2018
|
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. |
Fluorogenic labeling strategies for biological imaging Article de journal C Li; A G Tebo; A Gautier International Journal of Molecular Sciences, 18 (7), 2017. @article{Li:2017b,
title = {Fluorogenic labeling strategies for biological imaging},
author = {C Li and A G Tebo and A Gautier},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85023628010&doi=10.3390%2fijms18071473&partnerID=40&md5=d7fc35685b4a7cb4def13c1a52a66d92},
doi = {10.3390/ijms18071473},
year = {2017},
date = {2017-01-01},
journal = {International Journal of Molecular Sciences},
volume = {18},
number = {7},
abstract = {The spatiotemporal fluorescence imaging of biological processes requires effective tools to label intracellular biomolecules in living systems. This review presents a brief overview of recent labeling strategies that permits one to make protein and RNA strongly fluorescent using synthetic fluorogenic probes. Genetically encoded tags selectively binding the exogenously applied molecules ensure high labeling selectivity, while high imaging contrast is achieved using fluorogenic chromophores that are fluorescent only when bound to their cognate tag, and are otherwise dark. Beyond avoiding the need for removal of unbound synthetic dyes, these approaches allow the development of sophisticated imaging assays, and open exciting prospects for advanced imaging, particularly for multiplexed imaging and super-resolution microscopy. © 2017 by the authors. Licensee MDPI, Basel, Switzerland.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The spatiotemporal fluorescence imaging of biological processes requires effective tools to label intracellular biomolecules in living systems. This review presents a brief overview of recent labeling strategies that permits one to make protein and RNA strongly fluorescent using synthetic fluorogenic probes. Genetically encoded tags selectively binding the exogenously applied molecules ensure high labeling selectivity, while high imaging contrast is achieved using fluorogenic chromophores that are fluorescent only when bound to their cognate tag, and are otherwise dark. Beyond avoiding the need for removal of unbound synthetic dyes, these approaches allow the development of sophisticated imaging assays, and open exciting prospects for advanced imaging, particularly for multiplexed imaging and super-resolution microscopy. © 2017 by the authors. Licensee MDPI, Basel, Switzerland. |
Hybrid fluorescent probes for imaging cellular proteins on demand Article de journal L Jullien; A Gautier Medecine/Sciences, 33 (6-7), p. 576–578, 2017. @article{Jullien:2017,
title = {Hybrid fluorescent probes for imaging cellular proteins on demand},
author = {L Jullien and A Gautier},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85044173814&doi=10.1051%2fmedsci%2f20173306006&partnerID=40&md5=438f0ceb949779e8a90a779a37a1d890},
doi = {10.1051/medsci/20173306006},
year = {2017},
date = {2017-01-01},
journal = {Medecine/Sciences},
volume = {33},
number = {6-7},
pages = {576--578},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Resonant out-of-phase fluorescence microscopy and remote imaging overcome spectral limitations 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), 2017. @article{Querard:2017a,
title = {Resonant out-of-phase fluorescence microscopy and remote imaging overcome spectral limitations},
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-s2.0-85031811446&doi=10.1038%2fs41467-017-00847-3&partnerID=40&md5=c320b3585a15085c192d20ee6faa36fa},
doi = {10.1038/s41467-017-00847-3},
year = {2017},
date = {2017-01-01},
journal = {Nature Communications},
volume = {8},
number = {1},
abstract = {We present speed out-of-phase imaging after optical modulation (OPIOM), which exploits reversible photoswitchable fluorophores as fluorescent labels and combines optimized periodic illumination with phase-sensitive detection to specifically retrieve the label signal. Speed OPIOM can extract the fluorescence emission from a targeted label in the presence of spectrally interfering fluorophores and autofluorescence. Up to four fluorescent proteins exhibiting a similar green fluorescence have been distinguished in cells either sequentially or in parallel. Speed OPIOM is compatible with imaging biological processes in real time in live cells. Finally speed OPIOM is not limited to microscopy but is relevant for remote imaging as well, in particular, under ambient light. Thus, speed OPIOM has proved to enable fast and quantitative live microscopic and remote-multiplexed fluorescence imaging of biological samples while filtering out noise, interfering fluorophores, as well as ambient light. © 2017 The Author(s).},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
