Toolkit/OptoBAX
OptoBAX
Also known as: Cry2-BAX system, light activated Cry2-BAX system
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
OptoBAX is an optimized light-activated Cry2-BAX multi-component optogenetic system developed for one-click initiation of the BAX-mediated apoptotic cascade. It is used to trigger outer mitochondrial membrane permeabilization and induce early apoptotic events with light.
Usefulness & Problems
Why this is useful
OptoBAX provides optical control over initiation of apoptosis, enabling timed induction of BAX-dependent outer mitochondrial membrane permeabilization. In the cited work, it was used to measure the timing of morphological and biochemical changes during early apoptosis and to track MOMP-induced actin redistribution.
Source:
we have utilized OptoBAX in a series of experiments designed to measure the timing of the dramatic morphological and biochemical changes that occur in apoptotic cells following light-induced permeabilization of the outer mitochondrial membrane
Source:
in addition to reducing dark state cytotoxicity
Source:
The resulting optogenetic constructs have significantly reduced the frequency of light exposure required for the activation of membrane permeabilization
Source:
Previously, we have employed Cryptochrome 2 (Cry2)/CIB, a blue light photoreceptor protein - protein dimerization module from A. thaliana in conjunction with BAX, an OMM targeting pro-apoptotic protein, for light-mediated initiation of mitochondrial outer membrane permeabilization (MOMP) and downstream apoptosis.
Problem solved
This tool addresses the need for precise experimental initiation of the BAX-mediated apoptotic program so that early downstream cellular events can be temporally resolved. The optimized constructs also address dark-state cytotoxicity reported for earlier versions of the light-activated Cry2-BAX system.
Source:
we have utilized OptoBAX in a series of experiments designed to measure the timing of the dramatic morphological and biochemical changes that occur in apoptotic cells following light-induced permeabilization of the outer mitochondrial membrane
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
HeterodimerizationTechniques
Computational DesignTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
The tool is described as a light-activated Cry2-BAX multi-component system, indicating a construct architecture involving Cry2 and BAX. The provided evidence does not specify wavelengths, expression context, mitochondrial targeting design, or other construct-delivery details.
The supplied evidence does not provide quantitative performance metrics, illumination parameters, or direct comparative benchmarking beyond reduced dark-state cytotoxicity. Independent replication is not documented in the provided sources.
Validation
Supporting Sources
Ranked Claims
OptoBAX was used to measure the timing of morphological and biochemical changes in apoptotic cells after light-induced outer mitochondrial membrane permeabilization.
we have utilized OptoBAX in a series of experiments designed to measure the timing of the dramatic morphological and biochemical changes that occur in apoptotic cells following light-induced permeabilization of the outer mitochondrial membrane
OptoBAX was used to measure the timing of morphological and biochemical changes in apoptotic cells after light-induced outer mitochondrial membrane permeabilization.
we have utilized OptoBAX in a series of experiments designed to measure the timing of the dramatic morphological and biochemical changes that occur in apoptotic cells following light-induced permeabilization of the outer mitochondrial membrane
OptoBAX was used to measure the timing of morphological and biochemical changes in apoptotic cells after light-induced outer mitochondrial membrane permeabilization.
we have utilized OptoBAX in a series of experiments designed to measure the timing of the dramatic morphological and biochemical changes that occur in apoptotic cells following light-induced permeabilization of the outer mitochondrial membrane
OptoBAX was used to measure the timing of morphological and biochemical changes in apoptotic cells after light-induced outer mitochondrial membrane permeabilization.
we have utilized OptoBAX in a series of experiments designed to measure the timing of the dramatic morphological and biochemical changes that occur in apoptotic cells following light-induced permeabilization of the outer mitochondrial membrane
OptoBAX was used to measure the timing of morphological and biochemical changes in apoptotic cells after light-induced outer mitochondrial membrane permeabilization.
we have utilized OptoBAX in a series of experiments designed to measure the timing of the dramatic morphological and biochemical changes that occur in apoptotic cells following light-induced permeabilization of the outer mitochondrial membrane
OptoBAX was used to measure the timing of morphological and biochemical changes in apoptotic cells after light-induced outer mitochondrial membrane permeabilization.
we have utilized OptoBAX in a series of experiments designed to measure the timing of the dramatic morphological and biochemical changes that occur in apoptotic cells following light-induced permeabilization of the outer mitochondrial membrane
OptoBAX was used to measure the timing of morphological and biochemical changes in apoptotic cells after light-induced outer mitochondrial membrane permeabilization.
we have utilized OptoBAX in a series of experiments designed to measure the timing of the dramatic morphological and biochemical changes that occur in apoptotic cells following light-induced permeabilization of the outer mitochondrial membrane
The study constructs a timeline of biochemical and morphological events in early apoptosis and tracks MOMP-induced redistribution of actin.
