2022
|
An expanded palette of fluorogenic HaloTag probes with enhanced contrast for targeted cellular imaging Article de journal Sylvestre P J T Bachollet; Yuriy Shpinov; Fanny Broch; Hela Benaissa; Arnaud Gautier; Nicolas Pietrancosta; Jean-Maurice Mallet; Blaise Dumat Organic & Biomolecular Chemistry, 20 (17), p. 3619 - 3628, 2022, ISSN: 1477-0520. @article{Bachollet2022,
title = {An expanded palette of fluorogenic HaloTag probes with enhanced contrast for targeted cellular imaging},
author = {Sylvestre P J T Bachollet and Yuriy Shpinov and Fanny Broch and Hela Benaissa and Arnaud Gautier and Nicolas Pietrancosta and Jean-Maurice Mallet and Blaise Dumat},
url = {http://xlink.rsc.org/?DOI=D1OB02394B},
doi = {10.1039/D1OB02394B},
issn = {1477-0520},
year = {2022},
date = {2022-01-01},
journal = {Organic & Biomolecular Chemistry},
volume = {20},
number = {17},
pages = {3619 - 3628},
publisher = {Royal Society of Chemistry},
abstract = {A palette of fluorogenic molecular rotor probes with emissions from green to NIR was developed for wash-free and multicolor imaging of genetically-encoded HaloTag fusion proteins.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
A palette of fluorogenic molecular rotor probes with emissions from green to NIR was developed for wash-free and multicolor imaging of genetically-encoded HaloTag fusion proteins. |
2019
|
A split fluorescent reporter with rapid and reversible complementation Article de journal Alison G Tebo; Arnaud Gautier Nature Communications, 10 (1), p. 2822, 2019, ISSN: 2041-1723. @article{Tebo2019,
title = {A split fluorescent reporter with rapid and reversible complementation},
author = {Alison G Tebo and Arnaud Gautier},
url = {https://doi.org/10.1038/s41467-019-10855-0},
doi = {10.1038/s41467-019-10855-0},
issn = {2041-1723},
year = {2019},
date = {2019-01-01},
journal = {Nature Communications},
volume = {10},
number = {1},
pages = {2822},
abstract = {Interactions between proteins play an essential role in metabolic and signaling pathways, cellular processes and organismal systems. We report the development of splitFAST, a fluorescence complementation system for the visualization of transient protein-protein interactions in living cells. Engineered from the fluorogenic reporter FAST (Fluorescence-Activating and absorption-Shifting Tag), which specifically and reversibly binds fluorogenic hydroxybenzylidene rhodanine (HBR) analogs, splitFAST displays rapid and reversible complementation, allowing the real-time visualization of both the formation and the dissociation of a protein assembly.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Interactions between proteins play an essential role in metabolic and signaling pathways, cellular processes and organismal systems. We report the development of splitFAST, a fluorescence complementation system for the visualization of transient protein-protein interactions in living cells. Engineered from the fluorogenic reporter FAST (Fluorescence-Activating and absorption-Shifting Tag), which specifically and reversibly binds fluorogenic hydroxybenzylidene rhodanine (HBR) analogs, splitFAST displays rapid and reversible complementation, allowing the real-time visualization of both the formation and the dissociation of a protein assembly. |
Live Cell Super Resolution Imaging by Radial Fluctuations Using Fluorogen Binding Tags Article de journal Muthukumaran Venkatachalapathy; Vivek Belapurkar; Mini Jose; Arnaud Gautier; Deepak Nair Nanoscale, 11 (8), p. 3626-3632, 2019, ISSN: 2040-3364. @article{RN45,
title = {Live Cell Super Resolution Imaging by Radial Fluctuations Using Fluorogen Binding Tags},
author = {Muthukumaran Venkatachalapathy and Vivek Belapurkar and Mini Jose and Arnaud Gautier and Deepak Nair},
doi = {10.1039/C8NR07809B},
issn = {2040-3364},
year = {2019},
date = {2019-01-01},
journal = {Nanoscale},
volume = {11},
number = {8},
pages = {3626-3632},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Single-Molecule Localization Microscopy with the Fluorescence-Activating and Absorption-Shifting Tag (FAST) System Article de journal Elizabeth M Smith; Arnaud Gautier; Elias M Puchner ACS Chemical Biology, 14 (6), p. 1115-1120, 2019, ISSN: 1554-8929. @article{Smith2019,
title = {Single-Molecule Localization Microscopy with the Fluorescence-Activating and Absorption-Shifting Tag (FAST) System},
author = {Elizabeth M Smith and Arnaud Gautier and Elias M Puchner},
url = {https://doi.org/10.1021/acschembio.9b00149},
doi = {10.1021/acschembio.9b00149},
