Source 1primary paper2020ACS Sensors
Toolkit/Beggiatoa photoactivated adenylyl cyclase
Beggiatoa photoactivated adenylyl cyclase
Also known as: bPAC, light activatable adenylate cyclase, optogenetic analogue of adenylate cyclase, PAC, photoactivatable adenylyl cyclase, photoactivated adenylyl cyclase, photo-activated adenylyl cyclase bPAC, small bacterial photoactivated adenylyl cyclase
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Beggiatoa photoactivated adenylyl cyclase (bPAC) is a blue light-activated optogenetic adenylyl cyclase used to generate cyclic AMP in cells. The cited studies used it to drive cAMP-dependent signaling, including PKA activation, to increase endogenous cortisol in a blue light-dependent manner, and to localize cAMP production to defined subcellular compartments such as the cilium.
Usefulness & Problems
Why this is useful
bPAC provides optical control over intracellular cAMP production, enabling perturbation of cAMP-dependent pathways with spatial targeting and temporal triggering by light. The cited applications include mapping signaling microdomains in cardiac myocytes, monitoring PKA activation, and regulating inflammatory responses in a murine sepsis-associated cardiomyopathy context.
Source:
Beggiatoa photoactivated adenylyl cyclase is described as an optogenetic generator of cyclic AMP. In this paper it is used to activate the PKA pathway for monitoring with Booster-PKA.
Source:
optogenetic generation of cyclic AMP
Source:
driving PKA activation for coupled readout experiments
Problem solved
This tool addresses the need for a controllable actuator that induces cAMP without relying solely on endogenous receptor stimulation. The supplied evidence specifically supports its use for site-specific interrogation of intracellular signaling cascades and for compartmentalized manipulation of cAMP signaling.
Source:
It provides an optogenetic way to induce cyclic AMP and thereby activate PKA in a controlled manner. This makes it useful for testing biosensor compatibility with blue light-responsive optogenetic tools.
Source:
provides blue light-responsive optogenetic control of cyclic AMP production for integration with compatible biosensors
Published Workflows
Objective: Develop a red-shifted genetically encoded FRET biosensor backbone that avoids the multiplexing and blue-light compatibility limitations of CFP/YFP-based biosensors, then demonstrate its utility in vitro and in vivo.
Why it works: The workflow pairs a favorable red-shifted donor/acceptor set selected by Förster distance calculations with biosensor architecture optimization, then tests whether the resulting design retains biosensor performance while reducing spectral conflicts with other FRET sensors and blue-light optogenetic tools.
Förster resonance energy transfer-based reporting of signaling activityspectral separation to enable multiplexed imaging and optogenetic compatibilityFörster distance-based donor/acceptor selectionoptimization of fluorescent protein orderoptimization of modulatory domain arrangementproof-of-concept application testing
Stages
- 1.Donor-acceptor pair selection by Förster distance calculation(in_silico_filter)
This stage identifies a donor/acceptor pair suitable for building a red-shifted FRET biosensor.
Selection: Favorable donor and acceptor pair chosen by calculating the Förster distance.
- 2.Biosensor backbone optimization(library_design)
This stage converts the selected fluorescent protein pair into a working biosensor backbone.
Selection: Optimization of fluorescent protein order and modulatory domains.
- 3.Benchmarking with a PKA biosensor implementation(functional_characterization)
This stage checks whether the red-shifted backbone retains useful biosensor performance after engineering.
Selection: Comparison of Booster-PKA performance to AKAR3EV.
- 4.Proof-of-concept compatibility demonstrations(confirmatory_validation)
This stage confirms that the engineered spectral shift solves the intended compatibility problems in live-cell use cases.
Selection: Demonstration of simultaneous kinase monitoring and compatibility with a blue light-responsive optogenetic tool.
- 5.In vivo tissue imaging in transgenic mice(in_vivo_validation)
This stage validates that the biosensor can function in living tissues in an animal context, extending beyond in vitro demonstrations.
Selection: Presentation of PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Steps
- 1.Calculate Förster distance to choose donor and acceptor fluorescent proteins
Identify a favorable red-shifted donor/acceptor pair for the biosensor.
Pair selection is performed before biosensor backbone optimization because the fluorescent proteins define the core FRET pair used in the design.
- 2.Optimize fluorescent protein order and modulatory domains to build the Booster backboneengineered biosensor backbone
Convert the selected fluorescent protein pair into a functional red-shifted FRET biosensor backbone.
Architecture optimization follows pair selection because the chosen donor and acceptor must be arranged with modulatory domains to create a working biosensor.
- 3.Implement the Booster backbone as a PKA biosensor and compare it with AKAR3EVbiosensor under test and benchmark comparator
Determine whether the engineered red-shifted backbone retains practical biosensor performance.
Benchmarking occurs after backbone construction to verify that the redesigned sensor remains functionally comparable to an established PKA biosensor before broader application claims.
- 4.Test simultaneous monitoring with a CFP/YFP-based ERK FRET biosensorbiosensor under application test
Demonstrate multiplexed kinase activity imaging with a standard CFP/YFP-based FRET biosensor.
This proof-of-concept follows benchmarking because the authors next test whether the red-shifted design solves the intended multiplexing limitation.
- 5.Test monitoring of PKA activation driven by Beggiatoa photoactivated adenylyl cyclasebiosensor-actuator compatibility pair
Demonstrate compatibility of the red-shifted biosensor with a blue light-responsive optogenetic tool.
After showing multiplexed biosensor compatibility, the authors next test the second intended use case: compatibility with blue light-responsive optogenetic control.
- 6.Image PKA activity in living tissues of transgenic mice expressing Booster-PKAbiosensor under in vivo validation
Extend validation from in vitro proof-of-concept experiments to living tissue imaging in an animal model.
In vivo tissue imaging is presented last as a higher-context validation of versatility after in vitro compatibility demonstrations.
Objective: Develop a red-shifted genetically encoded FRET biosensor backbone that avoids the multiplexing and blue-light incompatibility limitations of CFP/YFP-based FRET biosensors, and demonstrate its utility with a PKA biosensor in vitro and in vivo.
Why it works: The workflow first addresses spectral design by selecting a favorable donor-acceptor pair and optimizing biosensor architecture, then tests whether the resulting backbone retains sensing performance while enabling multiplexing and blue-light optogenetic compatibility.
