Evidence map›Paper›PMID 26587834›Full record

ArticlePloS one2015

Developing Fast Fluorescent Protein Voltage Sensors by Optimizing FRET Interactions.

Uhna Sung, Masoud Sepehri-Rad, Hong Hua Piao, Lei Jin, Thomas Hughes, Lawrence B Cohen, Bradley J Baker

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 35 citations in OpenAlex.

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  10. Genetically Encoded Voltage Indicators.Advances in experimental medicine and biology · 2021
    Review
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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

7 authors at 3 institutions in 2 countries.

Uhna SungCenter for Functional Connectomics, Korea Institute of Science & Technology, Seoul, Korea.
Masoud Sepehri-RadCenter for Functional Connectomics, Korea Institute of Science & Technology, Seoul, Korea.
Hong Hua PiaoCenter for Functional Connectomics, Korea Institute of Science & Technology, Seoul, Korea.
Lei JinDepartment of Molecular and Cellular Physiology, Yale University School of Medicine, New Haven, CT, United States of America.
Thomas HughesDepartment of Cell Biology and Neuroscience, Montana State University, Bozeman, MT, United States of America.
Lawrence B CohenCenter for Functional Connectomics, Korea Institute of Science & Technology, Seoul, Korea.
Bradley J BakerCenter for Functional Connectomics, Korea Institute of Science & Technology, Seoul, Korea.
Korea Institute of Science and Technology · KRYale University · USMontana State University · US

Funding

Optical Studies of Neuron Activity and OrganizationR01DC005259 · NIDCD · YALE UNIVERSITY · PI COHEN, LAWRENCE B · 2002 to 2019
$5.4M
Scan of Protein Space for Optical Voltage ProbesU24NS057631 · NINDS · YALE UNIVERSITY · PI COHEN, LAWRENCE B · 2007 to 2011
$5.2M
Optical Studies of Neuron Activity and OrganizationR56DC005259 · NIDCD · YALE UNIVERSITY · PI COHEN, LAWRENCE B · 2007 to 2007
$413k
NIDCD NIH HHS DC005259NIDCD NIH HHS R01 DC005259NIDCD NIH HHS R56 DC005259NINDS NIH HHS U24 NS057631NINDS NIH HHS U24NS057631
6 · The paper itself

Abstract

FRET (Förster Resonance Energy Transfer)-based protein voltage sensors can be useful for monitoring neuronal activity in vivo because the ratio of signals between the donor and acceptor pair reduces common sources of noise such as heart beat artifacts. We improved the performance of FRET based genetically encoded Fluorescent Protein (FP) voltage sensors by optimizing the location of donor and acceptor FPs flanking the voltage sensitive domain of the Ciona intestinalis voltage sensitive phosphatase. First, we created 39 different "Nabi1" constructs by positioning the donor FP, UKG, at 8 different locations downstream of the voltage-sensing domain and the acceptor FP, mKO, at 6 positions upstream. Several of these combinations resulted in large voltage dependent signals and relatively fast kinetics. Nabi1 probes responded with signal size up to 11% ΔF/F for a 100 mV depolarization and fast response time constants both for signal activation (~2 ms) and signal decay (~3 ms). We improved expression in neuronal cells by replacing the mKO and UKG FRET pair with Clover (donor FP) and mRuby2 (acceptor FP) to create Nabi2 probes. Nabi2 probes also had large signals and relatively fast time constants in HEK293 cells. In primary neuronal culture, a Nabi2 probe was able to differentiate individual action potentials at 45 Hz.

Indexed as

Action PotentialsAnimalsCiona intestinalisFluorescence Resonance Energy TransferGreen Fluorescent ProteinsHEK293 CellsHumansNeuronsPhosphoric Monoester HydrolasesVoltage-Sensitive Dye ImagingGreen Fluorescent ProteinsPhosphoric Monoester Hydrolases

Identifiers

PMID26587834
PMCPMC4654489
OpenAlexW2268934537

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.