Utilizing this data, we construct a timeline of biochemical and morphological events in early apoptosis, in addition to tracking the MOMP-induced redistribution of actin
The study constructs a timeline of biochemical and morphological events in early apoptosis and tracks MOMP-induced redistribution of actin.
Utilizing this data, we construct a timeline of biochemical and morphological events in early apoptosis, in addition to tracking the MOMP-induced redistribution of actin
The study constructs a timeline of biochemical and morphological events in early apoptosis and tracks MOMP-induced redistribution of actin.
Utilizing this data, we construct a timeline of biochemical and morphological events in early apoptosis, in addition to tracking the MOMP-induced redistribution of actin
The study constructs a timeline of biochemical and morphological events in early apoptosis and tracks MOMP-induced redistribution of actin.
Utilizing this data, we construct a timeline of biochemical and morphological events in early apoptosis, in addition to tracking the MOMP-induced redistribution of actin
The study constructs a timeline of biochemical and morphological events in early apoptosis and tracks MOMP-induced redistribution of actin.
Utilizing this data, we construct a timeline of biochemical and morphological events in early apoptosis, in addition to tracking the MOMP-induced redistribution of actin
The study constructs a timeline of biochemical and morphological events in early apoptosis and tracks MOMP-induced redistribution of actin.
Utilizing this data, we construct a timeline of biochemical and morphological events in early apoptosis, in addition to tracking the MOMP-induced redistribution of actin
The study constructs a timeline of biochemical and morphological events in early apoptosis and tracks MOMP-induced redistribution of actin.
Utilizing this data, we construct a timeline of biochemical and morphological events in early apoptosis, in addition to tracking the MOMP-induced redistribution of actin
The optimized OptoBAX constructs reduce dark state cytotoxicity.
in addition to reducing dark state cytotoxicity
The optimized OptoBAX constructs reduce dark state cytotoxicity.
in addition to reducing dark state cytotoxicity
The optimized OptoBAX constructs reduce dark state cytotoxicity.
in addition to reducing dark state cytotoxicity
The optimized OptoBAX constructs reduce dark state cytotoxicity.
in addition to reducing dark state cytotoxicity
The optimized OptoBAX constructs reduce dark state cytotoxicity.
in addition to reducing dark state cytotoxicity
The optimized OptoBAX constructs reduce dark state cytotoxicity.
in addition to reducing dark state cytotoxicity
The optimized OptoBAX constructs reduce dark state cytotoxicity.
in addition to reducing dark state cytotoxicity
The optimized OptoBAX constructs reduce the frequency of light exposure required to activate membrane permeabilization.
The resulting optogenetic constructs have significantly reduced the frequency of light exposure required for the activation of membrane permeabilization
The optimized OptoBAX constructs reduce the frequency of light exposure required to activate membrane permeabilization.
The resulting optogenetic constructs have significantly reduced the frequency of light exposure required for the activation of membrane permeabilization
The optimized OptoBAX constructs reduce the frequency of light exposure required to activate membrane permeabilization.
The resulting optogenetic constructs have significantly reduced the frequency of light exposure required for the activation of membrane permeabilization
The optimized OptoBAX constructs reduce the frequency of light exposure required to activate membrane permeabilization.
The resulting optogenetic constructs have significantly reduced the frequency of light exposure required for the activation of membrane permeabilization
The optimized OptoBAX constructs reduce the frequency of light exposure required to activate membrane permeabilization.
The resulting optogenetic constructs have significantly reduced the frequency of light exposure required for the activation of membrane permeabilization
The optimized OptoBAX constructs reduce the frequency of light exposure required to activate membrane permeabilization.
The resulting optogenetic constructs have significantly reduced the frequency of light exposure required for the activation of membrane permeabilization
The optimized OptoBAX constructs reduce the frequency of light exposure required to activate membrane permeabilization.
The resulting optogenetic constructs have significantly reduced the frequency of light exposure required for the activation of membrane permeabilization
OptoBAX was further developed for one-click initiation of the BAX-mediated apoptotic cascade.
In this work, we are further developing our light activated Cry2-BAX system (henceforth referred to as "OptoBAX") for "one click" initiation of the BAX-mediated apoptotic cascade.
OptoBAX was further developed for one-click initiation of the BAX-mediated apoptotic cascade.
In this work, we are further developing our light activated Cry2-BAX system (henceforth referred to as "OptoBAX") for "one click" initiation of the BAX-mediated apoptotic cascade.
OptoBAX was further developed for one-click initiation of the BAX-mediated apoptotic cascade.
In this work, we are further developing our light activated Cry2-BAX system (henceforth referred to as "OptoBAX") for "one click" initiation of the BAX-mediated apoptotic cascade.
OptoBAX was further developed for one-click initiation of the BAX-mediated apoptotic cascade.
