Source 1primary paper2018Warwick Research Archive Portal (University of Warwick)
Toolkit/FerriTag
FerriTag
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
FerriTag is a genetically encoded, chemically inducible tag for correlative light-electron microscopy built as a fluorescent, electron-dense ferritin particle. It labels target proteins through induced heterodimerization and enables nanoscale localization in electron micrographs.
Usefulness & Problems
Why this is useful
FerriTag is useful for correlative light-electron microscopy because it provides an electron-dense label that is distinguishable from background in electron micrographs while remaining genetically encoded. The reported application is contextual nanoscale mapping of protein location relative to subcellular structures.
Source:
FerriTag can be used to perform contextual nanoscale mapping of protein location relative to a subcellular structure.
Source:
This was utilised to study the distribution and conformation of huntingtin-interacting protein 1 related (HIP1R) in and around clathrin-coated pits, providing insight to the roles played by HIP1R, clathrin and actin during clathrin-mediated endocytosis.
Source:
This thesis introduces FerriTag, a new genetically-encoded chemically-inducible tag for correlative light-electron microscopy.
Problem solved
FerriTag addresses the problem of localizing specific proteins at nanoscale resolution in electron microscopy using a genetically encoded tag. The cited work specifically positions it as a solution for mapping protein location relative to cellular ultrastructure and for analyzing proteins such as HIP1R around clathrin-coated pits.
Source:
FerriTag can be used to perform contextual nanoscale mapping of protein location relative to a subcellular structure.
Source:
This was utilised to study the distribution and conformation of huntingtin-interacting protein 1 related (HIP1R) in and around clathrin-coated pits, providing insight to the roles played by HIP1R, clathrin and actin during clathrin-mediated endocytosis.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Implementation Constraints
The tool is described as genetically encoded, chemically inducible, and based on a fluorescent ferritin particle for correlative light-electron microscopy. The current summary states that labeling is achieved through rapamycin-induced heterodimerization, but the provided extraction text does not add further construct-level or expression details.
The supplied evidence comes from a single thesis source and provides limited detail on performance across targets, cell types, or experimental systems. Practical constraints of the chemically inducible system, ferritin assembly, and any effects on target protein function are not described in the provided evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
FerriTag can be used for contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used to perform contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used for contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used to perform contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used for contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used to perform contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used for contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used to perform contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used for contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used to perform contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used for contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used to perform contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used for contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used to perform contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag was used to study the distribution and conformation of HIP1R in and around clathrin-coated pits.
This was utilised to study the distribution and conformation of huntingtin-interacting protein 1 related (HIP1R) in and around clathrin-coated pits, providing insight to the roles played by HIP1R, clathrin and actin during clathrin-mediated endocytosis.
FerriTag was used to study the distribution and conformation of HIP1R in and around clathrin-coated pits.
This was utilised to study the distribution and conformation of huntingtin-interacting protein 1 related (HIP1R) in and around clathrin-coated pits, providing insight to the roles played by HIP1R, clathrin and actin during clathrin-mediated endocytosis.
FerriTag was used to study the distribution and conformation of HIP1R in and around clathrin-coated pits.
This was utilised to study the distribution and conformation of huntingtin-interacting protein 1 related (HIP1R) in and around clathrin-coated pits, providing insight to the roles played by HIP1R, clathrin and actin during clathrin-mediated endocytosis.
FerriTag was used to study the distribution and conformation of HIP1R in and around clathrin-coated pits.
This was utilised to study the distribution and conformation of huntingtin-interacting protein 1 related (HIP1R) in and around clathrin-coated pits, providing insight to the roles played by HIP1R, clathrin and actin during clathrin-mediated endocytosis.
FerriTag was used to study the distribution and conformation of HIP1R in and around clathrin-coated pits.
This was utilised to study the distribution and conformation of huntingtin-interacting protein 1 related (HIP1R) in and around clathrin-coated pits, providing insight to the roles played by HIP1R, clathrin and actin during clathrin-mediated endocytosis.
FerriTag was used to study the distribution and conformation of HIP1R in and around clathrin-coated pits.
This was utilised to study the distribution and conformation of huntingtin-interacting protein 1 related (HIP1R) in and around clathrin-coated pits, providing insight to the roles played by HIP1R, clathrin and actin during clathrin-mediated endocytosis.