Förster resonance energy transferPKA activity sensingoptogenetic cAMP-driven PKA activationFörster distance-based fluorophore pair selectionoptimization of fluorescent protein orderoptimization of modulatory domain ordercomparative biosensor benchmarkingproof-of-concept application testing
Stages
- 1.Fluorophore pair selection(in_silico_filter)
This stage identifies a donor-acceptor pair suitable for building red-shifted FRET biosensors.
Selection: Calculated Förster distance used to choose a favorable donor and acceptor pair.
- 2.Backbone optimization(library_design)
This stage converts the selected fluorophore pair into a working biosensor backbone.
Selection: Optimization of the order of fluorescent proteins and modulatory domains.
- 3.Comparator performance testing(confirmatory_validation)
This stage checks whether the red-shifted backbone preserves performance relative to an established CFP/YFP PKA biosensor.
Selection: Comparison of Booster-PKA performance to AKAR3EV.
- 4.Multiplexing proof of concept(functional_characterization)
This stage tests whether the red-shifted design enables simultaneous use with standard CFP/YFP biosensors.
Selection: Ability to monitor two protein kinase activities simultaneously with Booster-PKA and a CFP/YFP ERK FRET biosensor.
- 5.Optogenetic compatibility testing(functional_characterization)
This stage tests whether the red-shifted biosensor can operate with a blue-light optogenetic actuator that would conflict with CFP/YFP biosensors.
Selection: Ability to monitor PKA activation driven by Beggiatoa photoactivated adenylyl cyclase.
- 6.In vivo tissue demonstration(in_vivo_validation)
This stage extends validation from in vitro demonstrations to living tissues in transgenic mice.
Selection: Presentation of PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Steps
- 1.Calculate Förster distance to choose donor and acceptor pair
Identify a favorable fluorescent protein pair for a red-shifted FRET biosensor.
Pair selection is done before backbone optimization because the chosen donor and acceptor define the spectral basis of the biosensor.
- 2.Optimize fluorescent protein and modulatory domain order to build Boosterengineered biosensor backbone
Convert the selected fluorophore pair into a functional red-shifted FRET biosensor backbone.
Architecture optimization follows fluorophore selection because domain order must be tuned around the chosen donor-acceptor pair.
- 3.Benchmark Booster-PKA against AKAR3EVbiosensor and comparator
Test whether the red-shifted PKA biosensor preserves performance relative to an established CFP/YFP biosensor.
Comparator benchmarking is performed after backbone construction to confirm that solving spectral compatibility did not compromise sensing performance.
- 4.Test simultaneous kinase monitoring with Booster-PKA and a CFP/YFP ERK biosensorbiosensor under application test
Demonstrate multiplexed monitoring of two kinase activities in the same setting.
This application test follows comparator benchmarking because multiplexing is a key intended advantage once baseline performance is established.
- 5.Monitor PKA activation driven by Beggiatoa photoactivated adenylyl cyclasebiosensor and optogenetic actuator
Demonstrate compatibility of the red-shifted biosensor with a blue-light optogenetic cAMP generator.
This test follows multiplexing proof of concept because blue-light compatibility is another central design goal enabled by spectral red-shifting.
- 6.Present PKA activity in living tissues of transgenic mice expressing Booster-PKAbiosensor under in vivo validation
Demonstrate that the biosensor can report PKA activity in living mouse tissues.
In vivo demonstration is placed after in vitro proof-of-concept tests as a higher-fidelity validation of practical imaging utility.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
enzymatic cyclic amp productionphotoactivationpka pathway activationsubcellular localization targetingTechniques
No technique tags yet.
Target processes
localizationrecombinationsignalingInput: Light
Implementation Constraints
The tool requires light stimulation and is described as blue light-dependent in at least one cited application. Evidence supports use through domain fusion or targeting constructs for subcellular localization, including localization to the cilium, and some experiments paired bPAC with downstream readouts such as a PKA biosensor or with LED-based illumination systems.
The supplied evidence does not provide quantitative performance metrics such as dynamic range, kinetics, dark activity, or wavelength-response curves. It also does not establish that bPAC itself is a reporter, and independent replication of specific performance characteristics is not documented in the provided material.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Observations
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c1 during normalization. In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane. Derived from claim c1. Quoted text: Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c2 during normalization. In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition. Derived from claim c2. Quoted text: Reporters with nuclear localization do not show this phosphorylation.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c4 during normalization. Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades. Derived from claim c4. Quoted text: We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Source:
successMammalian Cell Lineapplication demomacrophages
cytokine expression
Inferred from claim c1 during normalization. Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels. Derived from claim c1. Quoted text: blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Source:
successMouseapplication demomousecardiac
LPS-induced sepsis model
Inferred from claim c2 during normalization. The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction. Derived from claim c2. Quoted text: with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c1 during normalization. In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane. Derived from claim c1. Quoted text: Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c2 during normalization. In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition. Derived from claim c2. Quoted text: Reporters with nuclear localization do not show this phosphorylation.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c4 during normalization. Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades. Derived from claim c4. Quoted text: We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Source:
successMammalian Cell Lineapplication demomacrophages
cytokine expression
Inferred from claim c1 during normalization. Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels. Derived from claim c1. Quoted text: blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Source:
successMouseapplication demomousecardiac
LPS-induced sepsis model
Inferred from claim c2 during normalization. The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction. Derived from claim c2. Quoted text: with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c2 during normalization. In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition. Derived from claim c2. Quoted text: Reporters with nuclear localization do not show this phosphorylation.
