Source 1primary paper2020
Toolkit/LiCre
LiCre
Also known as: light-inducible Cre, light-inducible Cre recombinase
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Assembly Hierarchy
Components
- AsLOV2protein domain
Summary
LiCre is a single-chain light-inducible Cre recombinase optogenetic switch. The supplied evidence supports that blue light can activate Cre-dependent recombination outputs, including induction of antibiotic resistance gene expression in Escherichia coli.
Usefulness & Problems
Why this is useful
LiCre is useful for coupling light input to site-specific Cre-lox recombination without requiring a split recombinase format, based on the cited description of a single-chain light-inducible Cre. In the supplied application evidence, it enabled blue-light control of antibiotic resistance gene expression in E. coli and was linked to expression of a heterologous fatty acid enzyme to increase octanoic acid production.
Source:
We then link inducible resistance to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
Source:
We demonstrate light-activated resistance to four antibiotics: carbenicillin, kanamycin, chloramphenicol, and tetracycline.
Source:
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Problem solved
LiCre addresses the problem of externally controlling Cre-mediated recombination with light rather than constitutive activity. The provided evidence specifically shows its use for conditional survival and selectable gene expression under antibiotic pressure in E. coli.
Source:
We then link inducible resistance to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
Source:
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
Published Workflows
Likely fit
- •fast-no-cloning-screen: useful for reporter-based activity checks in yeast or mammalian cells
- •standard-construct-loop: useful when recombination background, response time, or host-context effects require iteration
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
editingrecombinationInput: Light
Output: Recombination
Implementation Constraints
The documented implementation context is expression in Escherichia coli with blue-light induction of Cre-dependent drug resistance genes. The evidence indicates use in constructs where recombination activates resistance outputs, but it does not provide domain architecture, chromophore requirements, illumination parameters, or construct design details.
The supplied evidence is concentrated on antibiotic-resistance activation in E. coli and does not provide quantitative recombination efficiencies, kinetics, leakiness measurements, or performance across other organisms. Although source titles describe LiCre as fast-responding and single-chain, the extraction evidence provided here does not include experimental details needed to substantiate those properties in this profile.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Observations
successBacteriaapplication demoEscherichia coli
Inferred from claim c3 during normalization. Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not. Derived from claim c3. Quoted text: Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
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successBacteriaapplication demoEscherichia coli
Inferred from claim c3 during normalization. Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not. Derived from claim c3. Quoted text: Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
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successBacteriaapplication demoEscherichia coli
Inferred from claim c3 during normalization. Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not. Derived from claim c3. Quoted text: Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Source:
successBacteriaapplication demoEscherichia coli
Inferred from claim c3 during normalization. Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not. Derived from claim c3. Quoted text: Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Source:
successBacteriaapplication demoEscherichia coli
Inferred from claim c3 during normalization. Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not. Derived from claim c3. Quoted text: Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Source:
successBacteriaapplication demoEscherichia coli
Inferred from claim c3 during normalization. Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not. Derived from claim c3. Quoted text: Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Source:
successBacteriaapplication demoEscherichia coli
Inferred from claim c3 during normalization. Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not. Derived from claim c3. Quoted text: Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and allowed light-controlled production of β-carotene. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and allowed light-controlled production of β-carotene. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and allowed light-controlled production of β-carotene. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and allowed light-controlled production of β-carotene. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and allowed light-controlled production of β-carotene. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and allowed light-controlled production of β-carotene. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and allowed light-controlled production of β-carotene. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and enabled light control of β-carotene production. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
Source:
successYeastapplication demo
Inferred from claim c4 during normalization. LiCre was efficient in yeast and allowed light control of beta-carotene production. Derived from claim c4. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in human cells. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and enabled light control of β-carotene production. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and enabled light control of β-carotene production. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
Source:
successYeastapplication demo
Inferred from claim c4 during normalization. LiCre was efficient in yeast and allowed light control of beta-carotene production. Derived from claim c4. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
Source:
successYeastapplication demo
Inferred from claim c4 during normalization. LiCre was efficient in yeast and allowed light control of beta-carotene production. Derived from claim c4. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in human cells. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and enabled light control of β-carotene production. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
Source:
successYeastapplication demo
Inferred from claim c4 during normalization. LiCre was efficient in yeast and allowed light control of beta-carotene production. Derived from claim c4. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in human cells. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and enabled light control of β-carotene production. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
Source:
successYeastapplication demo
Inferred from claim c4 during normalization. LiCre was efficient in yeast and allowed light control of beta-carotene production. Derived from claim c4. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in human cells. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and enabled light control of β-carotene production. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
Source:
successYeastapplication demo
Inferred from claim c4 during normalization. LiCre was efficient in yeast and allowed light control of beta-carotene production. Derived from claim c4. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in human cells. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in human cells. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successYeastapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in yeast and enabled light control of β-carotene production. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c6 during normalization. LiCre was efficient in human cells. Derived from claim c6. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
Source:
successYeastapplication demo
Inferred from claim c4 during normalization. LiCre was efficient in yeast and allowed light control of beta-carotene production. Derived from claim c4. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c5 during normalization. LiCre was efficient in human cells. Derived from claim c5. Quoted text: LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
Supporting Sources
Source 2primary paper2021eLife
Source 3primary paper2023Nature Communications
Source 4primary paper2021
Source 5primary paper2020
Ranked Claims
Inducible resistance was linked to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
We then link inducible resistance to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
Inducible resistance was linked to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
We then link inducible resistance to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
Inducible resistance was linked to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
We then link inducible resistance to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
Inducible resistance was linked to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
We then link inducible resistance to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
Inducible resistance was linked to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
We then link inducible resistance to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
Inducible resistance was linked to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
We then link inducible resistance to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
Inducible resistance was linked to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
We then link inducible resistance to expression of a heterologous fatty acid enzyme to increase production of octanoic acid.