We present speed out-of-phase imaging after optical modulation (OPIOM), which exploits reversible photoswitchable fluorophores as fluorescent labels and combines optimized periodic illumination with phase-sensitive detection to specifically retrieve the label signal. Speed OPIOM can extract the fluorescence emission from a targeted label in the presence of spectrally interfering fluorophores and autofluorescence. Up to four fluorescent proteins exhibiting a similar green fluorescence have been distinguished in cells either sequentially or in parallel. Speed OPIOM is compatible with imaging biological processes in real time in live cells. Finally speed OPIOM is not limited to microscopy but is relevant for remote imaging as well, in particular, under ambient light. Thus, speed OPIOM has proved to enable fast and quantitative live microscopic and remote-multiplexed fluorescence imaging of biological samples while filtering out noise, interfering fluorophores, as well as ambient light. © 2017 The Author(s). |
2016
|
Design and characterization of red fluorogenic push-pull chromophores holding great potential for bioimaging and biosensing Article de journal C Li; M -A Plamont; I Aujard; T Le Saux; L Jullien; A Gautier Organic and Biomolecular Chemistry, 14 (39), p. 9253–9261, 2016. @article{Li:2016,
title = {Design and characterization of red fluorogenic push-pull chromophores holding great potential for bioimaging and biosensing},
author = {C Li and M -A Plamont and I Aujard and T Le Saux and L Jullien and A Gautier},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84990182453&doi=10.1039%2fc6ob01612j&partnerID=40&md5=7cea2c6d4aeeeef91e6a3a5bd0d6b5ad},
doi = {10.1039/c6ob01612j},
year = {2016},
date = {2016-01-01},
journal = {Organic and Biomolecular Chemistry},
volume = {14},
number = {39},
pages = {9253--9261},
abstract = {Fluorogenic chromophores have been used recently for fluorescence reporting and biosensing. Their ability to turn on upon specific interaction with a given target has been exploited in particular for the design of fluorogen-based reporters enabling biomolecule labeling and imaging. In this paper, we report the development and exhaustive characterization of a new family of red fluorogenic push-pull chromophores, holding great potential for the development of fluorogen-based reporters or intracellular fluorogenic markers. The proposed methodology is generic and should find general applicability in the discovery of new fluorogenic dyes suitable for the design of fluorogen-based reporters and biosensors. © The Royal Society of Chemistry 2016.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Fluorogenic chromophores have been used recently for fluorescence reporting and biosensing. Their ability to turn on upon specific interaction with a given target has been exploited in particular for the design of fluorogen-based reporters enabling biomolecule labeling and imaging. In this paper, we report the development and exhaustive characterization of a new family of red fluorogenic push-pull chromophores, holding great potential for the development of fluorogen-based reporters or intracellular fluorogenic markers. The proposed methodology is generic and should find general applicability in the discovery of new fluorogenic dyes suitable for the design of fluorogen-based reporters and biosensors. © The Royal Society of Chemistry 2016. |
Kinetics of Reactive Modules Adds Discriminative Dimensions for Selective Cell Imaging Article de journal J Quérard; T Le Saux; A Gautier; D Alcor; V Croquette; A Lemarchand; C Gosse; L Jullien ChemPhysChem, 17 (10), p. 1396–1413, 2016. @article{Querard:2016,
title = {Kinetics of Reactive Modules Adds Discriminative Dimensions for Selective Cell Imaging},
author = {J Qu\'{e}rard and T Le Saux and A Gautier and D Alcor and V Croquette and A Lemarchand and C Gosse and L Jullien},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84957539317&doi=10.1002%2fcphc.201500987&partnerID=40&md5=4a514250af842ae7697b695eb73769fb},
doi = {10.1002/cphc.201500987},
year = {2016},
date = {2016-01-01},
journal = {ChemPhysChem},
volume = {17},
number = {10},
pages = {1396--1413},
abstract = {Living cells are chemical mixtures of exceptional interest and significance, whose investigation requires the development of powerful analytical tools fulfilling the demanding constraints resulting from their singular features. In particular, multiplexed observation of a large number of molecular targets with high spatiotemporal resolution appears highly desirable. One attractive road to address this analytical challenge relies on engaging the targets in reactions and exploiting the rich kinetic signature of the resulting reactive module, which originates from its topology and its rate constants. This review explores the various facets of this promising strategy. We first emphasize the singularity of the content of a living cell as a chemical mixture and suggest that its multiplexed observation is significant and timely. Then, we show that exploiting the kinetics of analytical processes is relevant to selectively detect a given analyte: upon perturbing the system, the kinetic window associated to response read-out has to be matched with that of the targeted reactive