FerriTag was used to study the distribution and conformation of HIP1R in and around clathrin-coated pits.
This was utilised to study the distribution and conformation of huntingtin-interacting protein 1 related (HIP1R) in and around clathrin-coated pits, providing insight to the roles played by HIP1R, clathrin and actin during clathrin-mediated endocytosis.
FerriTag is distinguishable from background in electron micrographs due to high signal to noise ratio and provides a labeling resolution of 10 ± 5 nm.
FerriTag is easily distinguished from background in electron micrographs due to its high signal to noise ratio and also provides a labelling resolution of 10 ± 5 nm.
labeling resolution 10 ± 5 nm
FerriTag is distinguishable from background in electron micrographs due to high signal to noise ratio and provides a labeling resolution of 10 ± 5 nm.
FerriTag is easily distinguished from background in electron micrographs due to its high signal to noise ratio and also provides a labelling resolution of 10 ± 5 nm.
labeling resolution 10 ± 5 nm
FerriTag is distinguishable from background in electron micrographs due to high signal to noise ratio and provides a labeling resolution of 10 ± 5 nm.
FerriTag is easily distinguished from background in electron micrographs due to its high signal to noise ratio and also provides a labelling resolution of 10 ± 5 nm.
labeling resolution 10 ± 5 nm
FerriTag is distinguishable from background in electron micrographs due to high signal to noise ratio and provides a labeling resolution of 10 ± 5 nm.
FerriTag is easily distinguished from background in electron micrographs due to its high signal to noise ratio and also provides a labelling resolution of 10 ± 5 nm.
labeling resolution 10 ± 5 nm
FerriTag is distinguishable from background in electron micrographs due to high signal to noise ratio and provides a labeling resolution of 10 ± 5 nm.
FerriTag is easily distinguished from background in electron micrographs due to its high signal to noise ratio and also provides a labelling resolution of 10 ± 5 nm.
labeling resolution 10 ± 5 nm
FerriTag is distinguishable from background in electron micrographs due to high signal to noise ratio and provides a labeling resolution of 10 ± 5 nm.
FerriTag is easily distinguished from background in electron micrographs due to its high signal to noise ratio and also provides a labelling resolution of 10 ± 5 nm.
labeling resolution 10 ± 5 nm
FerriTag is distinguishable from background in electron micrographs due to high signal to noise ratio and provides a labeling resolution of 10 ± 5 nm.
FerriTag is easily distinguished from background in electron micrographs due to its high signal to noise ratio and also provides a labelling resolution of 10 ± 5 nm.
labeling resolution 10 ± 5 nm
FerriTag is a fluorescent recombinant electron-dense ferritin particle that labels target proteins using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron- dense ferritin particle that can specifically label target proteins rapidly and efficiently using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron-dense ferritin particle that labels target proteins using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron- dense ferritin particle that can specifically label target proteins rapidly and efficiently using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron-dense ferritin particle that labels target proteins using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron- dense ferritin particle that can specifically label target proteins rapidly and efficiently using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron-dense ferritin particle that labels target proteins using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron- dense ferritin particle that can specifically label target proteins rapidly and efficiently using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron-dense ferritin particle that labels target proteins using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron- dense ferritin particle that can specifically label target proteins rapidly and efficiently using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron-dense ferritin particle that labels target proteins using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron- dense ferritin particle that can specifically label target proteins rapidly and efficiently using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron-dense ferritin particle that labels target proteins using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron- dense ferritin particle that can specifically label target proteins rapidly and efficiently using rapamycin-induced heterodimerization.
The described CLEM processing protocol is simple, robust, and potentially usable for tagging any protein of interest.
The processing protocol described for CLEM is simple yet robust and can potentially be used for tagging any protein-of- interest.
The described CLEM processing protocol is simple, robust, and potentially usable for tagging any protein of interest.
The processing protocol described for CLEM is simple yet robust and can potentially be used for tagging any protein-of- interest.
The described CLEM processing protocol is simple, robust, and potentially usable for tagging any protein of interest.
The processing protocol described for CLEM is simple yet robust and can potentially be used for tagging any protein-of- interest.
The described CLEM processing protocol is simple, robust, and potentially usable for tagging any protein of interest.