In this work, we are further developing our light activated Cry2-BAX system (henceforth referred to as "OptoBAX") for "one click" initiation of the BAX-mediated apoptotic cascade.
OptoBAX was further developed for one-click initiation of the BAX-mediated apoptotic cascade.
In this work, we are further developing our light activated Cry2-BAX system (henceforth referred to as "OptoBAX") for "one click" initiation of the BAX-mediated apoptotic cascade.
OptoBAX was further developed for one-click initiation of the BAX-mediated apoptotic cascade.
In this work, we are further developing our light activated Cry2-BAX system (henceforth referred to as "OptoBAX") for "one click" initiation of the BAX-mediated apoptotic cascade.
OptoBAX was further developed for one-click initiation of the BAX-mediated apoptotic cascade.
In this work, we are further developing our light activated Cry2-BAX system (henceforth referred to as "OptoBAX") for "one click" initiation of the BAX-mediated apoptotic cascade.
The reported optimization efforts aimed to reduce light-independent cell death and improve experimental control by manipulating photophysical properties of the Cry2/CIB interaction.
We also report results of experimental efforts to optimize our optogenetic switch to reduce light-independent cell death (dark activation), and to enhance experimental control of our switch by manipulating photophysical properties associated with the Cry2/CIB interaction.
The reported optimization efforts aimed to reduce light-independent cell death and improve experimental control by manipulating photophysical properties of the Cry2/CIB interaction.
We also report results of experimental efforts to optimize our optogenetic switch to reduce light-independent cell death (dark activation), and to enhance experimental control of our switch by manipulating photophysical properties associated with the Cry2/CIB interaction.
The reported optimization efforts aimed to reduce light-independent cell death and improve experimental control by manipulating photophysical properties of the Cry2/CIB interaction.
We also report results of experimental efforts to optimize our optogenetic switch to reduce light-independent cell death (dark activation), and to enhance experimental control of our switch by manipulating photophysical properties associated with the Cry2/CIB interaction.
The reported optimization efforts aimed to reduce light-independent cell death and improve experimental control by manipulating photophysical properties of the Cry2/CIB interaction.
We also report results of experimental efforts to optimize our optogenetic switch to reduce light-independent cell death (dark activation), and to enhance experimental control of our switch by manipulating photophysical properties associated with the Cry2/CIB interaction.
The reported optimization efforts aimed to reduce light-independent cell death and improve experimental control by manipulating photophysical properties of the Cry2/CIB interaction.
We also report results of experimental efforts to optimize our optogenetic switch to reduce light-independent cell death (dark activation), and to enhance experimental control of our switch by manipulating photophysical properties associated with the Cry2/CIB interaction.
The reported optimization efforts aimed to reduce light-independent cell death and improve experimental control by manipulating photophysical properties of the Cry2/CIB interaction.
We also report results of experimental efforts to optimize our optogenetic switch to reduce light-independent cell death (dark activation), and to enhance experimental control of our switch by manipulating photophysical properties associated with the Cry2/CIB interaction.
The reported optimization efforts aimed to reduce light-independent cell death and improve experimental control by manipulating photophysical properties of the Cry2/CIB interaction.
We also report results of experimental efforts to optimize our optogenetic switch to reduce light-independent cell death (dark activation), and to enhance experimental control of our switch by manipulating photophysical properties associated with the Cry2/CIB interaction.
The Cry2/CIB module used in conjunction with BAX enabled light-mediated initiation of mitochondrial outer membrane permeabilization and downstream apoptosis.
Previously, we have employed Cryptochrome 2 (Cry2)/CIB, a blue light photoreceptor protein - protein dimerization module from A. thaliana in conjunction with BAX, an OMM targeting pro-apoptotic protein, for light-mediated initiation of mitochondrial outer membrane permeabilization (MOMP) and downstream apoptosis.
The Cry2/CIB module used in conjunction with BAX enabled light-mediated initiation of mitochondrial outer membrane permeabilization and downstream apoptosis.
Previously, we have employed Cryptochrome 2 (Cry2)/CIB, a blue light photoreceptor protein - protein dimerization module from A. thaliana in conjunction with BAX, an OMM targeting pro-apoptotic protein, for light-mediated initiation of mitochondrial outer membrane permeabilization (MOMP) and downstream apoptosis.
The Cry2/CIB module used in conjunction with BAX enabled light-mediated initiation of mitochondrial outer membrane permeabilization and downstream apoptosis.
Previously, we have employed Cryptochrome 2 (Cry2)/CIB, a blue light photoreceptor protein - protein dimerization module from A. thaliana in conjunction with BAX, an OMM targeting pro-apoptotic protein, for light-mediated initiation of mitochondrial outer membrane permeabilization (MOMP) and downstream apoptosis.
The Cry2/CIB module used in conjunction with BAX enabled light-mediated initiation of mitochondrial outer membrane permeabilization and downstream apoptosis.
