ArticleNature communications2016
Single-point single-molecule FRAP distinguishes inner and outer nuclear membrane protein distribution.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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.
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.
Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- Fluorescence recovery in the super-resolution regime reveals subcompartments of 53BP1 foci.Cell reports methods · 2025Article
- Advanced imaging techniques for studying protein phase separation in living cells and at single-molecule level.Current opinion in chemical biology · 2023Review
- What's past is prologue: FRAP keeps delivering 50 years later.Biophysical journal · 2023Review
- Application of Super-resolution SPEED Microscopy in the Study of Cellular Dynamics.Chemical & biomedical imaging · 2023Review
- Unveiling the complexity: assessing models describing the structure and function of the nuclear pore complex.Frontiers in cell and developmental biology · 2023Review
- A distinct inner nuclear membrane proteome in Saccharomyces cerevisiae gametes.G3 (Bethesda, Md.) · 2021Article
- Article
- Sensing Hydration of Biomimetic Cell Membranes.Biosensors · 2021Article
- Protocol for single-molecule fluorescence recovery after photobleaching microscopy to analyze the dynamics and spatial locations of nuclear transmembrane proteins in live cells.STAR protocols · 2021Article
- Advanced Static and Dynamic Fluorescence Microscopy Techniques to Investigate Drug Delivery Systems.Pharmaceutics · 2021Review
- DeepFRAP: Fast fluorescence recovery after photobleaching data analysis using deep neural networks.Journal of microscopy · 2021Article
- Single-molecule FRET imaging of GPCR dimers in living cells.Nature methods · 2021Article
- High-speed super-resolution imaging of rotationally symmetric structures using SPEED microscopy and 2D-to-3D transformation.Nature protocols · 2021Article
- Nucleoplasmic signals promote directed transmembrane protein import simultaneously via multiple channels of nuclear pores.Nature communications · 2020Article
- Counting the Components of Protein Complexes in the Nuclear Envelope.Biophysical journal · 2020Article
- Casting a Wider Net: Differentiating between Inner Nuclear Envelope and Outer Nuclear Envelope Transmembrane Proteins.International journal of molecular sciences · 2019Review
- Simultaneous Quantification of the Interplay Between Molecular Turnover and Cell Mechanics by AFM-FRAP.Small (Weinheim an der Bergstrasse, Germany) · 2019Article
- Mapping the native organization of the yeast nuclear pore complex using nuclear radial intensity measurements.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Messages from the voices within: regulation of signaling by proteins of the nuclear lamina.Current opinion in cell biology · 2018Review
- Determination of Membrane Protein Distribution on the Nuclear Envelope by Single-Point Single-Molecule FRAP.Current protocols in cell biology · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The normal distribution of nuclear envelope transmembrane proteins (NETs) is disrupted in several human diseases. NETs are synthesized on the endoplasmic reticulum and then transported from the outer nuclear membrane (ONM) to the inner nuclear membrane (INM). Quantitative determination of the distribution of NETs on the ONM and INM is limited in available approaches, which moreover provide no information about translocation rates in the two membranes. Here we demonstrate a single-point single-molecule FRAP microscopy technique that enables determination of distribution and translocation rates for NETs in vivo.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.