Source 1primary paper2016DukeSpace (Duke University)
Toolkit/oligomerizing CRY2 component
oligomerizing CRY2 component
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The oligomerizing CRY2 component is a modified CRY2-based optogenetic construct tested in Drosophila melanogaster as a tool for negative regulation of targeted proteins. The available evidence indicates that it was evaluated in the context of adapting CRY2/CIB optogenetic components to Drosophila-specific constructs.
Usefulness & Problems
Why this is useful
This construct is useful as a light-responsive module for perturbing protein function in Drosophila. The cited work specifically positions the oligomerizing CRY2 variant as a candidate tool for negative regulation of targeted proteins, potentially enabling temporal and spatial control when integrated into CRY2/CIB-based designs.
Problem solved
It addresses the problem of achieving optogenetic negative regulation of specific proteins in Drosophila. More specifically, the source describes efforts to adapt the CRY2/CIB system into Drosophila-specific vectors, indicating a need for organism-compatible light-controlled protein regulation tools.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A reusable architecture pattern for arranging parts into an engineered system.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: actuatorswitch architecture: recruitment
The source indicates that CRY2 and CIB constructs were adapted into Drosophila-specific vectors, which is the main practical implementation detail available. Blue light is implicated in CRY2/CIB control in the same study context, and fusion of target proteins to CRY2 is discussed, but the exact design of the oligomerizing CRY2 construct is not described in the provided evidence.
The evidence does not report quantitative data on light response, reversibility, dynamic range, kinetics, or target specificity for this construct. It also does not identify the exact CRY2 variant, fusion architecture, illumination parameters, or the targeted proteins used for negative regulation.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The authors attempted to adapt the CRY2/CIB system to Drosophila using CRY2 and CIB constructs in Drosophila-specific vectors.
Using cloning techniques to generate CRY2 and CIB constructs in Drosophila specific vectors, we have attempted to adapt the CRY2/CIB system to Drosophila.
The authors attempted to adapt the CRY2/CIB system to Drosophila using CRY2 and CIB constructs in Drosophila-specific vectors.
Using cloning techniques to generate CRY2 and CIB constructs in Drosophila specific vectors, we have attempted to adapt the CRY2/CIB system to Drosophila.
The authors attempted to adapt the CRY2/CIB system to Drosophila using CRY2 and CIB constructs in Drosophila-specific vectors.
Using cloning techniques to generate CRY2 and CIB constructs in Drosophila specific vectors, we have attempted to adapt the CRY2/CIB system to Drosophila.
The authors attempted to adapt the CRY2/CIB system to Drosophila using CRY2 and CIB constructs in Drosophila-specific vectors.
Using cloning techniques to generate CRY2 and CIB constructs in Drosophila specific vectors, we have attempted to adapt the CRY2/CIB system to Drosophila.
The authors attempted to adapt the CRY2/CIB system to Drosophila using CRY2 and CIB constructs in Drosophila-specific vectors.
Using cloning techniques to generate CRY2 and CIB constructs in Drosophila specific vectors, we have attempted to adapt the CRY2/CIB system to Drosophila.
The authors attempted to adapt the CRY2/CIB system to Drosophila using CRY2 and CIB constructs in Drosophila-specific vectors.
Using cloning techniques to generate CRY2 and CIB constructs in Drosophila specific vectors, we have attempted to adapt the CRY2/CIB system to Drosophila.
The authors attempted to adapt the CRY2/CIB system to Drosophila using CRY2 and CIB constructs in Drosophila-specific vectors.
Using cloning techniques to generate CRY2 and CIB constructs in Drosophila specific vectors, we have attempted to adapt the CRY2/CIB system to Drosophila.
The authors attempted to adapt the CRY2/CIB system to Drosophila using CRY2 and CIB constructs in Drosophila-specific vectors.
Using cloning techniques to generate CRY2 and CIB constructs in Drosophila specific vectors, we have attempted to adapt the CRY2/CIB system to Drosophila.
The authors attempted to adapt the CRY2/CIB system to Drosophila using CRY2 and CIB constructs in Drosophila-specific vectors.