issn = {1554-8929},
year = {2019},
date = {2019-06-21},
journal = {ACS Chemical Biology},
volume = {14},
number = {6},
pages = {1115-1120},
publisher = {American Chemical Society},
abstract = {We develop and employ the Fluorescence-Activating and absorption-Shifting Tag (FAST) system for super-resolution (SR) imaging and single-molecule tracking based on single-molecule localizations. The fast off rate of fluorogen binding, combined with its spatially well-separated labeling of the densely expressed FAST fusion proteins, allowed single-molecule measurements to be performed in both living and fixed cells. The well-separated fluorescence localization density was achieved by either reversibly controlling the fluorogen concentration or by irreversibly photobleaching the FAST-fluorogen complex. The experimentally determined resolution of 28 nm allowed us to resolve Ensconsin-labeled microtubules and to track single molecules in mitochondria. Our results demonstrate that FAST is well-suited for single-molecule localization microscopy (SMLM). The small size and the availability of spectrally distinct fluorogens present unique advantages of the FAST system as a potential orthogonal labeling strategy that could be applied in conjunction with existing super-resolution dyes and photoactivatable proteins in versatile imaging applications.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
We develop and employ the Fluorescence-Activating and absorption-Shifting Tag (FAST) system for super-resolution (SR) imaging and single-molecule tracking based on single-molecule localizations. The fast off rate of fluorogen binding, combined with its spatially well-separated labeling of the densely expressed FAST fusion proteins, allowed single-molecule measurements to be performed in both living and fixed cells. The well-separated fluorescence localization density was achieved by either reversibly controlling the fluorogen concentration or by irreversibly photobleaching the FAST-fluorogen complex. The experimentally determined resolution of 28 nm allowed us to resolve Ensconsin-labeled microtubules and to track single molecules in mitochondria. Our results demonstrate that FAST is well-suited for single-molecule localization microscopy (SMLM). The small size and the availability of spectrally distinct fluorogens present unique advantages of the FAST system as a potential orthogonal labeling strategy that could be applied in conjunction with existing super-resolution dyes and photoactivatable proteins in versatile imaging applications. |
The Glowing Panoply of Fluorogen-based Markers for Advanced Bioimaging Book Chapter A Gautier The Glowing Panoply of Fluorogen-based Markers for Advanced Bioimaging, Chapitre 3, 2019. @inbook{Gautier:2019,
title = {The Glowing Panoply of Fluorogen-based Markers for Advanced Bioimaging},
author = {A Gautier},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85056600039&doi=10.1039%2f9781788013284-00041&partnerID=40&md5=5d754dc76f6a9652835200ef4214a41a},
doi = {10.1039/9781788013284-00041},
year = {2019},
date = {2019-01-01},
booktitle = {The Glowing Panoply of Fluorogen-based Markers for Advanced Bioimaging},
chapter = {3},
series = {Comprehensive Series in Photochemical and Photobiological Sciences},
abstract = {The biological sciences nowadays rely extensively on imaging tools to decipher the complexity of living organisms. Fluorescence microscopy allows the study of biological processes with unprecedented temporal and spatial resolution. The revolution in fluorescence imaging has been the development of a large toolbox of fluorescent proteins able to reveal the abundance, position and dynamics of proteins. The fluorescence toolbox has recently been expanded with innovative reporters that permit proteins, and other biomolecules such as RNA, to be visualized in new ways. These innovative reporters are bipartite systems composed of a genetically encoded tag forming a fluorescent complex with a small organic fluorogenic chromophore (also called fluorogens). This chapter is a user-oriented presentation of some of the most mature fluorogen-based markers available to biologists. © 2019 European Society for Photobiology.},
keywords = {},
pubstate = {published},
tppubtype = {inbook}
}