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c1 during normalization. In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane. Derived from claim c1. Quoted text: Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c4 during normalization. Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades. Derived from claim c4. Quoted text: We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Source:
successMammalian Cell Lineapplication demomacrophages
cytokine expression
Inferred from claim c1 during normalization. Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels. Derived from claim c1. Quoted text: blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Source:
successMouseapplication demomousecardiac
LPS-induced sepsis model
Inferred from claim c2 during normalization. The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction. Derived from claim c2. Quoted text: with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c1 during normalization. In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane. Derived from claim c1. Quoted text: Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c2 during normalization. In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition. Derived from claim c2. Quoted text: Reporters with nuclear localization do not show this phosphorylation.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c4 during normalization. Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades. Derived from claim c4. Quoted text: We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Source:
successMammalian Cell Lineapplication demomacrophages
cytokine expression
Inferred from claim c1 during normalization. Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels. Derived from claim c1. Quoted text: blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Source:
successMouseapplication demomousecardiac
LPS-induced sepsis model
Inferred from claim c2 during normalization. The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction. Derived from claim c2. Quoted text: with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c1 during normalization. In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane. Derived from claim c1. Quoted text: Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c2 during normalization. In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition. Derived from claim c2. Quoted text: Reporters with nuclear localization do not show this phosphorylation.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c4 during normalization. Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades. Derived from claim c4. Quoted text: We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Source:
successMammalian Cell Lineapplication demomacrophages
cytokine expression
Inferred from claim c1 during normalization. Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels. Derived from claim c1. Quoted text: blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Source:
successMouseapplication demomousecardiac
LPS-induced sepsis model
Inferred from claim c2 during normalization. The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction. Derived from claim c2. Quoted text: with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c1 during normalization. In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane. Derived from claim c1. Quoted text: Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c2 during normalization. In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition. Derived from claim c2. Quoted text: Reporters with nuclear localization do not show this phosphorylation.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c4 during normalization. Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades. Derived from claim c4. Quoted text: We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Source:
successMammalian Cell Lineapplication demomacrophages
cytokine expression
Inferred from claim c1 during normalization. Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels. Derived from claim c1. Quoted text: blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Source:
successMouseapplication demomousecardiac
LPS-induced sepsis model
Inferred from claim c2 during normalization. The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction. Derived from claim c2. Quoted text: with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c2 during normalization. In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition. Derived from claim c2. Quoted text: Reporters with nuclear localization do not show this phosphorylation.
Source:
successMammalian Cell Lineapplication demoH9c2
PKA reporter phosphorylation
Inferred from claim c1 during normalization. In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane. Derived from claim c1. Quoted text: Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c4 during normalization. Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades. Derived from claim c4. Quoted text: We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Source:
successMammalian Cell Lineapplication demomacrophages
cytokine expression
Inferred from claim c1 during normalization. Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels. Derived from claim c1. Quoted text: blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Source:
successMouseapplication demomousecardiac
LPS-induced sepsis model
Inferred from claim c2 during normalization. The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction. Derived from claim c2. Quoted text: with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
Source:
Supporting Sources
Source 2primary paper2015Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE
Source 3primary paper2022The FASEB Journal
Source 4primary paper2020eLife
Source 5review2017Trends in biotechnology
Source 6primary paper2022Frontiers in Immunology
Source 7primary paper2017Scientific Reports
Source 8primary paper2015Endocrinology
Source 9primary paper2010Journal of Biological Chemistry
Ranked Claims
Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades.
We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades.
We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades.
We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades.
We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades.
We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades.
We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades.
We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction.
with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction.
with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction.
with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction.
with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction.
with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction.
with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction.
with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
A light directed PKA optogenetic switch analog can direct PKA activity and retention to specific intracellular subdomains in cardiac cells.
The expression and recruitment are confirmed with live cell microscopy and demonstrate a unique ability to direct PKA activity and retention to specific intracellular subdomains.
A light directed PKA optogenetic switch analog can direct PKA activity and retention to specific intracellular subdomains in cardiac cells.
The expression and recruitment are confirmed with live cell microscopy and demonstrate a unique ability to direct PKA activity and retention to specific intracellular subdomains.
A light directed PKA optogenetic switch analog can direct PKA activity and retention to specific intracellular subdomains in cardiac cells.
The expression and recruitment are confirmed with live cell microscopy and demonstrate a unique ability to direct PKA activity and retention to specific intracellular subdomains.
A light directed PKA optogenetic switch analog can direct PKA activity and retention to specific intracellular subdomains in cardiac cells.
The expression and recruitment are confirmed with live cell microscopy and demonstrate a unique ability to direct PKA activity and retention to specific intracellular subdomains.
A light directed PKA optogenetic switch analog can direct PKA activity and retention to specific intracellular subdomains in cardiac cells.
The expression and recruitment are confirmed with live cell microscopy and demonstrate a unique ability to direct PKA activity and retention to specific intracellular subdomains.
A light directed PKA optogenetic switch analog can direct PKA activity and retention to specific intracellular subdomains in cardiac cells.
The expression and recruitment are confirmed with live cell microscopy and demonstrate a unique ability to direct PKA activity and retention to specific intracellular subdomains.
A light directed PKA optogenetic switch analog can direct PKA activity and retention to specific intracellular subdomains in cardiac cells.
The expression and recruitment are confirmed with live cell microscopy and demonstrate a unique ability to direct PKA activity and retention to specific intracellular subdomains.
Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels.
blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels.
blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels.
blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels.
blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels.
blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels.
blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels.
blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane.
Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane.
Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane.
Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane.
Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane.
Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane.
Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane.
Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition.
Reporters with nuclear localization do not show this phosphorylation.
In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition.
Reporters with nuclear localization do not show this phosphorylation.
In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition.
Reporters with nuclear localization do not show this phosphorylation.
In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition.
Reporters with nuclear localization do not show this phosphorylation.
In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition.
Reporters with nuclear localization do not show this phosphorylation.
In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition.
Reporters with nuclear localization do not show this phosphorylation.
In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition.
Reporters with nuclear localization do not show this phosphorylation.
Photo-activated regulation of macrophage function may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases.
our study may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases by photo-activated regulating macrophage function
Photo-activated regulation of macrophage function may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases.
our study may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases by photo-activated regulating macrophage function
Photo-activated regulation of macrophage function may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases.
our study may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases by photo-activated regulating macrophage function
Photo-activated regulation of macrophage function may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases.
our study may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases by photo-activated regulating macrophage function
Photo-activated regulation of macrophage function may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases.
our study may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases by photo-activated regulating macrophage function
Photo-activated regulation of macrophage function may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases.
our study may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases by photo-activated regulating macrophage function
Photo-activated regulation of macrophage function may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases.
our study may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases by photo-activated regulating macrophage function
The nanobody-based targeting approach overcomes loss of protein function observed after fusion to ciliary targeting sequences.
Thereby, we overcome the loss of protein function observed after fusion to ciliary targeting sequences.
