ArticleMethods (San Diego, Calif.)2019
Protein oligomerization and mobility within the nuclear envelope evaluated by the time-shifted mean-segmented Q factor.
Article in Methods (San Diego, Calif.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Chromosome movements in meiotic prophase: regulatory mechanisms and biological roles.Frontiers in cell and developmental biology · 2026Review
- Building and breaking mechanical bridges between the nucleus and cytoskeleton: Regulation of LINC complex assembly and disassembly.Current opinion in cell biology · 2023Review
- SUN4 is a spermatid type II inner nuclear membrane protein that forms heteromeric assemblies with SUN3 and interacts with lamin B3.Journal of cell science · 2023Article
- Autocorrelation function of finite-length data in fluorescence correlation spectroscopy.Biophysical journal · 2023Article
- Differentiating Luminal and Membrane-Associated Nuclear Envelope Proteins.Biophysical journal · 2020Article
- Counting the Components of Protein Complexes in the Nuclear Envelope.Biophysical journal · 2020Article
- Time-shifted mean-segmented Q data of a luminal protein measured at the nuclear envelope by fluorescence fluctuation microscopy.Data in brief · 2020Article
- Identifying Heteroprotein Complexes in the Nuclear Envelope.Biophysical journal · 2020Article
- Quantitative modeling of self-oligomerization of proteins in the nuclear envelope by fluorescence fluctuation analysis.Analytical biochemistry · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Analysis of fluorescence fluctuation experiments by the mean-segmented Q (MSQ) method was recently used to successfully characterize the oligomeric state and mobility of proteins within the nuclear envelope (NE) of living cells. However, two significant shortcomings of MSQ were recognized. Non-ideal detector behavior due to dead-time and afterpulsing as well as the lack of error analysis currently limit the potential of MSQ. This paper presents time-shifted MSQ (tsMSQ), a new formulation of MSQ that is robust with respect to dead-time and afterpulsing. In addition, a protocol for performing error analysis on tsMSQ data is introduced to assess the quality of fit models and estimate the uncertainties of fit parameters. Together, these developments significantly simplify and improve the analysis of fluorescence fluctuation data taken within the NE. To demonstrate these new developments, tsMSQ was used to characterize the oligomeric state and mobility of the luminal domains of two inner nuclear membrane SUN proteins. The results for the luminal domain of SUN2 obtained through tsMSQ without correction for non-ideal detector effects agree with a recent study that was conducted using the original MSQ formulation. Finally, tsMSQ was applied to characterize the oligomeric state and mobility of the luminal domain of the germline-restricted SUN3.
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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.