The system demonstrated light-activated resistance to carbenicillin, kanamycin, chloramphenicol, and tetracycline.
We demonstrate light-activated resistance to four antibiotics: carbenicillin, kanamycin, chloramphenicol, and tetracycline.
The system demonstrated light-activated resistance to carbenicillin, kanamycin, chloramphenicol, and tetracycline.
We demonstrate light-activated resistance to four antibiotics: carbenicillin, kanamycin, chloramphenicol, and tetracycline.
The system demonstrated light-activated resistance to carbenicillin, kanamycin, chloramphenicol, and tetracycline.
We demonstrate light-activated resistance to four antibiotics: carbenicillin, kanamycin, chloramphenicol, and tetracycline.
The system demonstrated light-activated resistance to carbenicillin, kanamycin, chloramphenicol, and tetracycline.
We demonstrate light-activated resistance to four antibiotics: carbenicillin, kanamycin, chloramphenicol, and tetracycline.
The system demonstrated light-activated resistance to carbenicillin, kanamycin, chloramphenicol, and tetracycline.
We demonstrate light-activated resistance to four antibiotics: carbenicillin, kanamycin, chloramphenicol, and tetracycline.
The system demonstrated light-activated resistance to carbenicillin, kanamycin, chloramphenicol, and tetracycline.
We demonstrate light-activated resistance to four antibiotics: carbenicillin, kanamycin, chloramphenicol, and tetracycline.
The system demonstrated light-activated resistance to carbenicillin, kanamycin, chloramphenicol, and tetracycline.
We demonstrate light-activated resistance to four antibiotics: carbenicillin, kanamycin, chloramphenicol, and tetracycline.
Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not.
Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not.
Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not.
Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not.
Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not.
Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not.
Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not.
Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Light-inducible Cre recombinase was used to activate expression of drug resistance genes in Escherichia coli.
Here, we use light-inducible Cre recombinase to activate expression of drug resistance genes in Escherichia coli.
Light-inducible Cre recombinase was used to activate expression of drug resistance genes in Escherichia coli.
Here, we use light-inducible Cre recombinase to activate expression of drug resistance genes in Escherichia coli.
Light-inducible Cre recombinase was used to activate expression of drug resistance genes in Escherichia coli.
Here, we use light-inducible Cre recombinase to activate expression of drug resistance genes in Escherichia coli.
Light-inducible Cre recombinase was used to activate expression of drug resistance genes in Escherichia coli.
Here, we use light-inducible Cre recombinase to activate expression of drug resistance genes in Escherichia coli.
Light-inducible Cre recombinase was used to activate expression of drug resistance genes in Escherichia coli.
Here, we use light-inducible Cre recombinase to activate expression of drug resistance genes in Escherichia coli.
Light-inducible Cre recombinase was used to activate expression of drug resistance genes in Escherichia coli.
Here, we use light-inducible Cre recombinase to activate expression of drug resistance genes in Escherichia coli.
Light-inducible Cre recombinase was used to activate expression of drug resistance genes in Escherichia coli.
Here, we use light-inducible Cre recombinase to activate expression of drug resistance genes in Escherichia coli.
Resistance induction was optimized by varying promoter strength, ribosome binding site strength, and enzyme variant strength using chromosome-based and plasmid-based constructs.
To optimize resistance induction, we vary promoter, ribosome binding site, and enzyme variant strength using chromosome and plasmid-based constructs.
Resistance induction was optimized by varying promoter strength, ribosome binding site strength, and enzyme variant strength using chromosome-based and plasmid-based constructs.
To optimize resistance induction, we vary promoter, ribosome binding site, and enzyme variant strength using chromosome and plasmid-based constructs.
Resistance induction was optimized by varying promoter strength, ribosome binding site strength, and enzyme variant strength using chromosome-based and plasmid-based constructs.
To optimize resistance induction, we vary promoter, ribosome binding site, and enzyme variant strength using chromosome and plasmid-based constructs.
