Source 1primary paper2015ACS Synthetic Biology
Toolkit/LOVpep/ePDZb
LOVpep/ePDZb
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
LOVpep/ePDZb is a blue-light-inducible heterodimerization system examined as one of three optogenetic dimer variants in a comparative cellular optogenetics study. It mediates light-dependent protein association that was used to control cellular localization and activity in assays including transcription, intracellular localization, and GTPase signaling.
Usefulness & Problems
Why this is useful
This system is useful as a multi-component optogenetic switch for controlling protein localization and activity with high spatial and temporal resolution under blue light. The cited comparative study further indicates that its binding behavior can be related to in vivo performance through colocalization and functional assays.
Source:
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Problem solved
LOVpep/ePDZb helps solve the problem of reversibly coupling protein association to light input for perturbing cellular processes such as transcription, localization, and signaling. It also addresses the need to compare how dark-state and lit-state binding affinities influence cellular optogenetic performance.
Problem links
Need conditional control of signaling activity
DerivedLOVpep/ePDZb is one of three examined blue-light-inducible dimer systems used as a multi-component optogenetic switch. It enables light-dependent protein association for control of cellular localization and activity in assays spanning transcription, intracellular localization, and GTPase signaling.
Need inducible protein relocalization or recruitment
DerivedLOVpep/ePDZb is one of three examined blue-light-inducible dimer systems used as a multi-component optogenetic switch. It enables light-dependent protein association for control of cellular localization and activity in assays spanning transcription, intracellular localization, and GTPase signaling.
Need precise spatiotemporal control with light input
DerivedLOVpep/ePDZb is one of three examined blue-light-inducible dimer systems used as a multi-component optogenetic switch. It enables light-dependent protein association for control of cellular localization and activity in assays spanning transcription, intracellular localization, and GTPase signaling.
Need tighter control over gene expression timing or amplitude
DerivedLOVpep/ePDZb is one of three examined blue-light-inducible dimer systems used as a multi-component optogenetic switch. It enables light-dependent protein association for control of cellular localization and activity in assays spanning transcription, intracellular localization, and GTPase signaling.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Target processes
localizationsignalingtranscriptionInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: actuatoroperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment
Implementation requires blue-light illumination because LOVpep/ePDZb is described as a blue-light-inducible dimer variant. The provided evidence supports use in colocalization and functional assays spanning transcription, intracellular localization, and GTPase signaling, but it does not specify wavelengths, cofactors, expression systems, or fusion architectures.
The supplied evidence does not provide quantitative affinity values, kinetic parameters, dynamic range, or construct-level design details specific to LOVpep/ePDZb. Independent replication is not established from the provided sources, which are limited to a comparative study and a Figshare record of the same work.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2019Figshare
Ranked Claims
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
Approval Evidence
2 sources6 linked approval claimsfirst-pass slug lovpep-epdzb
three blue-light-inducible dimer variants (cryptochrome2 (CRY2)/CIB1, iLID/SspB, and LOVpep/ePDZb)
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three blue-light-inducible dimer variants (cryptochrome2 (CRY2)/CIB1, iLID/SspB, and LOVpep/ePDZb)
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capabilitysupports
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
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comparative propertysupports
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
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correlationsupports
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
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assay applicationsupports
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
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comparative characterizationsupports
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
Source:
correlationsupports
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
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Comparisons
Source-backed strengths
The available evidence supports that LOVpep/ePDZb functions as a blue-light-inducible dimer for optical control of localization and activity. It was evaluated alongside CRY2/CIB1 and iLID/SspB, and the study reported that binding affinities of the examined dimers correlate with in vivo function measured by colocalization and functional assays.
Source:
We find that the switches vary dramatically in their dark and lit state binding affinities
Source:
We find that the switches vary dramatically in their dark and lit state binding affinities
Compared with BcLOV4-RhoA optogenetic fusion
LOVpep/ePDZb and BcLOV4-RhoA optogenetic fusion address a similar problem space because they share localization, signaling, transcription.
Shared frame: same top-level item type; shared target processes: localization, signaling, transcription; shared mechanisms: heterodimerization; same primary input modality: light
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with Cry2
LOVpep/ePDZb and Cry2 address a similar problem space because they share localization, signaling, transcription.
Shared frame: same top-level item type; shared target processes: localization, signaling, transcription; shared mechanisms: heterodimerization; same primary input modality: light
Strengths here: looks easier to implement in practice; may avoid an exogenous cofactor requirement.
Relative tradeoffs: appears more independently replicated.
Compared with iLID/SspB
LOVpep/ePDZb and iLID/SspB address a similar problem space because they share localization, signaling, transcription.
Shared frame: same top-level item type; shared target processes: localization, signaling, transcription; shared mechanisms: heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated.
Ranked Citations
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