Source 1primary paper2025
Toolkit/Avena sativa LOV2 domain variants
Avena sativa LOV2 domain variants
Also known as: LOV2 domain variants, optimized Avena sativa LOV2 domain variants
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Avena sativa LOV2 domain variants are engineered insertion modules used to build thermosensitive allosteric chimeric proteins. In Escherichia coli, insertion of optimized LOV2 variants into diverse, structurally and functionally unrelated proteins produced potent thermoswitchable variants operating within a narrow 37-41 °C range.
Usefulness & Problems
Why this is useful
These LOV2 domain variants provide a generalizable module for conferring temperature responsiveness onto otherwise unrelated proteins by allosteric insertion. The reported behavior in a physiologically relevant 37-41 °C window makes them useful for engineering protein activity control near bacterial growth and host-associated temperatures.
Source:
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
Problem solved
They address the challenge of engineering thermosensitive allosteric proteins in a modular way rather than requiring a bespoke redesign for each target protein. The source also indicates that thermosensing modules can be substituted, supporting the broader problem of portable temperature-control elements for protein engineering.
Source:
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
allosteric switchingallosteric switchingconformational uncagingconformational uncagingConformational UncagingTechniques
Structural CharacterizationTarget processes
No target processes tagged yet.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: actuatorswitch architecture: uncaging
Implementation is described as insertion of optimized Avena sativa LOV2 domain variants into target proteins to create thermosensitive allosteric chimeras. The available evidence supports use in Escherichia coli, but it does not specify construct architecture, linker design, cofactors, or expression requirements.
The supplied evidence is limited to demonstrations in Escherichia coli and does not specify the number of target proteins, quantitative switching metrics, reversibility, or performance in other organisms. The source also does not provide practical details on insertion sites, sequence changes in the optimized LOV2 variants, or comparative benchmarking against other thermosensing modules.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Observations
successBacteriaapplication demoEscherichia coli
Inferred from claim c2 during normalization. Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range. Derived from claim c2. Quoted text: Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
Source:
temperature control range(37-41)
successBacteriaapplication demoEscherichia coli
Inferred from claim c2 during normalization. Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range. Derived from claim c2. Quoted text: Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
Source:
temperature control range(37-41)
successBacteriaapplication demoEscherichia coli
Inferred from claim c2 during normalization. Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range. Derived from claim c2. Quoted text: Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
Source:
temperature control range(37-41)
successBacteriaapplication demoEscherichia coli
Inferred from claim c2 during normalization. Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range. Derived from claim c2. Quoted text: Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
Source:
temperature control range(37-41)
successBacteriaapplication demoEscherichia coli
Inferred from claim c2 during normalization. Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range. Derived from claim c2. Quoted text: Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
Source:
temperature control range(37-41)
successBacteriaapplication demoEscherichia coli
Inferred from claim c2 during normalization. Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range. Derived from claim c2. Quoted text: Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
Source:
temperature control range(37-41)
successBacteriaapplication demoEscherichia coli
Inferred from claim c2 during normalization. Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range. Derived from claim c2. Quoted text: Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
Source:
temperature control range(37-41)
Supporting Sources
Source 2primary paper2026Nature Chemical Biology
Ranked Claims
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
temperature control range 37-41 °C
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
A chemoreceptor domain can serve as an alternative thermosensing module, suggesting thermosensitivity may be widespread in receptor domains.
we showcase the incorporation of a chemoreceptor domain as an alternative thermosensing module, suggesting thermosensitivity to be a widespread feature in receptor domains
A chemoreceptor domain can serve as an alternative thermosensing module, suggesting thermosensitivity may be widespread in receptor domains.
we showcase the incorporation of a chemoreceptor domain as an alternative thermosensing module, suggesting thermosensitivity to be a widespread feature in receptor domains
A chemoreceptor domain can serve as an alternative thermosensing module, suggesting thermosensitivity may be widespread in receptor domains.
we showcase the incorporation of a chemoreceptor domain as an alternative thermosensing module, suggesting thermosensitivity to be a widespread feature in receptor domains
A chemoreceptor domain can serve as an alternative thermosensing module, suggesting thermosensitivity may be widespread in receptor domains.
we showcase the incorporation of a chemoreceptor domain as an alternative thermosensing module, suggesting thermosensitivity to be a widespread feature in receptor domains
A chemoreceptor domain can serve as an alternative thermosensing module, suggesting thermosensitivity may be widespread in receptor domains.
we showcase the incorporation of a chemoreceptor domain as an alternative thermosensing module, suggesting thermosensitivity to be a widespread feature in receptor domains
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
The authors engineered CRISPR-Cas genome editors in mammalian systems that are directly modulated by subtle temperature changes within the physiological range.
Extending this strategy to mammalian systems, we engineered the first CRISPR-Cas genome editors directly modulated by subtle temperature changes within the physiological range.
The authors engineered CRISPR-Cas genome editors in mammalian systems that are directly modulated by subtle temperature changes within the physiological range.
Extending this strategy to mammalian systems, we engineered the first CRISPR-Cas genome editors directly modulated by subtle temperature changes within the physiological range.
The authors engineered CRISPR-Cas genome editors in mammalian systems that are directly modulated by subtle temperature changes within the physiological range.
Extending this strategy to mammalian systems, we engineered the first CRISPR-Cas genome editors directly modulated by subtle temperature changes within the physiological range.