Using cloning techniques to generate CRY2 and CIB constructs in Drosophila specific vectors, we have attempted to adapt the CRY2/CIB system to Drosophila.
The authors attempted to adapt the CRY2/CIB system to Drosophila using CRY2 and CIB constructs in Drosophila-specific vectors.
Using cloning techniques to generate CRY2 and CIB constructs in Drosophila specific vectors, we have attempted to adapt the CRY2/CIB system to Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
If Rho1 is successfully fused to CRY2, blue light could spatially and temporally control recruitment of CRY2 to membrane-anchored CIB and thereby affect downstream events.
If Drosophila Rho1 proteins are successfully adapted to CRY2 components, upon blue light stimulation the recruitment of CRY2 to a CIB component anchored in the membrane could be spatially and temporally controlled to affect subsequent downstream events.
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
The light activation protocol was sensitive to inadvertent light stimulation during preparation for imaging.
discovered the sensitivity of the system to inadvertent light stimulation during preparation for imaging
The light activation protocol was sensitive to inadvertent light stimulation during preparation for imaging.
discovered the sensitivity of the system to inadvertent light stimulation during preparation for imaging
The light activation protocol was sensitive to inadvertent light stimulation during preparation for imaging.
discovered the sensitivity of the system to inadvertent light stimulation during preparation for imaging
The light activation protocol was sensitive to inadvertent light stimulation during preparation for imaging.
discovered the sensitivity of the system to inadvertent light stimulation during preparation for imaging
The light activation protocol was sensitive to inadvertent light stimulation during preparation for imaging.
discovered the sensitivity of the system to inadvertent light stimulation during preparation for imaging
The light activation protocol was sensitive to inadvertent light stimulation during preparation for imaging.
discovered the sensitivity of the system to inadvertent light stimulation during preparation for imaging
The light activation protocol was sensitive to inadvertent light stimulation during preparation for imaging.
discovered the sensitivity of the system to inadvertent light stimulation during preparation for imaging
The light activation protocol was sensitive to inadvertent light stimulation during preparation for imaging.
discovered the sensitivity of the system to inadvertent light stimulation during preparation for imaging
The light activation protocol was sensitive to inadvertent light stimulation during preparation for imaging.
discovered the sensitivity of the system to inadvertent light stimulation during preparation for imaging
The light activation protocol was sensitive to inadvertent light stimulation during preparation for imaging.
discovered the sensitivity of the system to inadvertent light stimulation during preparation for imaging
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Germline transformants of the CIBN component had been generated, while CRY2 germline transformants were still in progress.
Thus far, germline transformants of the CIBN component have been generated, and work will continue to generate the CRY2 germline transformants.
Blue light stimuli can selectively initiate protein-protein interactions in genetically encoded light-sensitive protein systems.
using blue light stimuli to selectively initiate protein-protein interactions
Blue light stimuli can selectively initiate protein-protein interactions in genetically encoded light-sensitive protein systems.
using blue light stimuli to selectively initiate protein-protein interactions
Blue light stimuli can selectively initiate protein-protein interactions in genetically encoded light-sensitive protein systems.
using blue light stimuli to selectively initiate protein-protein interactions
Blue light stimuli can selectively initiate protein-protein interactions in genetically encoded light-sensitive protein systems.
using blue light stimuli to selectively initiate protein-protein interactions
Blue light stimuli can selectively initiate protein-protein interactions in genetically encoded light-sensitive protein systems.
using blue light stimuli to selectively initiate protein-protein interactions
Blue light stimuli can selectively initiate protein-protein interactions in genetically encoded light-sensitive protein systems.
using blue light stimuli to selectively initiate protein-protein interactions
Blue light stimuli can selectively initiate protein-protein interactions in genetically encoded light-sensitive protein systems.
using blue light stimuli to selectively initiate protein-protein interactions
Blue light stimuli can selectively initiate protein-protein interactions in genetically encoded light-sensitive protein systems.
using blue light stimuli to selectively initiate protein-protein interactions
Blue light stimuli can selectively initiate protein-protein interactions in genetically encoded light-sensitive protein systems.
using blue light stimuli to selectively initiate protein-protein interactions
Blue light stimuli can selectively initiate protein-protein interactions in genetically encoded light-sensitive protein systems.
