Source 1primary paper2021ACS Synthetic Biology
Toolkit/C-terminal iLID fusion
C-terminal iLID fusion
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
C-terminal iLID fusion is a commonly used anchor configuration within the iLID optogenetic recruitment system. In the cited study, it functions as a baseline membrane-anchor design for light-controlled recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
Usefulness & Problems
Why this is useful
This configuration is useful as part of the iLID system for controlling subcellular protein localization with optical input. The cited work places it within a toolset intended to provide greater control of subcellular protein localization across diverse cell biological applications.
Source:
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Source:
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
Source:
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
Problem solved
It helps address the problem of selectively recruiting molecular components to defined subcellular locations using light. The cited evidence specifically supports recruitment to micron-scale regions of the plasma membrane.
Source:
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
No technique tags yet.
Target processes
localizationsignalingImplementation Constraints
The evidence identifies this tool as a C-terminal fusion form of an iLID anchor used for optogenetic protein recruitment. The supplied material does not specify construct architecture beyond C-terminal placement, nor does it provide details on cofactors, expression systems, illumination parameters, or delivery methods.
The supplied evidence does not provide direct performance metrics for the C-terminal iLID fusion itself beyond identifying it as a commonly used configuration. Quantitative data on kinetics, dynamic range, background recruitment, expression dependence, or validation across cell types are not provided here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.
These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.
the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.
Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.
we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
The study defines guidelines for component expression regimes that optimize recruitment for both cell-wide and subcellular recruitment strategies.
We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.
Approval Evidence
1 source1 linked approval claimfirst-pass slug c-terminal-ilid-fusion
the commonly used C-terminal iLID fusion
Source:
comparative performancesupports
Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Source:
Comparisons
Source-backed strengths
The available evidence supports that the iLID system, in which this C-terminal fusion configuration is commonly used, enables selective subcellular recruitment with micron-scale spatial targeting at the plasma membrane. It is also established enough in the literature to serve as the comparison baseline for anchor optimization.
Source:
Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.
Ranked Citations
- 1.