The nanobody-based targeting approach overcomes loss of protein function observed after fusion to ciliary targeting sequences.
Thereby, we overcome the loss of protein function observed after fusion to ciliary targeting sequences.
The nanobody-based targeting approach overcomes loss of protein function observed after fusion to ciliary targeting sequences.
Thereby, we overcome the loss of protein function observed after fusion to ciliary targeting sequences.
The nanobody-based targeting approach overcomes loss of protein function observed after fusion to ciliary targeting sequences.
Thereby, we overcome the loss of protein function observed after fusion to ciliary targeting sequences.
The nanobody-based targeting approach overcomes loss of protein function observed after fusion to ciliary targeting sequences.
Thereby, we overcome the loss of protein function observed after fusion to ciliary targeting sequences.
The nanobody-based targeting approach overcomes loss of protein function observed after fusion to ciliary targeting sequences.
Thereby, we overcome the loss of protein function observed after fusion to ciliary targeting sequences.
The nanobody-based targeting approach overcomes loss of protein function observed after fusion to ciliary targeting sequences.
Thereby, we overcome the loss of protein function observed after fusion to ciliary targeting sequences.
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor activities of two protein kinases.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor activities of two protein kinases.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor activities of two protein kinases.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor activities of two protein kinases.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor activities of two protein kinases.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor activities of two protein kinases.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor activities of two protein kinases.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor activities of two protein kinases.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA enabled simultaneous monitoring of two protein kinase activities together with a CFP/YFP-based ERK FRET biosensor.
For the proof of concept, we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP.
Using the nanobody-based targeting approach, the authors studied the contribution of spatial cAMP signaling in controlling cilia length.
Using this approach, we studied the contribution of spatial cAMP signaling in controlling cilia length.
Using the nanobody-based targeting approach, the authors studied the contribution of spatial cAMP signaling in controlling cilia length.
Using this approach, we studied the contribution of spatial cAMP signaling in controlling cilia length.
Using the nanobody-based targeting approach, the authors studied the contribution of spatial cAMP signaling in controlling cilia length.
Using this approach, we studied the contribution of spatial cAMP signaling in controlling cilia length.
Using the nanobody-based targeting approach, the authors studied the contribution of spatial cAMP signaling in controlling cilia length.
Using this approach, we studied the contribution of spatial cAMP signaling in controlling cilia length.
Using the nanobody-based targeting approach, the authors studied the contribution of spatial cAMP signaling in controlling cilia length.
Using this approach, we studied the contribution of spatial cAMP signaling in controlling cilia length.
Using the nanobody-based targeting approach, the authors studied the contribution of spatial cAMP signaling in controlling cilia length.
Using this approach, we studied the contribution of spatial cAMP signaling in controlling cilia length.
Using the nanobody-based targeting approach, the authors studied the contribution of spatial cAMP signaling in controlling cilia length.
Using this approach, we studied the contribution of spatial cAMP signaling in controlling cilia length.
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV
Booster-PKA performance was comparable to that of AKAR3EV.
The performance of the protein kinase A (PKA) biosensor based on the Booster backbone (Booster-PKA) was comparable to that of AKAR3EV, a previously developed FRET biosensor comprising CFP and YFP.
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor two protein kinase activities.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor two protein kinase activities.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor two protein kinase activities.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor two protein kinase activities.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor two protein kinase activities.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor two protein kinase activities.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA can be used simultaneously with a CFP/YFP-based ERK FRET biosensor to monitor two protein kinase activities.
we first showed simultaneous monitoring of activities of two protein kinases with Booster-PKA and ERK FRET biosensors based on CFP and YFP
Booster-PKA enabled monitoring of PKA activation driven by Beggiatoa photoactivated adenylyl cyclase.
we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP
Booster-PKA enabled monitoring of PKA activation driven by Beggiatoa photoactivated adenylyl cyclase.
we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP
Booster-PKA enabled monitoring of PKA activation driven by Beggiatoa photoactivated adenylyl cyclase.
we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP
Booster-PKA enabled monitoring of PKA activation driven by Beggiatoa photoactivated adenylyl cyclase.
we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP
Booster-PKA enabled monitoring of PKA activation driven by Beggiatoa photoactivated adenylyl cyclase.
we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP
Booster-PKA enabled monitoring of PKA activation driven by Beggiatoa photoactivated adenylyl cyclase.
we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP
Booster-PKA enabled monitoring of PKA activation driven by Beggiatoa photoactivated adenylyl cyclase.
we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP
Booster-PKA is compatible with blue-light optogenetic activation of cAMP signaling using Beggiatoa photoactivated adenylyl cyclase.
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
Booster-PKA is compatible with blue-light optogenetic activation of cAMP signaling using Beggiatoa photoactivated adenylyl cyclase.
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
Booster-PKA is compatible with blue-light optogenetic activation of cAMP signaling using Beggiatoa photoactivated adenylyl cyclase.
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
Booster-PKA is compatible with blue-light optogenetic activation of cAMP signaling using Beggiatoa photoactivated adenylyl cyclase.
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
Booster-PKA is compatible with blue-light optogenetic activation of cAMP signaling using Beggiatoa photoactivated adenylyl cyclase.
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
Booster-PKA is compatible with blue-light optogenetic activation of cAMP signaling using Beggiatoa photoactivated adenylyl cyclase.
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
Booster-PKA is compatible with blue-light optogenetic activation of cAMP signaling using Beggiatoa photoactivated adenylyl cyclase.
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
Booster-PKA is compatible with blue-light optogenetic activation of cAMP signaling using Beggiatoa photoactivated adenylyl cyclase.
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
Booster-PKA was used to monitor PKA activation driven by Beggiatoa photoactivated adenylyl cyclase.
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
The Booster design selected mKOκ and mKate2 as the donor and acceptor pair based on calculated Förster distance.
We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance.
The Booster design selected mKOκ and mKate2 as the donor and acceptor pair based on calculated Förster distance.
We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance.
The Booster design selected mKOκ and mKate2 as the donor and acceptor pair based on calculated Förster distance.
We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance.
The Booster design selected mKOκ and mKate2 as the donor and acceptor pair based on calculated Förster distance.
We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance.
The Booster design selected mKOκ and mKate2 as the donor and acceptor pair based on calculated Förster distance.