The processing protocol described for CLEM is simple yet robust and can potentially be used for tagging any protein-of- interest.
The described CLEM processing protocol is simple, robust, and potentially usable for tagging any protein of interest.
The processing protocol described for CLEM is simple yet robust and can potentially be used for tagging any protein-of- interest.
The described CLEM processing protocol is simple, robust, and potentially usable for tagging any protein of interest.
The processing protocol described for CLEM is simple yet robust and can potentially be used for tagging any protein-of- interest.
The described CLEM processing protocol is simple, robust, and potentially usable for tagging any protein of interest.
The processing protocol described for CLEM is simple yet robust and can potentially be used for tagging any protein-of- interest.
FerriTag is a new genetically encoded chemically inducible tag for correlative light-electron microscopy.
This thesis introduces FerriTag, a new genetically-encoded chemically-inducible tag for correlative light-electron microscopy.
FerriTag is a new genetically encoded chemically inducible tag for correlative light-electron microscopy.
This thesis introduces FerriTag, a new genetically-encoded chemically-inducible tag for correlative light-electron microscopy.
FerriTag is a new genetically encoded chemically inducible tag for correlative light-electron microscopy.
This thesis introduces FerriTag, a new genetically-encoded chemically-inducible tag for correlative light-electron microscopy.
FerriTag is a new genetically encoded chemically inducible tag for correlative light-electron microscopy.
This thesis introduces FerriTag, a new genetically-encoded chemically-inducible tag for correlative light-electron microscopy.
FerriTag is a new genetically encoded chemically inducible tag for correlative light-electron microscopy.
This thesis introduces FerriTag, a new genetically-encoded chemically-inducible tag for correlative light-electron microscopy.
FerriTag is a new genetically encoded chemically inducible tag for correlative light-electron microscopy.
This thesis introduces FerriTag, a new genetically-encoded chemically-inducible tag for correlative light-electron microscopy.
FerriTag is a new genetically encoded chemically inducible tag for correlative light-electron microscopy.
This thesis introduces FerriTag, a new genetically-encoded chemically-inducible tag for correlative light-electron microscopy.
Approval Evidence
1 source6 linked approval claimsfirst-pass slug ferritag
This thesis introduces FerriTag, a new genetically-encoded chemically-inducible tag for correlative light-electron microscopy.
Source:
application capabilitysupports
FerriTag can be used for contextual nanoscale mapping of protein location relative to a subcellular structure.
FerriTag can be used to perform contextual nanoscale mapping of protein location relative to a subcellular structure.
Source:
application examplesupports
FerriTag was used to study the distribution and conformation of HIP1R in and around clathrin-coated pits.
This was utilised to study the distribution and conformation of huntingtin-interacting protein 1 related (HIP1R) in and around clathrin-coated pits, providing insight to the roles played by HIP1R, clathrin and actin during clathrin-mediated endocytosis.
Source:
imaging performancesupports
FerriTag is distinguishable from background in electron micrographs due to high signal to noise ratio and provides a labeling resolution of 10 ± 5 nm.
FerriTag is easily distinguished from background in electron micrographs due to its high signal to noise ratio and also provides a labelling resolution of 10 ± 5 nm.
Source:
mechanism descriptionsupports
FerriTag is a fluorescent recombinant electron-dense ferritin particle that labels target proteins using rapamycin-induced heterodimerization.
FerriTag is a fluorescent recombinant electron- dense ferritin particle that can specifically label target proteins rapidly and efficiently using rapamycin-induced heterodimerization.
Source:
protocol propertysupports
The described CLEM processing protocol is simple, robust, and potentially usable for tagging any protein of interest.
The processing protocol described for CLEM is simple yet robust and can potentially be used for tagging any protein-of- interest.
Source:
tool introductionsupports
FerriTag is a new genetically encoded chemically inducible tag for correlative light-electron microscopy.
This thesis introduces FerriTag, a new genetically-encoded chemically-inducible tag for correlative light-electron microscopy.
Source:
Comparisons
Source-backed strengths
The source reports that FerriTag has a high signal-to-noise ratio in electron micrographs and a labeling resolution of 10 ± 5 nm. It was also applied to study the distribution and conformation of HIP1R in and around clathrin-coated pits, supporting utility in contextual nanoscale mapping.
Ranked Citations
- 1.