional fluctuation process, as suggested by results obtained for luminal and nuclear membrane-associated EGFP-tagged proteins. Finally, we applied these insights to study the oligomerization of the luminal domains of two nuclear membrane proteins, nesprin-2 and SUN2, which interact transluminally to form a nuclear envelope-spanning linker molecular bridge known as the linker of the nucleoskeleton and cytoskeleton complex.

Indexed as

AlgorithmsBacterial ProteinsCell Line, TumorDermoscopyDiffusionGreen Fluorescent ProteinsHumansIntracellular Signaling Peptides and ProteinsLuminescent ProteinsMembrane ProteinsMicrofilament ProteinsMolecular ImagingNerve Tissue ProteinsNuclear EnvelopeNuclear ProteinsPolymerizationBacterial Proteinsenhanced green fluorescent proteinGreen Fluorescent ProteinsIntracellular Signaling Peptides and ProteinsLuminescent ProteinsMembrane ProteinsMicrofilament ProteinsNerve Tissue ProteinsNuclear ProteinsSUN2 protein, humanSYNE2 protein, humanWateryellow fluorescent protein, Bacteria

Identifiers

PMID28700912
PMCPMC5510813
OpenAlexW2735723450

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.