Resistance induction was optimized by varying promoter strength, ribosome binding site strength, and enzyme variant strength using chromosome-based and plasmid-based constructs.
To optimize resistance induction, we vary promoter, ribosome binding site, and enzyme variant strength using chromosome and plasmid-based constructs.
Resistance induction was optimized by varying promoter strength, ribosome binding site strength, and enzyme variant strength using chromosome-based and plasmid-based constructs.
To optimize resistance induction, we vary promoter, ribosome binding site, and enzyme variant strength using chromosome and plasmid-based constructs.
Resistance induction was optimized by varying promoter strength, ribosome binding site strength, and enzyme variant strength using chromosome-based and plasmid-based constructs.
To optimize resistance induction, we vary promoter, ribosome binding site, and enzyme variant strength using chromosome and plasmid-based constructs.
Resistance induction was optimized by varying promoter strength, ribosome binding site strength, and enzyme variant strength using chromosome-based and plasmid-based constructs.
To optimize resistance induction, we vary promoter, ribosome binding site, and enzyme variant strength using chromosome and plasmid-based constructs.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in yeast and allowed light control of beta-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and allowed light control of beta-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and allowed light control of beta-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and allowed light control of beta-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and allowed light control of beta-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and allowed light control of beta-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and allowed light control of beta-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split-unit Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split-unit Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split-unit Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split-unit Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split-unit Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split-unit Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split-unit Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant with destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant with destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant with destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant with destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant with destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant with destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant with destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
The N-terminal alphaA helix and C-terminal alphaN helix of Cre are critical for recombinase activity.
The stabilizing N-ter and C-ter α-helices of the Cre recombinase are critical for its activity.
The N-terminal alphaA helix and C-terminal alphaN helix of Cre are critical for recombinase activity.
The stabilizing N-ter and C-ter α-helices of the Cre recombinase are critical for its activity.
The N-terminal alphaA helix and C-terminal alphaN helix of Cre are critical for recombinase activity.
The stabilizing N-ter and C-ter α-helices of the Cre recombinase are critical for its activity.
The N-terminal alphaA helix and C-terminal alphaN helix of Cre are critical for recombinase activity.
The stabilizing N-ter and C-ter α-helices of the Cre recombinase are critical for its activity.
The N-terminal alphaA helix and C-terminal alphaN helix of Cre are critical for recombinase activity.
The stabilizing N-ter and C-ter α-helices of the Cre recombinase are critical for its activity.
The N-terminal alphaA helix and C-terminal alphaN helix of Cre are critical for recombinase activity.
The stabilizing N-ter and C-ter α-helices of the Cre recombinase are critical for its activity.
The N-terminal alphaA helix and C-terminal alphaN helix of Cre are critical for recombinase activity.
The stabilizing N-ter and C-ter α-helices of the Cre recombinase are critical for its activity.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
Approval Evidence
5 sources27 linked approval claimsfirst-pass slugs licre, light-inducible-cre-recombinase
Here, we use light-inducible Cre recombinase to activate expression of drug resistance genes in Escherichia coli.
Source:
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
Source:
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
Source:
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
Source:
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
Source:
capabilitysupports
The system demonstrated light-activated resistance to carbenicillin, kanamycin, chloramphenicol, and tetracycline.
We demonstrate light-activated resistance to four antibiotics: carbenicillin, kanamycin, chloramphenicol, and tetracycline.
Source:
conditional survivalsupports
Cells exposed to blue light survived in the presence of lethal antibiotic concentrations, whereas cells kept in the dark did not.
Cells exposed to blue light survive in the presence of lethal antibiotic concentrations, while those kept in the dark do not.
Source:
mechanismsupports
Light-inducible Cre recombinase was used to activate expression of drug resistance genes in Escherichia coli.
Here, we use light-inducible Cre recombinase to activate expression of drug resistance genes in Escherichia coli.
Source:
activation kineticssupports
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
Source:
activation propertysupports
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
Source:
applicationsupports
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
applicationsupports
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
application performancesupports
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
application performancesupports
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
Source:
comparative performancesupports
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Source:
comparative performancesupports
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Source:
compositionsupports
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
Source:
molecular compositionsupports
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
Source:
tool developmentsupports
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
Source:
activation propertysupports
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
Source:
activation responsesupports
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
Source:
applicationsupports
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
applicationsupports
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
Source:
applicationsupports
LiCre was efficient in yeast and allowed light control of beta-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
applicationsupports
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
Source:
Comparisons
Source-backed strengths
The evidence shows that LiCre supported light-activated resistance to carbenicillin, kanamycin, chloramphenicol, and tetracycline. Cells exposed to blue light survived lethal antibiotic concentrations whereas cells kept in the dark did not, indicating strong functional separation between illuminated and non-illuminated conditions in this assay context.
Source:
To optimize resistance induction, we vary promoter, ribosome binding site, and enzyme variant strength using chromosome and plasmid-based constructs.
Source:
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Source:
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Source:
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
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