Toolkit/iLID N414L variant

iLID N414L variant

Multi-Component Switch·Research·Since 2016

Also known as: N414L

Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.

Summary

The iLID N414L variant is a modified iLID light-inducible dimerization system in which an N414L point mutation in the LOV domain lengthens the reversion half-life. In combination with SspB binding partners, it supports blue-light-dependent control of protein colocalization and has been used in reengineered iLID-SspB systems for processes including transmembrane protein localization.

Usefulness & Problems

Why this is useful

This variant is useful because it alters the temporal behavior of the iLID switch by prolonging the lit-state reversion kinetics. The associated iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 uM, addressing conditions where dark-state association can compromise optical control.

Source:

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

Source:

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

Problem solved

The tool helps solve the problem of insufficient kinetic tuning in light-inducible dimerization systems, specifically by lengthening iLID reversion half-life through the N414L LOV-domain mutation. In the broader reengineered iLID-SspB context, it addresses control of protein interactions at high effective concentrations and reduces limitations from excessive dark-state colocalization when paired with appropriate SspB variants.

Source:

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

Source:

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

Problem links

Need conditional recombination or state switching

Derived

The iLID N414L variant is a light-inducible dimerization system variant in which an N414L point mutation in the LOV domain lengthens the reversion half-life of iLID. It is used with SspB binding partners to control blue-light-dependent protein colocalization and related processes such as recombination.

Need precise spatiotemporal control with light input

Derived

The iLID N414L variant is a light-inducible dimerization system variant in which an N414L point mutation in the LOV domain lengthens the reversion half-life of iLID. It is used with SspB binding partners to control blue-light-dependent protein colocalization and related processes such as recombination.

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

recombination

Input: 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 the iLID construct carrying the N414L point mutation in the LOV domain and a compatible SspB binding partner. The system is activated by blue light, and the cited engineering work focused on tuning iLID-SspB behavior for proteins at effective concentrations of 5-100 uM, including transmembrane protein colocalization in neurons.

The supplied evidence directly supports the kinetic effect of the N414L mutation but does not provide a quantitative reversion half-life value for this variant. It also does not isolate application-specific performance of N414L itself apart from the broader iLID-SspB engineering context, so validation for recombination or other target processes is not detailed here.

Validation

Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication

Supporting Sources

Ranked Claims

Claim 1application performancesupports2020Source 2needs review

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
Claim 2application performancesupports2020Source 2needs review

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
Claim 3application performancesupports2020Source 2needs review

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
Claim 4application performancesupports2020Source 2needs review

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
Claim 5application performancesupports2020Source 2needs review

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
Claim 6application performancesupports2020Source 2needs review

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
Claim 7application performancesupports2020Source 2needs review

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
Claim 8application performancesupports2020Source 2needs review

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
Claim 9application performancesupports2020Source 2needs review

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
Claim 10application performancesupports2020Source 2needs review

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
Claim 11binding affinity changesupports2020Source 2needs review

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
Claim 12binding affinity changesupports2020Source 2needs review

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
Claim 13binding affinity changesupports2020Source 2needs review

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
Claim 14binding affinity changesupports2020Source 2needs review

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
Claim 15binding affinity changesupports2020Source 2needs review

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
Claim 16binding affinity changesupports2020Source 2needs review

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
Claim 17binding affinity changesupports2020Source 2needs review

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
Claim 18binding affinity changesupports2020Source 2needs review

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
Claim 19binding affinity changesupports2020Source 2needs review

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
Claim 20binding affinity changesupports2020Source 2needs review

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
Claim 21engineering resultsupports2020Source 2needs review

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
Claim 22engineering resultsupports2020Source 2needs review

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
Claim 23engineering resultsupports2020Source 2needs review

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
Claim 24engineering resultsupports2020Source 2needs review

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
Claim 25engineering resultsupports2020Source 2needs review

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
Claim 26engineering resultsupports2020Source 2needs review

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
Claim 27engineering resultsupports2020Source 2needs review

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
Claim 28engineering resultsupports2020Source 2needs review

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
Claim 29engineering resultsupports2020Source 2needs review

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
Claim 30engineering resultsupports2020Source 2needs review

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
Claim 31kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 32kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 33kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 34kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 35kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 36kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 37kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 38kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 39kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 40kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 41kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 42kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 43kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 44kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 45kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 46kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 47kinetic tuningsupports2020Source 2needs review