We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance.
The Booster design selected mKOκ and mKate2 as the donor and acceptor pair based on calculated Förster distance.
We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance.
The Booster design selected mKOκ and mKate2 as the donor and acceptor pair based on calculated Förster distance.
We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance.
The Booster design selected mKOκ and mKate2 as the donor and acceptor pair based on calculated Förster distance.
We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance.
Booster is a red-shifted genetically encoded FRET biosensor backbone developed to overcome limitations of CFP/YFP-based FRET biosensors for multiplexing and blue-light optogenetic compatibility.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths... we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed to overcome limitations of CFP/YFP-based FRET biosensors for multiplexing and blue-light optogenetic compatibility.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths... we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed to overcome limitations of CFP/YFP-based FRET biosensors for multiplexing and blue-light optogenetic compatibility.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths... we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed to overcome limitations of CFP/YFP-based FRET biosensors for multiplexing and blue-light optogenetic compatibility.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths... we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed to overcome limitations of CFP/YFP-based FRET biosensors for multiplexing and blue-light optogenetic compatibility.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths... we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed to overcome limitations of CFP/YFP-based FRET biosensors for multiplexing and blue-light optogenetic compatibility.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths... we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed to overcome limitations of CFP/YFP-based FRET biosensors for multiplexing and blue-light optogenetic compatibility.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths... we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed to overcome limitations of CFP/YFP-based FRET biosensors for multiplexing and blue-light optogenetic compatibility.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths... we developed a FRET biosensor backbone named "Booster".
The authors developed red-shifted FRET biosensors and a biosensor backbone named Booster by choosing mKOκ and mKate2 and optimizing fluorescent protein order and modulatory domains.
We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance. By optimizing the order of fluorescent proteins and modulatory domains of the FRET biosensors, we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed by optimizing fluorescent protein order and modulatory domains.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths. We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance. By optimizing the order of fluorescent proteins and modulatory domains of the FRET biosensors, we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed by optimizing fluorescent protein order and modulatory domains.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths. We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance. By optimizing the order of fluorescent proteins and modulatory domains of the FRET biosensors, we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed by optimizing fluorescent protein order and modulatory domains.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths. We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance. By optimizing the order of fluorescent proteins and modulatory domains of the FRET biosensors, we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed by optimizing fluorescent protein order and modulatory domains.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths. We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance. By optimizing the order of fluorescent proteins and modulatory domains of the FRET biosensors, we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed by optimizing fluorescent protein order and modulatory domains.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths. We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance. By optimizing the order of fluorescent proteins and modulatory domains of the FRET biosensors, we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed by optimizing fluorescent protein order and modulatory domains.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths. We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance. By optimizing the order of fluorescent proteins and modulatory domains of the FRET biosensors, we developed a FRET biosensor backbone named "Booster".
Booster is a red-shifted genetically encoded FRET biosensor backbone developed by optimizing fluorescent protein order and modulatory domains.
To overcome these problems, here, we have developed FRET biosensors with red-shifted excitation and emission wavelengths. We chose mKOκ and mKate2 as the favorable donor and acceptor pair by calculating the Förster distance. By optimizing the order of fluorescent proteins and modulatory domains of the FRET biosensors, we developed a FRET biosensor backbone named "Booster".
Booster-PKA was used to present PKA activity in living tissues of transgenic mice.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Booster-PKA was used to present PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Finally, we presented PKA activity in living tissues of transgenic mice expressing Booster-PKA.
Using the nanobody-based targeting approach, bPAC, LAPD, and mlCNBD-FRET were functionally localized to the cilium.
We functionally localized modifiers of cAMP signaling, the photo-activated adenylyl cyclase bPAC and the light-activated phosphodiesterase LAPD, and the cAMP biosensor mlCNBD-FRET to the cilium.
Using the nanobody-based targeting approach, bPAC, LAPD, and mlCNBD-FRET were functionally localized to the cilium.
We functionally localized modifiers of cAMP signaling, the photo-activated adenylyl cyclase bPAC and the light-activated phosphodiesterase LAPD, and the cAMP biosensor mlCNBD-FRET to the cilium.
Using the nanobody-based targeting approach, bPAC, LAPD, and mlCNBD-FRET were functionally localized to the cilium.
We functionally localized modifiers of cAMP signaling, the photo-activated adenylyl cyclase bPAC and the light-activated phosphodiesterase LAPD, and the cAMP biosensor mlCNBD-FRET to the cilium.
Using the nanobody-based targeting approach, bPAC, LAPD, and mlCNBD-FRET were functionally localized to the cilium.
We functionally localized modifiers of cAMP signaling, the photo-activated adenylyl cyclase bPAC and the light-activated phosphodiesterase LAPD, and the cAMP biosensor mlCNBD-FRET to the cilium.
Using the nanobody-based targeting approach, bPAC, LAPD, and mlCNBD-FRET were functionally localized to the cilium.
We functionally localized modifiers of cAMP signaling, the photo-activated adenylyl cyclase bPAC and the light-activated phosphodiesterase LAPD, and the cAMP biosensor mlCNBD-FRET to the cilium.
Using the nanobody-based targeting approach, bPAC, LAPD, and mlCNBD-FRET were functionally localized to the cilium.
We functionally localized modifiers of cAMP signaling, the photo-activated adenylyl cyclase bPAC and the light-activated phosphodiesterase LAPD, and the cAMP biosensor mlCNBD-FRET to the cilium.
Using the nanobody-based targeting approach, bPAC, LAPD, and mlCNBD-FRET were functionally localized to the cilium.
We functionally localized modifiers of cAMP signaling, the photo-activated adenylyl cyclase bPAC and the light-activated phosphodiesterase LAPD, and the cAMP biosensor mlCNBD-FRET to the cilium.
The paper describes a nanobody-based targeting approach for optogenetic tools to specifically analyze ciliary signaling and function.
Here, we describe a nanobody-based targeting approach for optogenetic tools in mammalian cells and in vivo in zebrafish to specifically analyze ciliary signaling and function.
The paper describes a nanobody-based targeting approach for optogenetic tools to specifically analyze ciliary signaling and function.
Here, we describe a nanobody-based targeting approach for optogenetic tools in mammalian cells and in vivo in zebrafish to specifically analyze ciliary signaling and function.