The biological sciences nowadays rely extensively on imaging tools to decipher the complexity of living organisms. Fluorescence microscopy allows the study of biological processes with unprecedented temporal and spatial resolution. The revolution in fluorescence imaging has been the development of a large toolbox of fluorescent proteins able to reveal the abundance, position and dynamics of proteins. The fluorescence toolbox has recently been expanded with innovative reporters that permit proteins, and other biomolecules such as RNA, to be visualized in new ways. These innovative reporters are bipartite systems composed of a genetically encoded tag forming a fluorescent complex with a small organic fluorogenic chromophore (also called fluorogens). This chapter is a user-oriented presentation of some of the most mature fluorogen-based markers available to biologists. © 2019 European Society for Photobiology. |
2018
|
Circularly Permuted Fluorogenic Proteins for the Design of Modular Biosensors Article de journal A G Tebo; F M Pimenta; M Zoumpoulaki; C Kikuti; H Sirkia; M -A Plamont; A Houdusse; A Gautier ACS Chemical Biology, 13 (9), p. 2392–2397, 2018. @article{Tebo:2018,
title = {Circularly Permuted Fluorogenic Proteins for the Design of Modular Biosensors},
author = {A G Tebo and F M Pimenta and M Zoumpoulaki and C Kikuti and H Sirkia and M -A Plamont and A Houdusse and A Gautier},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85052286419&doi=10.1021%2facschembio.8b00417&partnerID=40&md5=f7f8a46015d14cb7450f3d6d2b70a529},
doi = {10.1021/acschembio.8b00417},
year = {2018},
date = {2018-01-01},
journal = {ACS Chemical Biology},
volume = {13},
number = {9},
pages = {2392--2397},
abstract = {Fluorescent reporters are essential components for the design of optical biosensors that are able to image intracellular analytes in living cells. Herein, we describe the development of circularly permuted variants of Fluorescence-Activating and absorption-Shifting Tag (FAST) and demonstrate their potential as reporting module in biosensors. Circularly permutated FAST (cpFAST) variants allow one to condition the binding and activation of a fluorogenic ligand (and thus fluorescence) to analyte recognition by coupling them with analyte-binding domains. We demonstrated their use for biosensor design by generating multicolor plug-and-play fluorogenic biosensors for imaging the intracellular levels of Ca2+ in living mammalian cells in real time. © 2018 American Chemical Society.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Fluorescent reporters are essential components for the design of optical biosensors that are able to image intracellular analytes in living cells. Herein, we describe the development of circularly permuted variants of Fluorescence-Activating and absorption-Shifting Tag (FAST) and demonstrate their potential as reporting module in biosensors. Circularly permutated FAST (cpFAST) variants allow one to condition the binding and activation of a fluorogenic ligand (and thus fluorescence) to analyte recognition by coupling them with analyte-binding domains. We demonstrated their use for biosensor design by generating multicolor plug-and-play fluorogenic biosensors for imaging the intracellular levels of Ca2+ in living mammalian cells in real time. © 2018 American Chemical Society. |
Fluorogenic Probing of Membrane Protein Trafficking Article de journal C Li; A Mourton; M -A Plamont; V Rodrigues; I Aujard; M Volovitch; T Le Saux; F Perez; S Vriz; L Jullien; A Joliot; A Gautier Bioconjugate Chemistry, 29 (6), p. 1823–1828, 2018. @article{Li:2018a,
title = {Fluorogenic Probing of Membrane Protein Trafficking},
author = {C Li and A Mourton and M -A Plamont and V Rodrigues and I Aujard and M Volovitch and T Le Saux and F Perez and S Vriz and L Jullien and A Joliot and A Gautier},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85047641063&doi=10.1021%2facs.bioconjchem.8b00180&partnerID=40&md5=bcbb74499b742fa8b0762b8c52ebf5dd},
doi = {10.1021/acs.bioconjchem.8b00180},
year = {2018},
date = {2018-01-01},
journal = {Bioconjugate Chemistry},
volume = {29},
number = {6},
pages = {1823--1828},
