Evidence map›Paper›PMID 40252740›Full record

ArticleBiochimica et biophysica acta. General subjects2025

Celebrating 50 years of fluorescence correlation spectroscopy (FCS): Advancing live-cell massively parallel FCS studies with photostable GFPs, mStayGold and StayGold/E138D.

Sho Oasa, Borislav Stoyanov, Yuta Hamada, Stanko N Nikolić, Aleksandar J Krmpot, Akira Kitamura, Vladana Vukojević

Abstract read
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In one paragraph

Article in Biochimica et biophysica acta. General subjects, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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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

1 citing paper in PubMed.

  1. Article
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

7 authors.

Sho OasaDepartment of Clinical Neuroscience, Center for Molecular Medicine, Karolinska Institutet, 17176 Stockholm, Sweden. Electronic address: sho.oasa@ki.se.
Borislav StoyanovSchool of Science, Constructor University, 28759 Bremen, Germany.
Yuta HamadaLaboratory of Cellular and Molecular Sciences, Graduate School of Life Science, Hokkaido University, Sapporo 001-0021, Japan.
Stanko N NikolićDepartment of Clinical Neuroscience, Center for Molecular Medicine, Karolinska Institutet, 17176 Stockholm, Sweden; Institute of Physics Belgrade, University of Belgrade, 11080 Belgrade, Serbia.
Aleksandar J KrmpotDepartment of Clinical Neuroscience, Center for Molecular Medicine, Karolinska Institutet, 17176 Stockholm, Sweden; Institute of Physics Belgrade, University of Belgrade, 11080 Belgrade, Serbia.
Akira KitamuraLaboratory of Cellular and Molecular Sciences, Faculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, Japan.
Vladana VukojevićDepartment of Clinical Neuroscience, Center for Molecular Medicine, Karolinska Institutet, 17176 Stockholm, Sweden. Electronic address: vladana.vukojevic@ki.se.

Funding

Drug targeting the dynamics of opioid systems in alcohol dependenceR01AA028549 · NIAAA · KAROLINSKA INSTITUTE · PI MARTIN-FARDON, REMI, TALISMAN, TIJANA · 2020 to 2024
$2.6M
NIAAA NIH HHS R01 AA028549
6 · The paper itself

Abstract

More than 50 years after its inception, fluorescence correlation spectroscopy (FCS) remains a cornerstone technique for quantitative characterization of the cellular dynamics of molecules and their concentration and interactions in live cells. The enhanced green fluorescent protein (eGFP) has long been a preferred tag in live-cell FCS, valued for its brightness, photostability and lack of posttranslational modifications. However, low eGFP photostability limits measurement durations, posing challenges for studying dynamic cellular processes necessitating longer measurement time. Recent advancements in fluorescent protein engineering have yielded mStayGold and StayGold/E138D, two highly photostable monomeric GFP variants. In this study, we evaluate their performance in live cells and utility for FCS by quantifying glucocorticoid receptor (GR) homodimerization and nuclear import/export dynamics in live cells. Our study shows that both mStayGold and StayGold/E138D exhibit twice the brightness of eGFP, significantly enhancing the signal-to-noise ratio (SNR). Using massively parallel FCS (mpFCS) and two-foci cross-correlation to characterize the direction of GR nucleocytoplasmic transport along the nuclear envelope, we also confirm that these proteins show significantly improved photostability over eGFP.

Indexed as

Green Fluorescent ProteinsReceptors, GlucocorticoidActive Transport, Cell NucleusHEK293 CellsHumansProtein MultimerizationSpectrometry, Fluorescenceenhanced green fluorescent proteinGreen Fluorescent ProteinsReceptors, GlucocorticoidApparent brightness analysisFluorescence correlation spectroscopy (FCS) and massively parallel FCSGlucocorticoid receptorHomodimerizationmStayGoldNucleocytoplasmic transport

Identifiers

PMID40252740
PMCPMC13276660

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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.