The paper describes a nanobody-based targeting approach for optogenetic tools to specifically analyze ciliary signaling and function.
Here, we describe a nanobody-based targeting approach for optogenetic tools in mammalian cells and in vivo in zebrafish to specifically analyze ciliary signaling and function.
The paper describes a nanobody-based targeting approach for optogenetic tools to specifically analyze ciliary signaling and function.
Here, we describe a nanobody-based targeting approach for optogenetic tools in mammalian cells and in vivo in zebrafish to specifically analyze ciliary signaling and function.
The paper describes a nanobody-based targeting approach for optogenetic tools to specifically analyze ciliary signaling and function.
Here, we describe a nanobody-based targeting approach for optogenetic tools in mammalian cells and in vivo in zebrafish to specifically analyze ciliary signaling and function.
The paper describes a nanobody-based targeting approach for optogenetic tools to specifically analyze ciliary signaling and function.
Here, we describe a nanobody-based targeting approach for optogenetic tools in mammalian cells and in vivo in zebrafish to specifically analyze ciliary signaling and function.
The paper describes a nanobody-based targeting approach for optogenetic tools to specifically analyze ciliary signaling and function.
Here, we describe a nanobody-based targeting approach for optogenetic tools in mammalian cells and in vivo in zebrafish to specifically analyze ciliary signaling and function.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
Booster biosensors are effective and versatile imaging tools in vitro and in vivo.
Collectively, the results demonstrate the effectiveness and versatility of Booster biosensors as an imaging tool in vitro and in vivo.
The review discusses bPAC as an optogenetic tool for cAMP control.
The review discusses iGluSnFR as a neurotransmitter reporter relevant to synaptic function assays.
The review discusses optoXRs as optogenetic tools for GPCR signaling in discovery-oriented applications.
bPAC expression and activation increase cAMP and insulin secretion in murine islets and β-cell pseudoislets, with pseudoislets showing more pronounced light-triggered hormone secretion than β-cell monolayers.
Furthermore, the expression and activation of bPAC increased cAMP and insulin secretion in murine islets and in β-cell pseudoislets, which displayed a more pronounced light-triggered hormone secretion compared to that of β-cell monolayers.
The review describes Optopatch as pairing CheRiff with QuasAr voltage indicators.
Light activation of Beggiatoa photoactivatable adenylyl cyclase in pancreatic β-cells increases intracellular cAMP and enhances insulin secretion.
A cAMP increase was noted within 5 minutes of photostimulation and a significant drop at 12 minutes post-illumination. The concomitant augmented insulin secretion was comparable to that from β-cells treated with secretagogues.
cAMP drop timing 12 minutescAMP increase timing within 5 minutes
Calcium channel blocking reduces the enhanced insulin response produced by bPAC activity.
Calcium channel blocking curtailed the enhanced insulin response due to bPAC activity.
This review centers optogenetic and all-optical electrophysiology approaches for phenotypic screening in drug discovery.
Repeated cycles of bPAC photoinduction produce greater insulin release without adverse effects on viability and proliferation.
Greater insulin release was also observed over repeated cycles of photoinduction without adverse effects on viability and proliferation.
Optical modulation for optogenetic assays can be obtained in a miniaturized 384-well plate format using the FLIPR instrument.
we sought to determine if this optical modulation can be obtained also in a miniaturized format, such as a 384-well plate, using the instrumentations normally dedicated to fluorescence analysis in High Throughput Screening (HTS) activities, such as for example the FLIPR (Fluorometric Imaging Plate Reader) instrument
plate format 384-well
Optical modulation for optogenetic assays can be obtained in a miniaturized 384-well plate format using the FLIPR instrument.
we sought to determine if this optical modulation can be obtained also in a miniaturized format, such as a 384-well plate, using the instrumentations normally dedicated to fluorescence analysis in High Throughput Screening (HTS) activities, such as for example the FLIPR (Fluorometric Imaging Plate Reader) instrument
plate format 384-well
Optical modulation for optogenetic assays can be obtained in a miniaturized 384-well plate format using the FLIPR instrument.
we sought to determine if this optical modulation can be obtained also in a miniaturized format, such as a 384-well plate, using the instrumentations normally dedicated to fluorescence analysis in High Throughput Screening (HTS) activities, such as for example the FLIPR (Fluorometric Imaging Plate Reader) instrument
plate format 384-well
Optical modulation for optogenetic assays can be obtained in a miniaturized 384-well plate format using the FLIPR instrument.
we sought to determine if this optical modulation can be obtained also in a miniaturized format, such as a 384-well plate, using the instrumentations normally dedicated to fluorescence analysis in High Throughput Screening (HTS) activities, such as for example the FLIPR (Fluorometric Imaging Plate Reader) instrument
plate format 384-well
Optical modulation for optogenetic assays can be obtained in a miniaturized 384-well plate format using the FLIPR instrument.
we sought to determine if this optical modulation can be obtained also in a miniaturized format, such as a 384-well plate, using the instrumentations normally dedicated to fluorescence analysis in High Throughput Screening (HTS) activities, such as for example the FLIPR (Fluorometric Imaging Plate Reader) instrument
plate format 384-well
Optical modulation for optogenetic assays can be obtained in a miniaturized 384-well plate format using the FLIPR instrument.
we sought to determine if this optical modulation can be obtained also in a miniaturized format, such as a 384-well plate, using the instrumentations normally dedicated to fluorescence analysis in High Throughput Screening (HTS) activities, such as for example the FLIPR (Fluorometric Imaging Plate Reader) instrument
plate format 384-well
Optical modulation for optogenetic assays can be obtained in a miniaturized 384-well plate format using the FLIPR instrument.
we sought to determine if this optical modulation can be obtained also in a miniaturized format, such as a 384-well plate, using the instrumentations normally dedicated to fluorescence analysis in High Throughput Screening (HTS) activities, such as for example the FLIPR (Fluorometric Imaging Plate Reader) instrument
plate format 384-well
The reported approach enables specific manipulation of steroidogenic interrenal cell activity for studying both hypo- and hypercortisolemia in zebrafish.
Thus, our approach allows specific manipulations of steroidogenic interrenal cell activity for studying the effects of both hypo- and hypercortisolemia in zebrafish.