abstract = {Methods to differentially label cell-surface and intracellular membrane proteins are indispensable for understanding their function and the regulation of their trafficking. We present an efficient strategy for the rapid and selective fluorescent labeling of membrane proteins based on the chemical-genetic fluorescent marker FAST (fluorescence-activating and absorption-shifting tag). Cell-surface FAST-tagged proteins could be selectively and rapidly labeled using fluorogenic membrane-impermeant 4-hydroxybenzylidene rhodanine (HBR) analogs. This approach allows the study of protein trafficking at the plasma membrane with various fluorometric techniques, and opens exciting prospects for the high-throughput screening of small molecules able to restore disease-related trafficking defects. © 2018 American Chemical Society.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Methods to differentially label cell-surface and intracellular membrane proteins are indispensable for understanding their function and the regulation of their trafficking. We present an efficient strategy for the rapid and selective fluorescent labeling of membrane proteins based on the chemical-genetic fluorescent marker FAST (fluorescence-activating and absorption-shifting tag). Cell-surface FAST-tagged proteins could be selectively and rapidly labeled using fluorogenic membrane-impermeant 4-hydroxybenzylidene rhodanine (HBR) analogs. This approach allows the study of protein trafficking at the plasma membrane with various fluorometric techniques, and opens exciting prospects for the high-throughput screening of small molecules able to restore disease-related trafficking defects. © 2018 American Chemical Society. |
Fluorogenic Protein-Based Strategies for Detection, Actuation, and Sensing Article de journal A Gautier; A G Tebo BioEssays, 40 (10), 2018. @article{Gautier:2018,
title = {Fluorogenic Protein-Based Strategies for Detection, Actuation, and Sensing},
author = {A Gautier and A G Tebo},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85053180336&doi=10.1002%2fbies.201800118&partnerID=40&md5=92409e91810fa2bf17d3eef357bc1bc9},
doi = {10.1002/bies.201800118},
year = {2018},
date = {2018-01-01},
journal = {BioEssays},
volume = {40},
number = {10},
abstract = {Fluorescence imaging has become an indispensable tool in cell and molecular biology. GFP-like fluorescent proteins have revolutionized fluorescence microscopy, giving experimenters exquisite control over the localization and specificity of tagged constructs. However, these systems present certain drawbacks and as such, alternative systems based on a fluorogenic interaction between a chromophore and a protein have been developed. While these systems are initially designed as fluorescent labels, they also present new opportunities for the development of novel labeling and detection strategies. This review focuses on new labeling protocols, actuation methods, and biosensors based on fluorogenic protein systems. © 2018 WILEY Periodicals, Inc.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Fluorescence imaging has become an indispensable tool in cell and molecular biology. GFP-like fluorescent proteins have revolutionized fluorescence microscopy, giving experimenters exquisite control over the localization and specificity of tagged constructs. However, these systems present certain drawbacks and as such, alternative systems based on a fluorogenic interaction between a chromophore and a protein have been developed. While these systems are initially designed as fluorescent labels, they also present new opportunities for the development of novel labeling and detection strategies. This review focuses on new labeling protocols, actuation methods, and biosensors based on fluorogenic protein systems. © 2018 WILEY Periodicals, Inc. |
Improved Chemical-Genetic Fluorescent Markers for Live Cell Microscopy Article de journal A G Tebo; F M Pimenta; Y Zhang; A Gautier Biochemistry, 57 (39), p. 5648–5653, 2018. @article{Tebo:2018a,
title = {Improved Chemical-Genetic Fluorescent Markers for Live Cell Microscopy},
author = {A G Tebo and F M Pimenta and Y Zhang and A Gautier},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85053681817&doi=10.1021%2facs.biochem.8b00649&partnerID=40&md5=550c3f9cf88557339074b67771afd7d7},
doi = {10.1021/acs.biochem.8b00649},
year = {2018},
date = {2018-01-01},
journal = {Biochemistry},
volume = {57},
number = {39},
pages = {5648--5653},
