Evidence map›Paper›PMID 35147933›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

FRET Imaging of Rho GTPase Activity with Red Fluorescent Protein-Based FRET Pairs.

Bryce T Bajar, Xinmeng Guan, Amy Lam, Michael Z Lin, Ryohei Yasuda, Tal Laviv, Jun Chu

Open access · greenAbstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. 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
1.5field-weighted citation impact, top 20% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Review
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 at 5 institutions in 3 countries.

Bryce T Bajar *Department of Biological Chemistry, Medical Scientist Training Program, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA.
Xinmeng Guan *Guangdong Provincial Key Laboratory of Biomedical Optical Imaging Technology & Center for Biomedical Optics and Molecular Imaging, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen, China.
Amy Lam *Departments of Neurobiology and Bioengineering, Stanford University, Stanford, CA, USA.
Michael Z LinDepartments of Neurobiology and Bioengineering, Stanford University, Stanford, CA, USA.
Ryohei YasudaNeuronal Signal Transduction Group, Max Planck Florida Institute for Neuroscience, Jupiter, FL, USA.
Tal LavivNeuronal Signal Transduction Group, Max Planck Florida Institute for Neuroscience, Jupiter, FL, USA. lavivtal@tauex.tau.ac.il.
Jun ChuGuangdong Provincial Key Laboratory of Biomedical Optical Imaging Technology & Center for Biomedical Optics and Molecular Imaging, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen, China. jun.chu@siat.ac.cn.
Shenzhen Institutes of Advanced Technology · CNStanford University · USLos Angeles Medical Center · USMax Planck Florida Institute for Neuroscience · USTel Aviv University · IL

Funding

UCLA-Caltech Medical Scientist Training ProgramT32GM008042 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI AJIJOLA, OLUJIMI A, DAWSON, DAVID WAYNE · 1985 to 2023
$29.9M
Neuronal Intracellular Signaling Underlying Synaptic, Circuit and Behavioral PlasticityR35NS116804 · NINDS · MAX PLANCK FLORIDA CORPORATION · PI Ryohei Yasuda · 2020 to 2026
$7.8M
Mechanisms of Ras Signaling in Single SynapsesR01MH080047 · NIMH · MAX PLANCK FLORIDA CORPORATION · PI YASUDA, RYOHEI · 2007 to 2023
$6.8M
Deciphering Biochemical Networks in Single Dendritic SpinesDP1NS096787 · NINDS · MAX PLANCK FLORIDA CORPORATION · PI YASUDA, RYOHEI · 2015 to 2019
$4.8M
Determining the function and mechanism of spontaneous network activity during synaptogenesis in the Drosophila visual systemF30EY029952 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BAJAR, BRYCE T · 2019 to 2022
$149k
NEI NIH HHS F30 EY029952NIGMS NIH HHS T32 GM008042NIMH NIH HHS R01 MH080047NINDS NIH HHS DP1 NS096787NINDS NIH HHS R35 NS116804
6 · The paper itself

Abstract

With the development of fluorescent proteins (FPs) and advanced optical microscopy techniques, Förster or fluorescence resonance energy transfer (FRET) has become a powerful tool for real-time noninvasive visualization of a variety of biological processes, including kinase activities, with high spatiotemporal resolution in living cells and organisms. FRET can be detected in appropriately configured microscopes as changes in fluorescence intensity, lifetime, and anisotropy. Here, we describe the preparation of samples expressing FP-based FRET sensors for RhoA kinase, intensity- and lifetime-based FRET imaging, and postimaging data analysis.

Indexed as

Fluorescence Resonance Energy Transferrho GTP-Binding ProteinsGreen Fluorescent ProteinsLuminescent ProteinsMicroscopy, FluorescenceRed Fluorescent ProteinGreen Fluorescent ProteinsLuminescent ProteinsRed Fluorescent Proteinrho GTP-Binding ProteinsFLIM-FRETFluorescence lifetimeFluorescent proteinFRETRhoARho GTPaseSensitized emission FRET

Identifiers

PMID35147933
PMCPMC9976416
OpenAlexW4211050763

What OpenQuestion holds

Textmetadata
LicenceTDM
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.