module. Eventually, we introduce the state-of-the-art of cell imaging exploiting protocols based on reaction kinetics and draw some promising perspectives. Live recording: In living cells, the multiplexed observation of a large number of targets has recently emerged as a desirable goal. To address this challenge, an attractive road relies on engaging the targets in reactions and exploiting the kinetic signature of the resulting reactive module. This review explores the facets of this strategy and draw some promising perspectives. © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Living cells are chemical mixtures of exceptional interest and significance, whose investigation requires the development of powerful analytical tools fulfilling the demanding constraints resulting from their singular features. In particular, multiplexed observation of a large number of molecular targets with high spatiotemporal resolution appears highly desirable. One attractive road to address this analytical challenge relies on engaging the targets in reactions and exploiting the rich kinetic signature of the resulting reactive module, which originates from its topology and its rate constants. This review explores the various facets of this promising strategy. We first emphasize the singularity of the content of a living cell as a chemical mixture and suggest that its multiplexed observation is significant and timely. Then, we show that exploiting the kinetics of analytical processes is relevant to selectively detect a given analyte: upon perturbing the system, the kinetic window associated to response read-out has to be matched with that of the targeted reactive module. Eventually, we introduce the state-of-the-art of cell imaging exploiting protocols based on reaction kinetics and draw some promising perspectives. Live recording: In living cells, the multiplexed observation of a large number of targets has recently emerged as a desirable goal. To address this challenge, an attractive road relies on engaging the targets in reactions and exploiting the kinetic signature of the resulting reactive module. This review explores the facets of this strategy and draw some promising perspectives. © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. |
Small Fluorescence-Activating and Absorption-Shifting Tag for Tunable Protein Imaging in Vivo Article de journal Marie-Aude Plamont; Emmanuelle Billon-Denis; Sylvie Maurin; Carole Gauron; Frederico M Pimenta; Christian G Specht; Jian Shi; Jérôme Querard; Buyan Pan; Julien Rossignol; Karine Moncoq; Nelly Morellet; Michel Volovitch; Ewen Lescop; Yong Chen; Antoine Triller; Sophie Vriz; Thomas Le Saux; Ludovic Jullien; Arnaud Gautier Proceedings of the National Academy of Sciences, 113 (3), p. 497, 2016. @article{RN50,
title = {Small Fluorescence-Activating and Absorption-Shifting Tag for Tunable Protein Imaging in Vivo},
author = {Marie-Aude Plamont and Emmanuelle {Billon-Denis} and Sylvie Maurin and Carole Gauron and Frederico M Pimenta and Christian G Specht and Jian Shi and J\'{e}r\^{o}me Querard and Buyan Pan and Julien Rossignol and Karine Moncoq and Nelly Morellet and Michel Volovitch and Ewen Lescop and Yong Chen and Antoine Triller and Sophie Vriz and Thomas Le Saux and Ludovic Jullien and Arnaud Gautier},
doi = {10.1073/pnas.1513094113},
year = {2016},
date = {2016-01-01},
journal = {Proceedings of the National Academy of Sciences},
volume = {113},
number = {3},
pages = {497},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2015
|
Expanding discriminative dimensions for analysis and imaging Article de journal J Querard; A Gautier; T Le Saux; L Jullien Chemical Science, 6 (5), p. 2968–2978, 2015. @article{Querard:2015,
title = {Expanding discriminative dimensions for analysis and imaging},
author = {J Querard and A Gautier and T Le Saux and L Jullien},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84928139717&doi=10.1039%2fc4sc03955f&partnerID=40&md5=aeed36c64e258429fa7a7aa11b8baba8},
doi = {10.1039/c4sc03955f},
year = {2015},
date = {2015-01-01},
journal = {Chemical Science},
volume = {6},
number = {5},
pages = {2968--2978},
abstract = {Eliminating the contribution of interfering compounds is a key step in chemical analysis. In complex media, one possible approach is to perform a preliminary separation. However purification is often demanding, long, and costly; it may also considerably alter the properties of interacting components of the mixture (e.g. in a living cell). Hence there is a strong interest for developing separation-free non-invasive analytical protocols. Using photoswitchable probes as labelling and titration contrast agents, we demonstrate that the association of a modulated monochromatic light excitation with a kinetic filtering of the overall observable is much more attractive than constant excitation to read-out the contribution from a target probe under adverse conditions. An extensive theoretical framework enabled us to optimize the out-of-phase concentration first-order response of a photoswitchable probe to modulated illumination by appropriately matching the average light intensity and the radial frequency of the light modulation to the probe dynamics. Thus, we can selectively and quantitatively extract from an overall signal the contribution from a target photoswitchable probe within a mixture of species, photoswitchable or not. This simple titration strategy is more specifically developed in the context of fluorescence imaging, which offers promising perspectives. © The Royal Society of Chemistry 2015.