abstract = {Inducible chemical-genetic fluorescent markers are promising tools for live cell imaging requiring high spatiotemporal resolution and low background fluorescence. The fluorescence-activating and absorption shifting tag (FAST) was recently developed to form fluorescent molecular complexes with a family of small, synthetic fluorogenic chromophores (so-called fluorogens). Here, we use rational design to modify the binding pocket of the protein and screen for improved fluorescence performances with four different fluorogens. The introduction of a single mutation results in improvements in both quantum yield and dissociation constant with nearly all fluorogens tested. Our improved FAST (iFAST) allowed the generation of a tandem iFAST (td-iFAST) that forms green and red fluorescent reporters 1.6-fold and 2-fold brighter than EGFP and mCherry, respectively, while having a comparable size. © Copyright 2018 American Chemical Society.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Inducible chemical-genetic fluorescent markers are promising tools for live cell imaging requiring high spatiotemporal resolution and low background fluorescence. The fluorescence-activating and absorption shifting tag (FAST) was recently developed to form fluorescent molecular complexes with a family of small, synthetic fluorogenic chromophores (so-called fluorogens). Here, we use rational design to modify the binding pocket of the protein and screen for improved fluorescence performances with four different fluorogens. The introduction of a single mutation results in improvements in both quantum yield and dissociation constant with nearly all fluorogens tested. Our improved FAST (iFAST) allowed the generation of a tandem iFAST (td-iFAST) that forms green and red fluorescent reporters 1.6-fold and 2-fold brighter than EGFP and mCherry, respectively, while having a comparable size. © Copyright 2018 American Chemical Society. |
Macroscale fluorescence imaging against autofluorescence under ambient light Article de journal R Zhang; R Chouket; M -A Plamont; Z Kelemen; A Espagne; A G Tebo; A Gautier; L Gissot; J -D Faure; L Jullien; V Croquette; T Le Saux Light: Science and Applications, 7 (1), 2018. @article{Zhang:2018c,
title = {Macroscale fluorescence imaging against autofluorescence under ambient light},
author = {R Zhang and R Chouket and M -A Plamont and Z Kelemen and A Espagne and A G Tebo and A Gautier and L Gissot and J -D Faure and L Jullien and V Croquette and T Le Saux},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85058077105&doi=10.1038%2fs41377-018-0098-6&partnerID=40&md5=958a21f219ba413e687d1860d21c2767},
doi = {10.1038/s41377-018-0098-6},
year = {2018},
date = {2018-01-01},
journal = {Light: Science and Applications},
volume = {7},
number = {1},
abstract = {Macroscale fluorescence imaging is increasingly used to observe biological samples. However, it may suffer from spectral interferences that originate from ambient light or autofluorescence of the sample or its support. In this manuscript, we built a simple and inexpensive fluorescence macroscope, which has been used to evaluate the performance of Speed OPIOM (Out of Phase Imaging after Optical Modulation), which is a reference-free dynamic contrast protocol, to selectively image reversibly photoswitchable fluorophores as labels against detrimental autofluorescence and ambient light. By tuning the intensity and radial frequency of the modulated illumination to the Speed OPIOM resonance and adopting a phase-sensitive detection scheme that ensures noise rejection, we enhanced the sensitivity and the signal-to-noise ratio for fluorescence detection in blot assays by factors of 50 and 10, respectively, over direct fluorescence observation under constant illumination. Then, we overcame the strong autofluorescence of growth media that are currently used in microbiology and realized multiplexed fluorescence observation of colonies of spectrally similar fluorescent bacteria with a unique configuration of excitation and emission wavelengths. Finally, we easily discriminated fluorescent labels from the autofluorescent and reflective background in labeled leaves, even under the interference of incident light at intensities that are comparable to sunlight. The proposed approach is expected to find multiple applications, from biological assays to outdoor observations, in fluorescence macroimaging. © 2018, The Author(s).},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Macroscale fluorescence imaging is increasingly used to observe biological samples. However, it may suffer from spectral interferences that originate from ambient light or autofluorescence of the sample or its support. In this manuscript, we built a simple and inexpensive fluorescence macroscope, which has been used to evaluate the performance of Speed OPIOM (Out of Phase Imaging after Optical Modulation), which is a reference-free dynamic contrast protocol, to selectively image reversibly photoswitchable fluorophores as labels against detrimental autofluorescence and ambient light. By tuning the intensity and radial frequency of