using blue light stimuli to selectively initiate protein-protein interactions
The CRY2/CIB module offers a genetically encoded mechanism to study protein roles in a tissue-specific manner during development.
the CRY2/CIB module, offers a powerful genetically encoded mechanism by which to study the role of proteins in a tissue-specific manner during various stages of development
The CRY2/CIB module offers a genetically encoded mechanism to study protein roles in a tissue-specific manner during development.
the CRY2/CIB module, offers a powerful genetically encoded mechanism by which to study the role of proteins in a tissue-specific manner during various stages of development
The CRY2/CIB module offers a genetically encoded mechanism to study protein roles in a tissue-specific manner during development.
the CRY2/CIB module, offers a powerful genetically encoded mechanism by which to study the role of proteins in a tissue-specific manner during various stages of development
The CRY2/CIB module offers a genetically encoded mechanism to study protein roles in a tissue-specific manner during development.
the CRY2/CIB module, offers a powerful genetically encoded mechanism by which to study the role of proteins in a tissue-specific manner during various stages of development
The CRY2/CIB module offers a genetically encoded mechanism to study protein roles in a tissue-specific manner during development.
the CRY2/CIB module, offers a powerful genetically encoded mechanism by which to study the role of proteins in a tissue-specific manner during various stages of development
The CRY2/CIB module offers a genetically encoded mechanism to study protein roles in a tissue-specific manner during development.
the CRY2/CIB module, offers a powerful genetically encoded mechanism by which to study the role of proteins in a tissue-specific manner during various stages of development
The CRY2/CIB module offers a genetically encoded mechanism to study protein roles in a tissue-specific manner during development.
the CRY2/CIB module, offers a powerful genetically encoded mechanism by which to study the role of proteins in a tissue-specific manner during various stages of development
The CRY2/CIB module offers a genetically encoded mechanism to study protein roles in a tissue-specific manner during development.
the CRY2/CIB module, offers a powerful genetically encoded mechanism by which to study the role of proteins in a tissue-specific manner during various stages of development
The CRY2/CIB module offers a genetically encoded mechanism to study protein roles in a tissue-specific manner during development.
the CRY2/CIB module, offers a powerful genetically encoded mechanism by which to study the role of proteins in a tissue-specific manner during various stages of development
The CRY2/CIB module offers a genetically encoded mechanism to study protein roles in a tissue-specific manner during development.
the CRY2/CIB module, offers a powerful genetically encoded mechanism by which to study the role of proteins in a tissue-specific manner during various stages of development
Approval Evidence
1 source2 linked approval claimsfirst-pass slug oligomerizing-cry2-component
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
Source:
intended functionsupports
An oligomerizing version of CRY2 was tested as a tool for negative regulation of targeted proteins in Drosophila.
We tested an oligomerizing version of the CRY2 component as a tool for the negative regulation of targeted proteins in Drosophila.
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negative resultcontradicts
The authors were unable to repeat in Drosophila the clustering results previously observed in yeast for the oligomerizing CRY2 component.
Although we were unable to repeat the clustering results observed in yeast
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Comparisons
Source-backed strengths
The main demonstrated strength is that an oligomerizing CRY2 version was tested in the Drosophila context rather than only proposed in principle. The broader source also supports compatibility of CRY2/CIB-based construct adaptation to Drosophila-specific vectors, but no quantitative performance metrics are provided for the oligomerizing variant itself.
Source:
Using cloning techniques to generate CRY2 and CIB constructs in Drosophila specific vectors, we have attempted to adapt the CRY2/CIB system to Drosophila.
Compared with optogenetic Amyloid-b2 peptide
oligomerizing CRY2 component and optogenetic Amyloid-b2 peptide address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: oligomerization
Strengths here: looks easier to implement in practice.
Compared with optogenetic zebrafish ALS model
oligomerizing CRY2 component and optogenetic zebrafish ALS model address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: oligomerization
Strengths here: looks easier to implement in practice.
Compared with Q-PAS1
oligomerizing CRY2 component and Q-PAS1 address a similar problem space.
Shared frame: shared mechanisms: oligomerization
Ranked Citations
- 1.