Source 1primary paper2023ACS Chemical Biology
Toolkit/allosteric Cre regulation with NS3 ligands
allosteric Cre regulation with NS3 ligands
Also known as: allosteric Cre regulation, orthogonal recombination tools
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Allosteric Cre regulation with NS3 ligands is a chemical multi-component recombination switch in which an NS3-based ligand-responsive system is used to allosterically regulate Cre recombinase. It was reported as an orthogonal recombination control strategy in eukaryotic cells and as a way to control prokaryotic recombinase activity across divergent organisms.
Usefulness & Problems
Why this is useful
This tool provides chemical control over site-specific recombination using an NS3 ligand-responsive architecture rather than relying on standard recombinase control schemes. The reported value is orthogonal regulation of recombination in eukaryotic cells and portability to control prokaryotic recombinase activity in divergent organisms.
Problem solved
It addresses the problem of achieving orthogonal, ligand-responsive control of Cre recombinase activity through a newly developed allosteric mechanism. The available evidence indicates recombination control in both eukaryotic contexts and across divergent organisms, but does not provide more granular application details.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
allosteric switchingconformational uncagingConformational Uncagingdrug-induced complex displacementTechniques
No technique tags yet.
Target processes
recombinationInput: Chemical
Implementation Constraints
The system is NS3-based and chemically responsive, and related evidence states that NS3-peptide complexes can be displaced by FDA-approved drugs in other control modalities. However, the provided evidence for this specific Cre tool does not detail construct design, expression system, ligand dosing, or delivery requirements.
The supplied evidence does not specify the exact NS3 construct architecture, the identity of the drugs used in the Cre-regulation configuration, or quantitative performance metrics such as dynamic range, leakiness, or kinetics. Independent replication and detailed validation across cell types or in vivo settings are not documented in the provided material.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
Approval Evidence
1 source2 linked approval claimsfirst-pass slug allosteric-cre-regulation-with-ns3-ligands
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase. Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells
Source:
functional scopesupports
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Source:
mechanism inventionsupports
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
Source:
Comparisons
Source-backed strengths
The source explicitly states that the system introduced a new mechanism for allosteric regulation of Cre recombinase. It also reports functional scope spanning orthogonal recombination tools in eukaryotic cells and control of prokaryotic recombinase activity across divergent organisms.
Ranked Citations
- 1.