the modulated illumination to the Speed OPIOM resonance and adopting a phase-sensitive detection scheme that ensures noise rejection, we enhanced the sensitivity and the signal-to-noise ratio for fluorescence detection in blot assays by factors of 50 and 10, respectively, over direct fluorescence observation under constant illumination. Then, we overcame the strong autofluorescence of growth media that are currently used in microbiology and realized multiplexed fluorescence observation of colonies of spectrally similar fluorescent bacteria with a unique configuration of excitation and emission wavelengths. Finally, we easily discriminated fluorescent labels from the autofluorescent and reflective background in labeled leaves, even under the interference of incident light at intensities that are comparable to sunlight. The proposed approach is expected to find multiple applications, from biological assays to outdoor observations, in fluorescence macroimaging. © 2018, The Author(s). |
Spying on cells with chemical-genetic hybrids Article de journal A Gautier Actualite Chimique, (435), p. 31–35, 2018. @article{Gautier:2018b,
title = {Spying on cells with chemical-genetic hybrids},
author = {A Gautier},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85059310973&partnerID=40&md5=89fdbcf594a9f3d4fe3ad8b1507ccef9},
year = {2018},
date = {2018-01-01},
journal = {Actualite Chimique},
number = {435},
pages = {31--35},
abstract = {Cells and organisms are complex machines regulated by a set of dynamic events orchestrated in space and time. Our understanding of their inner workings is intimately linked to our ability to observe how their constituents organize and interact. Optical microscopy allows to observe living systems at submicrometric scale. The development of high-performance fluorescent markers makes possible nowadays to monitor the dynamics of biomolecules with an unprecedented spatial and temporal resolution. This article presents how chemistry and biology can team up to develop next-generation markers that push the boundaries of biological imaging. © 2018 Societe Francaise de Chimie. All rights reserved.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Cells and organisms are complex machines regulated by a set of dynamic events orchestrated in space and time. Our understanding of their inner workings is intimately linked to our ability to observe how their constituents organize and interact. Optical microscopy allows to observe living systems at submicrometric scale. The development of high-performance fluorescent markers makes possible nowadays to monitor the dynamics of biomolecules with an unprecedented spatial and temporal resolution. This article presents how chemistry and biology can team up to develop next-generation markers that push the boundaries of biological imaging. © 2018 Societe Francaise de Chimie. All rights reserved. |
The Inducible Chemical-Genetic Fluorescent Marker FAST Outperforms Classical Fluorescent Proteins in the Quantitative Reporting of Bacterial Biofilm Dynamics Article de journal Amaury Monmeyran; Philippe Thomen; Hugo Jonqui`ere; Franck Sureau; Chenge Li; Marie-Aude Plamont; Carine Douarche; Jean-Franc cois Casella; Arnaud Gautier; Nelly Henry Scientific Reports, 8 (1), p. 10336, 2018, ISSN: 2045-2322. @article{RN36b,
title = {The Inducible Chemical-Genetic Fluorescent Marker FAST Outperforms Classical Fluorescent Proteins in the Quantitative Reporting of Bacterial Biofilm Dynamics},
author = {Amaury Monmeyran and Philippe Thomen and Hugo Jonqui{`e}re and Franck Sureau and Chenge Li and Marie-Aude Plamont and Carine Douarche and Jean-Fran{c c}ois Casella and Arnaud Gautier and Nelly Henry},
doi = {10.1038/s41598-018-28643-z},
issn = {2045-2322},
year = {2018},
date = {2018-01-01},
journal = {Scientific Reports},
volume = {8},
number = {1},
pages = {10336},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2017
|
Chromophore Renewal and Fluorogen-Binding Tags: A Match Made to Last Article de journal Frederico M Pimenta; Giovanni Chiappetta; Thomas Le Saux; Jo"elle Vinh; Ludovic Jullien; Arnaud Gautier Scientific Reports, 7 (1), p. 12316, 2017, ISSN: 2045-2322. @article{RN35b,
title = {Chromophore Renewal and Fluorogen-Binding Tags: A Match Made to Last},
author = {Frederico M Pimenta and Giovanni Chiappetta and Thomas Le Saux and Jo{"e}lle Vinh and Ludovic Jullien and Arnaud Gautier},
doi = {10.1038/s41598-017-12400-9},
issn = {2045-2322},
year = {2017},
date = {2017-01-01},
journal = {Scientific Reports},