Stable, robust, and miniaturized cellular assays can be developed using different optogenetic tools and modulated by FLIPR LEDs in a 384-well format.
stable, robust and miniaturized cellular assays can be developed using different optogenetic tools, and efficiently modulated by the FLIPR instrument LEDs in a 384-well format
plate format 384-well
Stable, robust, and miniaturized cellular assays can be developed using different optogenetic tools and modulated by FLIPR LEDs in a 384-well format.
stable, robust and miniaturized cellular assays can be developed using different optogenetic tools, and efficiently modulated by the FLIPR instrument LEDs in a 384-well format
plate format 384-well
Stable, robust, and miniaturized cellular assays can be developed using different optogenetic tools and modulated by FLIPR LEDs in a 384-well format.
stable, robust and miniaturized cellular assays can be developed using different optogenetic tools, and efficiently modulated by the FLIPR instrument LEDs in a 384-well format
plate format 384-well
Stable, robust, and miniaturized cellular assays can be developed using different optogenetic tools and modulated by FLIPR LEDs in a 384-well format.
stable, robust and miniaturized cellular assays can be developed using different optogenetic tools, and efficiently modulated by the FLIPR instrument LEDs in a 384-well format
plate format 384-well
Stable, robust, and miniaturized cellular assays can be developed using different optogenetic tools and modulated by FLIPR LEDs in a 384-well format.
stable, robust and miniaturized cellular assays can be developed using different optogenetic tools, and efficiently modulated by the FLIPR instrument LEDs in a 384-well format
plate format 384-well
Stable, robust, and miniaturized cellular assays can be developed using different optogenetic tools and modulated by FLIPR LEDs in a 384-well format.
stable, robust and miniaturized cellular assays can be developed using different optogenetic tools, and efficiently modulated by the FLIPR instrument LEDs in a 384-well format
plate format 384-well
Stable, robust, and miniaturized cellular assays can be developed using different optogenetic tools and modulated by FLIPR LEDs in a 384-well format.
stable, robust and miniaturized cellular assays can be developed using different optogenetic tools, and efficiently modulated by the FLIPR instrument LEDs in a 384-well format
plate format 384-well
bPAC adenylyl cyclase was used to modulate the HCN2 cyclic nucleotide gated channel in an optogenetic assay.
the HCN2 cyclic nucleotide gated (CNG) channel was modulated by the light activated bPAC adenylyl cyclase
bPAC adenylyl cyclase was used to modulate the HCN2 cyclic nucleotide gated channel in an optogenetic assay.
the HCN2 cyclic nucleotide gated (CNG) channel was modulated by the light activated bPAC adenylyl cyclase
bPAC adenylyl cyclase was used to modulate the HCN2 cyclic nucleotide gated channel in an optogenetic assay.
the HCN2 cyclic nucleotide gated (CNG) channel was modulated by the light activated bPAC adenylyl cyclase
bPAC adenylyl cyclase was used to modulate the HCN2 cyclic nucleotide gated channel in an optogenetic assay.
the HCN2 cyclic nucleotide gated (CNG) channel was modulated by the light activated bPAC adenylyl cyclase
bPAC adenylyl cyclase was used to modulate the HCN2 cyclic nucleotide gated channel in an optogenetic assay.
the HCN2 cyclic nucleotide gated (CNG) channel was modulated by the light activated bPAC adenylyl cyclase
bPAC adenylyl cyclase was used to modulate the HCN2 cyclic nucleotide gated channel in an optogenetic assay.
the HCN2 cyclic nucleotide gated (CNG) channel was modulated by the light activated bPAC adenylyl cyclase
bPAC adenylyl cyclase was used to modulate the HCN2 cyclic nucleotide gated channel in an optogenetic assay.
the HCN2 cyclic nucleotide gated (CNG) channel was modulated by the light activated bPAC adenylyl cyclase
Channelrhodopsin-2 was used to modulate the CaV1.3 calcium channel in an optogenetic assay.
the CaV1.3 calcium channel was modulated by the light-activated Channelrhodopsin-2
Channelrhodopsin-2 was used to modulate the CaV1.3 calcium channel in an optogenetic assay.
the CaV1.3 calcium channel was modulated by the light-activated Channelrhodopsin-2
Channelrhodopsin-2 was used to modulate the CaV1.3 calcium channel in an optogenetic assay.
the CaV1.3 calcium channel was modulated by the light-activated Channelrhodopsin-2
Channelrhodopsin-2 was used to modulate the CaV1.3 calcium channel in an optogenetic assay.
the CaV1.3 calcium channel was modulated by the light-activated Channelrhodopsin-2
Channelrhodopsin-2 was used to modulate the CaV1.3 calcium channel in an optogenetic assay.
the CaV1.3 calcium channel was modulated by the light-activated Channelrhodopsin-2
Channelrhodopsin-2 was used to modulate the CaV1.3 calcium channel in an optogenetic assay.
the CaV1.3 calcium channel was modulated by the light-activated Channelrhodopsin-2
Beggiatoa photoactivated adenylyl cyclase targeted to interrenal cells increases endogenous cortisol concentrations in a blue light-dependent manner.
Next, we coupled this regulatory region to an optogenetic actuator, Beggiatoa photoactivated adenylyl cyclase, to increase endogenous cortisol concentrations in a blue light-dependent manner.
bPAC is a light-activated adenylyl cyclase with low activity in darkness and strongly increased activity in light.
this photoactivated adenylyl cyclase (bPAC) showed cyclase activity that is low in darkness but increased 300-fold in the light
fold increase in cyclase activity in light 300 fold
bPAC is well expressed in pyramidal neurons and, together with cyclic nucleotide gated channels, enables efficient light-induced depolarization.
bPAC is well expressed in pyramidal neurons and, in combination with cyclic nucleotide gated channels, causes efficient light-induced depolarization
In the Drosophila central nervous system, bPAC mediates light-dependent cAMP increase and behavioral changes in freely moving animals.
In the Drosophila central nervous system, bPAC mediates light-dependent cAMP increase and behavioral changes in freely moving animals
The light-activated enzymatic activity of bPAC decays thermally within 20 seconds in parallel with the red-shifted BLUF photointermediate.