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Eliminating the contribution of interfering compounds is a key step in chemical analysis. In complex media, one possible approach is to perform a preliminary separation. However purification is often demanding, long, and costly; it may also considerably alter the properties of interacting components of the mixture (e.g. in a living cell). Hence there is a strong interest for developing separation-free non-invasive analytical protocols. Using photoswitchable probes as labelling and titration contrast agents, we demonstrate that the association of a modulated monochromatic light excitation with a kinetic filtering of the overall observable is much more attractive than constant excitation to read-out the contribution from a target probe under adverse conditions. An extensive theoretical framework enabled us to optimize the out-of-phase concentration first-order response of a photoswitchable probe to modulated illumination by appropriately matching the average light intensity and the radial frequency of the light modulation to the probe dynamics. Thus, we can selectively and quantitatively extract from an overall signal the contribution from a target photoswitchable probe within a mixture of species, photoswitchable or not. This simple titration strategy is more specifically developed in the context of fluorescence imaging, which offers promising perspectives. © The Royal Society of Chemistry 2015. |
Fluorogen-Based Reporters for Fluorescence Imaging: A Review Article de journal Ludovic Jullien; Arnaud Gautier Methods and Applications in Fluorescence, 3 (4), p. 042007, 2015, ISSN: 2050-6120. @article{RN38,
title = {Fluorogen-Based Reporters for Fluorescence Imaging: A Review},
author = {Ludovic Jullien and Arnaud Gautier},
doi = {10.1088/2050-6120/3/4/042007},
issn = {2050-6120},
year = {2015},
date = {2015-01-01},
journal = {Methods and Applications in Fluorescence},
volume = {3},
number = {4},
pages = {042007},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Light-Activated Proteolysis for the Spatiotemporal Control of Proteins Article de journal Quentin Delacour; Chenge Li; Marie-Aude Plamont; Emmanuelle Billon-Denis; Isabelle Aujard; Thomas Le Saux; Ludovic Jullien; Arnaud Gautier ACS Chemical Biology, 10 (7), p. 1643-1647, 2015, ISSN: 1554-8929. @article{RN37,
title = {Light-Activated Proteolysis for the Spatiotemporal Control of Proteins},
author = {Quentin Delacour and Chenge Li and Marie-Aude Plamont and Emmanuelle {Billon-Denis} and Isabelle Aujard and Thomas Le Saux and Ludovic Jullien and Arnaud Gautier},
doi = {10.1021/acschembio.5b00069},
issn = {1554-8929},
year = {2015},
date = {2015-01-01},
journal = {ACS Chemical Biology},
volume = {10},
number = {7},
pages = {1643-1647},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Photoswitching Kinetics and Phase-Sensitive Detection Add Discriminative Dimensions for Selective Fluorescence Imaging Article de journal Jérôme Querard; Tal-Zvi Markus; Marie-Aude Plamont; Carole Gauron; Pengcheng Wang; Agathe Espagne; Michel Volovitch; Sophie Vriz; Vincent Croquette; Arnaud Gautier; Thomas Le Saux; Ludovic Jullien Angewandte Chemie International Edition, 54 (9), p. 2633-2637, 2015, ISSN: 1433-7851. @article{RN43b,
title = {Photoswitching Kinetics and Phase-Sensitive Detection Add Discriminative Dimensions for Selective Fluorescence Imaging},
author = {J\'{e}r\^{o}me Querard and Tal-Zvi Markus and Marie-Aude Plamont and Carole Gauron and Pengcheng Wang and Agathe Espagne and Michel Volovitch and Sophie Vriz and Vincent Croquette and Arnaud Gautier and Thomas Le Saux and Ludovic Jullien},
doi = {10.1002/anie.201408985},
issn = {1433-7851},
year = {2015},
date = {2015-01-01},
journal = {Angewandte Chemie International Edition},
volume = {54},
number = {9},
pages = {2633-2637},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2014
|
How to Control Proteins with Light in Living Systems Article de journal Arnaud Gautier; Carole Gauron; Michel Volovitch; David Bensimon; Ludovic Jullien; Sophie Vriz Nature Chemical Biology, 10 , p. 533, 2014. @article{RN42,
title = {How to Control Proteins with Light in Living Systems},
author = {Arnaud Gautier and Carole Gauron and Michel Volovitch and David Bensimon and Ludovic Jullien and Sophie Vriz},
doi = {10.1038/nchembio.1534},
year = {2014},
date = {2014-01-01},
journal = {Nature Chemical Biology},
volume = {10},
pages = {533},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