volume = {7},
number = {1},
pages = {12316},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Dynamic multicolor protein labeling in living cells Article de journal C Li; M -A Plamont; H L Sladitschek; V Rodrigues; I Aujard; P Neveu; T Le Saux; L Jullien; A Gautier Chemical Science, 8 (8), p. 5598–5605, 2017. @article{Li:2017a,
title = {Dynamic multicolor protein labeling in living cells},
author = {C Li and M -A Plamont and H L Sladitschek and V Rodrigues and I Aujard and P Neveu and T Le Saux and L Jullien and A Gautier},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85023627118&doi=10.1039%2fc7sc01364g&partnerID=40&md5=dee65e052a12f416631a2699edfa5dd1},
doi = {10.1039/c7sc01364g},
year = {2017},
date = {2017-01-01},
journal = {Chemical Science},
volume = {8},
number = {8},
pages = {5598--5605},
abstract = {Yellow Fluorescence-Activating and absorption-Shifting Tag (Y-FAST, hereafter called FAST) is a 14 kDa protein tag giving a bright green-yellow fluorescent complex upon interaction with the fluorogenic dye 4-hydroxy-3-methylbenzylidene rhodanine (HMBR). Here, we report a collection of fluorogens enabling tuning of the fluorescence color of FAST from green-yellow to orange and red. Beyond allowing the multicolor imaging of FAST-tagged proteins in live cells, these fluorogens enable dynamic color switching because of FAST's reversible labeling. This unprecedented behavior allows for selective detection of FAST-tagged proteins in cells expressing both green and red fluorescent species through two-color cross-correlation, opening up exciting prospects to overcome spectral crowding and push the frontiers of multiplexed imaging. © 2017 The Royal Society of Chemistry.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Yellow Fluorescence-Activating and absorption-Shifting Tag (Y-FAST, hereafter called FAST) is a 14 kDa protein tag giving a bright green-yellow fluorescent complex upon interaction with the fluorogenic dye 4-hydroxy-3-methylbenzylidene rhodanine (HMBR). Here, we report a collection of fluorogens enabling tuning of the fluorescence color of FAST from green-yellow to orange and red. Beyond allowing the multicolor imaging of FAST-tagged proteins in live cells, these fluorogens enable dynamic color switching because of FAST's reversible labeling. This unprecedented behavior allows for selective detection of FAST-tagged proteins in cells expressing both green and red fluorescent species through two-color cross-correlation, opening up exciting prospects to overcome spectral crowding and push the frontiers of multiplexed imaging. © 2017 The Royal Society of Chemistry. |
Erratum: Author Correction: Resonant out-of-phase fluorescence microscopy and remote imaging overcome spectral limitations (Nature communications (2017) 8 1 (969)) Article de journal J Quérard; R Zhang; Z Kelemen; M -A Plamont; X Xie; R Chouket; I Roemgens; Y Korepina; S Albright; E Ipendey; M Volovitch; H L Sladitschek; P Neveu; L Gissot; A Gautier; J -D Faure; V Croquette; T Le Saux; L Jullien Nature communications, 8 (1), p. 2173, 2017. @article{Querard:2017,
title = {Erratum: Author Correction: Resonant out-of-phase fluorescence microscopy and remote imaging overcome spectral limitations (Nature communications (2017) 8 1 (969))},
author = {J Qu\'{e}rard and R Zhang and Z Kelemen and M -A Plamont and X Xie and R Chouket and I Roemgens and Y Korepina and S Albright and E Ipendey and M Volovitch and H L Sladitschek and P Neveu and L Gissot and A Gautier and J -D Faure and V Croquette and T Le Saux and L Jullien},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85058747083&doi=10.1038%2fs41467-017-02133-8&partnerID=40&md5=15b4153817b7bd74d9691a4083989504},
doi = {10.1038/s41467-017-02133-8},
year = {2017},
date = {2017-01-01},
journal = {Nature communications},
volume = {8},
number = {1},
pages = {2173},
abstract = {The Peer Review File associated with this Article was updated shortly after publication to redact from the authors' point-by-point response a description of unpublished work describing how Speed OPIOM may in future be used to facilitate discrimination between FRET and direct excitation.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The Peer Review File associated with this Article was updated shortly after publication to redact from the authors' point-by-point response a description of unpublished work describing how Speed OPIOM may in future be used to facilitate discrimination between FRET and direct excitation. |