This enzymatic activity decays thermally within 20 s in parallel with the red-shifted BLUF photointermediate
thermal decay time 20 s
bPAC is presented as an optogenetic tool for light modulation of cAMP in neuronal cells and tissues and for studying cAMP-dependent processes in live animals.
bPAC seems a perfect optogenetic tool for light modulation of cAMP in neuronal cells and tissues and for studying cAMP-dependent processes in live animals
Approval Evidence
7 sources16 linked approval claimsfirst-pass slugs beggiatoa-photoactivated-adenylyl-cyclase, beggiatoa-sp-pac, bpac, bpac-adenylyl-cyclase
Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC)
Source:
we introduced two photoactivated adenylyl cyclases (PACs), Beggiatoa sp. PAC (bPAC) and Beggiatoa sp. IS2 PAC (biPAC) into macrophages by transfection
Source:
Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP
Source:
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
Source:
We functionally localized modifiers of cAMP signaling, the photo-activated adenylyl cyclase bPAC ... to the cilium.
Source:
The review discusses applications to bPAC-based cAMP control.
Source:
the HCN2 cyclic nucleotide gated (CNG) channel was modulated by the light activated bPAC adenylyl cyclase
Source:
Next, we coupled this regulatory region to an optogenetic actuator, Beggiatoa photoactivated adenylyl cyclase, to increase endogenous cortisol concentrations in a blue light-dependent manner.
Source:
application conclusionsupports
Light directed signaling in cardiac myocytes can provide a site-specific view of intracellular signaling cascades.
We conclude from these results that light directed signaling in cardiac myocytes can provide a site‐specific view of intracellular signaling cascades.
Source:
application effectsupports
The GelMA-Macrophages-LED system enabled in situ light regulation of cardiac inflammation in murine LPS-induced sepsis models and was associated with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction.
with murine models of LPS-induced sepsis. Our results showed significant inhibition of leukocytes infiltration, especially macrophages and neutrophils, suppression of pro-inflammatory cytokines release, and alleviation of sepsis-induced cardiac dysfunction
Source:
functional effectsupports
Blue light-induced activation of bPAC or biPAC in transfected macrophages inhibited production of the pro-inflammatory cytokines IL-1 and TNF-b1 at both mRNA and protein levels.
blue light-induced bPAC or biPAC activation considerably inhibited the production of pro-inflammatory cytokines IL-1 and TNF-b1, both at mRNA and protein levels
Source:
functional effectsupports
In H9c2 cardiac cells, global cAMP production through bPAC leads to phosphorylation of PKA reporters anchored at the outer mitochondrial membrane and plasma membrane.
Results indicate that global cAMP production, through a light activatable adenylate cyclase (bPAC), leads to phosphorylation of a PKA reporter anchored at the outer mitochondrial membrane and plasma membrane.
Source:
localization specific effectsupports
In H9c2 cardiac cells, nuclear-localized PKA reporters do not show phosphorylation under the reported bPAC-driven global cAMP production condition.
Reporters with nuclear localization do not show this phosphorylation.
Source:
therapeutic potentialsupports
Photo-activated regulation of macrophage function may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases.
our study may represent an emerging means to treat sepsis-induced myocardiopathy and other cardiovascular diseases by photo-activated regulating macrophage function
Source:
biological applicationsupports
Using the nanobody-based targeting approach, the authors studied the contribution of spatial cAMP signaling in controlling cilia length.
Using this approach, we studied the contribution of spatial cAMP signaling in controlling cilia length.
Source:
compatibilitysupports
Booster-PKA enabled monitoring of PKA activation driven by Beggiatoa photoactivated adenylyl cyclase.
we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP
Source:
compatibilitysupports
Booster-PKA is compatible with blue-light optogenetic activation of cAMP signaling using Beggiatoa photoactivated adenylyl cyclase.
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
Source:
compatibilitysupports
Booster-PKA was used to monitor PKA activation driven by Beggiatoa photoactivated adenylyl cyclase.
Second, we showed monitoring of PKA activation by Beggiatoa photoactivated adenylyl cyclase, an optogenetic generator of cyclic AMP.
Source:
localizationsupports
Using the nanobody-based targeting approach, bPAC, LAPD, and mlCNBD-FRET were functionally localized to the cilium.
We functionally localized modifiers of cAMP signaling, the photo-activated adenylyl cyclase bPAC and the light-activated phosphodiesterase LAPD, and the cAMP biosensor mlCNBD-FRET to the cilium.
Source:
application scopesupports
The review discusses bPAC as an optogenetic tool for cAMP control.
Source:
application scopesupports
The reported approach enables specific manipulation of steroidogenic interrenal cell activity for studying both hypo- and hypercortisolemia in zebrafish.
Thus, our approach allows specific manipulations of steroidogenic interrenal cell activity for studying the effects of both hypo- and hypercortisolemia in zebrafish.
Source:
assay performancesupports
Stable, robust, and miniaturized cellular assays can be developed using different optogenetic tools and modulated by FLIPR LEDs in a 384-well format.
stable, robust and miniaturized cellular assays can be developed using different optogenetic tools, and efficiently modulated by the FLIPR instrument LEDs in a 384-well format
Source:
modulation target pairingsupports
bPAC adenylyl cyclase was used to modulate the HCN2 cyclic nucleotide gated channel in an optogenetic assay.
the HCN2 cyclic nucleotide gated (CNG) channel was modulated by the light activated bPAC adenylyl cyclase
Source:
optogenetic controlsupports
Beggiatoa photoactivated adenylyl cyclase targeted to interrenal cells increases endogenous cortisol concentrations in a blue light-dependent manner.
Next, we coupled this regulatory region to an optogenetic actuator, Beggiatoa photoactivated adenylyl cyclase, to increase endogenous cortisol concentrations in a blue light-dependent manner.
Source:
Comparisons
Source-backed strengths
The evidence consistently describes bPAC as an optogenetic generator of cyclic AMP and shows blue light-dependent activation in multiple application settings. Reported uses include PKA pathway activation, ciliary localization of cAMP-modifying activity, and association with reduced leukocyte infiltration, reduced pro-inflammatory cytokine release, and alleviated sepsis-induced cardiac dysfunction in a GelMA-Macrophages-LED system.
Source:
functions as an optogenetic generator of cyclic AMP
Source:
used in combination with Booster-PKA in the abstract's proof-of-concept
Ranked Citations
- 1.
- 2.
- 3.
- 4.
- 5.
- 6.