The authors engineered CRISPR-Cas genome editors in mammalian systems that are directly modulated by subtle temperature changes within the physiological range.
Extending this strategy to mammalian systems, we engineered the first CRISPR-Cas genome editors directly modulated by subtle temperature changes within the physiological range.
The authors engineered CRISPR-Cas genome editors in mammalian systems that are directly modulated by subtle temperature changes within the physiological range.
Extending this strategy to mammalian systems, we engineered the first CRISPR-Cas genome editors directly modulated by subtle temperature changes within the physiological range.
The authors engineered CRISPR-Cas genome editors in mammalian systems that are directly modulated by subtle temperature changes within the physiological range.
Extending this strategy to mammalian systems, we engineered the first CRISPR-Cas genome editors directly modulated by subtle temperature changes within the physiological range.
The authors engineered CRISPR-Cas genome editors in mammalian systems that are directly modulated by subtle temperature changes within the physiological range.
Extending this strategy to mammalian systems, we engineered the first CRISPR-Cas genome editors directly modulated by subtle temperature changes within the physiological range.
The authors engineered CRISPR-Cas genome editors in mammalian systems that are directly modulated by subtle temperature changes within the physiological range.
Extending this strategy to mammalian systems, we engineered the first CRISPR-Cas genome editors directly modulated by subtle temperature changes within the physiological range.
The authors engineered CRISPR-Cas genome editors in mammalian systems that are directly modulated by subtle temperature changes within the physiological range.
Extending this strategy to mammalian systems, we engineered the first CRISPR-Cas genome editors directly modulated by subtle temperature changes within the physiological range.
The authors engineered CRISPR-Cas genome editors in mammalian systems that are directly modulated by subtle temperature changes within the physiological range.
Extending this strategy to mammalian systems, we engineered the first CRISPR-Cas genome editors directly modulated by subtle temperature changes within the physiological range.
A chemoreceptor domain can serve as an alternative thermosensing module, suggesting thermo-sensitivity may be widespread in receptor domains.
we showcase the incorporation of a chemoreceptor domain as an alternative thermosensing module, suggesting thermo-sensitivity to be a widespread feature in receptor domains
A chemoreceptor domain can serve as an alternative thermosensing module, suggesting thermo-sensitivity may be widespread in receptor domains.
we showcase the incorporation of a chemoreceptor domain as an alternative thermosensing module, suggesting thermo-sensitivity to be a widespread feature in receptor domains
A chemoreceptor domain can serve as an alternative thermosensing module, suggesting thermo-sensitivity may be widespread in receptor domains.
we showcase the incorporation of a chemoreceptor domain as an alternative thermosensing module, suggesting thermo-sensitivity to be a widespread feature in receptor domains
A chemoreceptor domain can serve as an alternative thermosensing module, suggesting thermo-sensitivity may be widespread in receptor domains.
we showcase the incorporation of a chemoreceptor domain as an alternative thermosensing module, suggesting thermo-sensitivity to be a widespread feature in receptor domains
A chemoreceptor domain can serve as an alternative thermosensing module, suggesting thermo-sensitivity may be widespread in receptor domains.
we showcase the incorporation of a chemoreceptor domain as an alternative thermosensing module, suggesting thermo-sensitivity to be a widespread feature in receptor domains
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
Approval Evidence
2 sources5 linked approval claimsfirst-pass slug avena-sativa-lov2-domain-variants
through the insertion of optimized Avena sativa LOV2 domain variants
Source:
through the insertion of optimized Avena sativa LOV2 domain variants
Source:
application resultsupports
Applying the LOV2-based strategy to diverse structurally and functionally unrelated proteins in Escherichia coli generated potent thermoswitchable chimeric variants controllable within a narrow 37-41 °C temperature range.
Applying this approach to a diverse set of structurally and functionally unrelated proteins in Escherichia coli, we generated potent, thermoswitchable chimeric variants that can be tightly controlled within narrow temperature ranges (37-41 °C).
Source:
engineering strategysupports
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
Source:
toolkit expansionsupports
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
Source:
engineering strategysupports
The paper presents a generalizable strategy for engineering thermosensitive allosteric proteins by inserting optimized Avena sativa LOV2 domain variants.
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
Source:
scope statementsupports
This work expands the thermogenetics toolkit and provides a blueprint for temperature-dependent control of virtually any protein of interest.
This work expands the toolkit of thermogenetics, providing a blueprint for temperature-dependent control of virtually any protein of interest.
Source:
Comparisons
Source-backed strengths
The reported strategy was applied to diverse structurally and functionally unrelated proteins, supporting modularity across multiple protein contexts. The resulting chimeras were described as potent thermoswitchable variants with control confined to a narrow 37-41 °C range in E. coli.
Source:
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
Source:
we present a generalizable strategy for engineering thermosensitive allosteric proteins through the insertion of optimized Avena sativa LOV2 domain variants
Compared with CIB1 helix 10 pocket
Avena sativa LOV2 domain variants and CIB1 helix 10 pocket address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: conformational uncaging, conformational_uncaging
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with CRY2 C-terminal tail
Avena sativa LOV2 domain variants and CRY2 C-terminal tail address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: allosteric switching
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with Diaphanous Autoregulatory Domain from mDia1
Avena sativa LOV2 domain variants and Diaphanous Autoregulatory Domain from mDia1 address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: allosteric switching
Strengths here: appears more independently replicated; looks easier to implement in practice.
Ranked Citations
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- 2.