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Claim 48mechanismsupports2020Source 2needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
Claim 49mechanismsupports2020Source 2needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
Claim 50mechanismsupports2020Source 2needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
Claim 51mechanismsupports2020Source 2needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
Claim 52mechanismsupports2020Source 2needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
Claim 53mechanismsupports2020Source 2needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
Claim 54mechanismsupports2020Source 2needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
Claim 55mechanismsupports2020Source 2needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
Claim 56mechanismsupports2020Source 2needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
Claim 57mechanismsupports2020Source 2needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
Claim 58scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 59scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 60scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 61scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 62scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 63scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 64scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 65scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 66scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 67scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 68scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 69scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 70scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 71scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 72scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 73scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 74scope expansionsupports2020Source 2needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
Claim 75application performancesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
Claim 76application performancesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
Claim 77application performancesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
Claim 78application performancesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
Claim 79application performancesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
Claim 80application performancesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
Claim 81application performancesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
Claim 82application performancesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
Claim 83application performancesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
Claim 84application performancesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
Claim 85binding affinity changesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
Claim 86binding affinity changesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
Claim 87binding affinity changesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
Claim 88binding affinity changesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
Claim 89binding affinity changesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
Claim 90binding affinity changesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
Claim 91binding affinity changesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
Claim 92binding affinity changesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
Claim 93binding affinity changesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
Claim 94binding affinity changesupports2016Source 1needs review

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
Claim 95engineering resultsupports2016Source 1needs review

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
Claim 96engineering resultsupports2016Source 1needs review

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
Claim 97engineering resultsupports2016Source 1needs review

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
Claim 98engineering resultsupports2016Source 1needs review

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
Claim 99engineering resultsupports2016Source 1needs review

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
Claim 100engineering resultsupports2016Source 1needs review

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
Claim 101engineering resultsupports2016Source 1needs review

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
Claim 102engineering resultsupports2016Source 1needs review

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
Claim 103engineering resultsupports2016Source 1needs review

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
Claim 104engineering resultsupports2016Source 1needs review

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
Claim 105kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 106kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 107kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 108kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 109kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 110kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 111kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 112kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 113kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 114kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 115kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 116kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 117kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 118kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 119kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 120kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 121kinetic tuningsupports2016Source 1needs review

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
Claim 122mechanismsupports2016Source 1needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
Claim 123mechanismsupports2016Source 1needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
Claim 124mechanismsupports2016Source 1needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
Claim 125mechanismsupports2016Source 1needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
Claim 126mechanismsupports2016Source 1needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
Claim 127mechanismsupports2016Source 1needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
Claim 128mechanismsupports2016Source 1needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
Claim 129mechanismsupports2016Source 1needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
Claim 130mechanismsupports2016Source 1needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
Claim 131mechanismsupports2016Source 1needs review

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
Claim 132scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 133scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 134scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 135scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 136scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 137scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 138scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 139scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 140scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 141scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 142scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 143scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 144scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 145scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 146scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 147scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
Claim 148scope expansionsupports2016Source 1needs review

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.

Approval Evidence

2 sources4 linked approval claimsfirst-pass slug ilid-n414l-variant
with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID

Source:

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID

Source:

kinetic tuningsupports

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID

Source:

scope expansionsupports

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light

Source:

kinetic tuningsupports

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.

Source:

scope expansionsupports

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.

Source:

Comparisons

Source-backed strengths

The defining engineered property supported by the evidence is a lengthened reversion half-life caused by the N414L mutation in the LOV domain. In the related tuned iLID-SspB system, the SspB A58V dimer variant enabled light-activated colocalization of transmembrane proteins in neurons, and this partner showed a 42-fold light-dependent affinity change from 3 ± 2 uM to 125 ± 40 nM.

Source:

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)

Source:

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).

Compared with AQTrip EL222 variant

iLID N414L variant and AQTrip EL222 variant address a similar problem space because they share recombination.

Shared frame: same top-level item type; shared target processes: recombination; shared mechanisms: heterodimerization; same primary input modality: light

Strengths here: appears more independently replicated; looks easier to implement in practice.

Compared with CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system

iLID N414L variant and CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system address a similar problem space because they share recombination.

Shared frame: same top-level item type; shared target processes: recombination; shared mechanisms: heterodimerization; same primary input modality: light

Strengths here: appears more independently replicated; looks easier to implement in practice.

Compared with PA-Cre 3.0

iLID N414L variant and PA-Cre 3.0 address a similar problem space because they share recombination.

Shared frame: same top-level item type; shared target processes: recombination; shared mechanisms: heterodimerization; same primary input modality: light

Strengths here: appears more independently replicated; looks easier to implement in practice.

Ranked Citations

  1. 1.
    StructuralSource 1Biochemistry2016Claim 83Claim 84Claim 83

    Extracted from this source document.

  2. 2.
    StructuralSource 2Figshare2020Claim 6Claim 6Claim 6

    Extracted from this source document.