Previously, we have employed Cryptochrome 2 (Cry2)/CIB, a blue light photoreceptor protein - protein dimerization module from A. thaliana in conjunction with BAX, an OMM targeting pro-apoptotic protein, for light-mediated initiation of mitochondrial outer membrane permeabilization (MOMP) and downstream apoptosis.
The Cry2/CIB module used in conjunction with BAX enabled light-mediated initiation of mitochondrial outer membrane permeabilization and downstream apoptosis.
Previously, we have employed Cryptochrome 2 (Cry2)/CIB, a blue light photoreceptor protein - protein dimerization module from A. thaliana in conjunction with BAX, an OMM targeting pro-apoptotic protein, for light-mediated initiation of mitochondrial outer membrane permeabilization (MOMP) and downstream apoptosis.
The Cry2/CIB module used in conjunction with BAX enabled light-mediated initiation of mitochondrial outer membrane permeabilization and downstream apoptosis.
Previously, we have employed Cryptochrome 2 (Cry2)/CIB, a blue light photoreceptor protein - protein dimerization module from A. thaliana in conjunction with BAX, an OMM targeting pro-apoptotic protein, for light-mediated initiation of mitochondrial outer membrane permeabilization (MOMP) and downstream apoptosis.
The Cry2/CIB module used in conjunction with BAX enabled light-mediated initiation of mitochondrial outer membrane permeabilization and downstream apoptosis.
Previously, we have employed Cryptochrome 2 (Cry2)/CIB, a blue light photoreceptor protein - protein dimerization module from A. thaliana in conjunction with BAX, an OMM targeting pro-apoptotic protein, for light-mediated initiation of mitochondrial outer membrane permeabilization (MOMP) and downstream apoptosis.
Approval Evidence
we have further developed our original light activated Cry2-BAX system (henceforth referred to as “OptoBAX”)
Source:
In this work, we are further developing our light activated Cry2-BAX system (henceforth referred to as "OptoBAX") for "one click" initiation of the BAX-mediated apoptotic cascade.
Source:
OptoBAX was used to measure the timing of morphological and biochemical changes in apoptotic cells after light-induced outer mitochondrial membrane permeabilization.
we have utilized OptoBAX in a series of experiments designed to measure the timing of the dramatic morphological and biochemical changes that occur in apoptotic cells following light-induced permeabilization of the outer mitochondrial membrane
Source:
The study constructs a timeline of biochemical and morphological events in early apoptosis and tracks MOMP-induced redistribution of actin.
Utilizing this data, we construct a timeline of biochemical and morphological events in early apoptosis, in addition to tracking the MOMP-induced redistribution of actin
Source:
The optimized OptoBAX constructs reduce dark state cytotoxicity.
in addition to reducing dark state cytotoxicity
Source:
The optimized OptoBAX constructs reduce the frequency of light exposure required to activate membrane permeabilization.
The resulting optogenetic constructs have significantly reduced the frequency of light exposure required for the activation of membrane permeabilization
Source:
OptoBAX was further developed for one-click initiation of the BAX-mediated apoptotic cascade.
In this work, we are further developing our light activated Cry2-BAX system (henceforth referred to as "OptoBAX") for "one click" initiation of the BAX-mediated apoptotic cascade.
Source:
The reported optimization efforts aimed to reduce light-independent cell death and improve experimental control by manipulating photophysical properties of the Cry2/CIB interaction.
We also report results of experimental efforts to optimize our optogenetic switch to reduce light-independent cell death (dark activation), and to enhance experimental control of our switch by manipulating photophysical properties associated with the Cry2/CIB interaction.
Source:
The Cry2/CIB module used in conjunction with BAX enabled light-mediated initiation of mitochondrial outer membrane permeabilization and downstream apoptosis.
Previously, we have employed Cryptochrome 2 (Cry2)/CIB, a blue light photoreceptor protein - protein dimerization module from A. thaliana in conjunction with BAX, an OMM targeting pro-apoptotic protein, for light-mediated initiation of mitochondrial outer membrane permeabilization (MOMP) and downstream apoptosis.
Source:
Comparisons
Source-backed strengths
The reported optimized OptoBAX constructs reduce dark-state cytotoxicity. The system supported construction of a timeline of biochemical and morphological events in early apoptosis after light-induced outer mitochondrial membrane permeabilization.
Source:
In this work, we are further developing our light activated Cry2-BAX system (henceforth referred to as "OptoBAX") for "one click" initiation of the BAX-mediated apoptotic cascade.
Source:
We also report results of experimental efforts to optimize our optogenetic switch to reduce light-independent cell death (dark activation), and to enhance experimental control of our switch by manipulating photophysical properties associated with the Cry2/CIB interaction.
Ranked Citations
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- 2.