Professeur des Universités, Sorbonne Université
Responsable du pôle de Chimie Physique et Biologique de la Matière Vivante
PASTEUR, Département de chimie, École Normale Supérieure, PSL University, Sorbonne Université, CNRS
24 rue Lhomond, 75005 Paris, France
Email: Ludovic.Jullien@ens.psl.eu or Ludovic.Jullien@sorbonne-universite.fr
Phone: +33 144323333
Office: E142c
Home page: https://ludovicjullien.org/
Publications
2023 |
Near-infrared co-illumination of fluorescent proteins reduces photobleaching and phototoxicity Article de journal L Ludvikova; E Simon; M Deygas; T Panier; M A Plamont; J Ollion; A Tebo; M Piel; L Jullien; L Robert; T Le Saux; A Espagne Nature Biotechnology, p. 12, 2023, ISSN: 1087-0156. @article{RN156, title = {Near-infrared co-illumination of fluorescent proteins reduces photobleaching and phototoxicity}, author = {L Ludvikova and E Simon and M Deygas and T Panier and M A Plamont and J Ollion and A Tebo and M Piel and L Jullien and L Robert and T Le Saux and A Espagne}, url = {<Go to ISI>://WOS:001042699900001}, doi = {10.1038/s41587-023-01893-7}, issn = {1087-0156}, year = {2023}, date = {2023-01-01}, journal = {Nature Biotechnology}, pages = {12}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
2021 |
Arnaud Gautier; Ludovic Jullien; Chenge Li; Marie-Aude Plamont; Alison G Tebo; Marion Thauvin; Michel Volovitch; Sophie Vriz Springer US, New York, NY, 2021, ISBN: 978-1-07-161593-5. @book{gautier_versatile_2021, title = {Versatile On-Demand Fluorescent Labeling of Fusion Proteins Using Fluorescence-Activating and Absorption-Shifting Tag (FAST)}, author = {Arnaud Gautier and Ludovic Jullien and Chenge Li and Marie-Aude Plamont and Alison G Tebo and Marion Thauvin and Michel Volovitch and Sophie Vriz}, editor = {Eli Zamir}, url = {https://doi.org/10.1007/978-1-0716-1593-5_16}, doi = {10.1007/978-1-0716-1593-5_16}, isbn = {978-1-07-161593-5}, year = {2021}, date = {2021-01-01}, urldate = {2023-10-31}, booktitle = {Multiplexed Imaging: Methods and Protocols}, pages = {253--265}, publisher = {Springer US}, address = {New York, NY}, series = {Methods in Molecular Biology}, abstract = {Observing the localization, the concentration, and the distribution of proteins in cells or organisms is essential to understand theirs functions. General and versatile methods allowing multiplexed imaging of proteins under a large variety of experimental conditions are thus essential for deciphering the inner workings of cells and organisms. Here, we present a general method based on the non-covalent labeling of a small protein tag, named FAST (fluorescence-activating and absorption-shifting tag), with various fluorogenic ligands that light up upon labeling, which makes the simple, robust, and versatile on-demand labeling of fusion proteins in a wide range of experimental systems possible.}, keywords = {}, pubstate = {published}, tppubtype = {book} } Observing the localization, the concentration, and the distribution of proteins in cells or organisms is essential to understand theirs functions. General and versatile methods allowing multiplexed imaging of proteins under a large variety of experimental conditions are thus essential for deciphering the inner workings of cells and organisms. Here, we present a general method based on the non-covalent labeling of a small protein tag, named FAST (fluorescence-activating and absorption-shifting tag), with various fluorogenic ligands that light up upon labeling, which makes the simple, robust, and versatile on-demand labeling of fusion proteins in a wide range of experimental systems possible. |
2020 |
Dynamic contrast for overcoming spectral interferences in fluorescence imaging Article de journal R Chouket; A Pellissier-Tanon; A Lemarchand; A Espagne; T Le Saux; L Jullien Journal of Physics-Photonics, 2 (3), p. 8, 2020, ISSN: 2515-7647. @article{RN1_30, title = {Dynamic contrast for overcoming spectral interferences in fluorescence imaging}, author = {R Chouket and A Pellissier-Tanon and A Lemarchand and A Espagne and T Le Saux and L Jullien}, url = {<Go to ISI>://WOS:000572940200001}, doi = {10.1088/2515-7647/ab9099}, issn = {2515-7647}, year = {2020}, date = {2020-01-01}, journal = {Journal of Physics-Photonics}, volume = {2}, number = {3}, pages = {8}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Dynamic contrast with reversibly photoswitchable fluorescent labels for imaging living cells Article de journal R Chouket; A Pellissier-Tanon; A Lemarchand; A Espagne; T Le Saux; L Jullien Chemical Science, 11 (11), p. 2882-2887, 2020, ISSN: 2041-6520. @article{RN2x, title = {Dynamic contrast with reversibly photoswitchable fluorescent labels for imaging living cells}, author = {R Chouket and A Pellissier-Tanon and A Lemarchand and A Espagne and T Le Saux and L Jullien}, url = {<Go to ISI>://WOS:000521247400002}, doi = {10.1039/d0sc00182a}, issn = {2041-6520}, year = {2020}, date = {2020-01-01}, journal = {Chemical Science}, volume = {11}, number = {11}, pages = {2882-2887}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
2019 |
Fatima Hamouri; Weiting Zhang; Isabelle Aujard; Thomas Le Saux; Bertrand Ducos; Sophie Vriz; Ludovic Jullien; David Bensimon Academic Press, 2019. @book{hamouri_chapter_2019, title = {Chapter One - Optical control of protein activity and gene expression by photoactivation of caged cyclofen}, author = {Fatima Hamouri and Weiting Zhang and Isabelle Aujard and Thomas Le Saux and Bertrand Ducos and Sophie Vriz and Ludovic Jullien and David Bensimon}, editor = {Alexander Deiters}, url = {https://www.sciencedirect.com/science/article/pii/S0076687919301247}, doi = {10.1016/bs.mie.2019.04.009}, year = {2019}, date = {2019-01-01}, urldate = {2023-10-31}, booktitle = {Methods in Enzymology}, volume = {624}, pages = {1--23}, publisher = {Academic Press}, series = {Optochemical Biology}, abstract = {The use of light to control the expression of genes and the activity of proteins is a rapidly expanding field. While many of these approaches use a fusion between a light activatable protein and the protein of interest to control the activity of the latter, it is also possible to control the activity of a protein by uncaging a specific ligand. In that context, controlling the activation of a protein fused to the modified estrogen receptor (ERT) by uncaging its ligand cyclofen-OH has emerged as a generic and versatile method to control the activation of proteins quantitatively, quickly and locally in a live organism. Here, we present the experimental details behind this approach.}, keywords = {}, pubstate = {published}, tppubtype = {book} } The use of light to control the expression of genes and the activity of proteins is a rapidly expanding field. While many of these approaches use a fusion between a light activatable protein and the protein of interest to control the activity of the latter, it is also possible to control the activity of a protein by uncaging a specific ligand. In that context, controlling the activation of a protein fused to the modified estrogen receptor (ERT) by uncaging its ligand cyclofen-OH has emerged as a generic and versatile method to control the activation of proteins quantitatively, quickly and locally in a live organism. Here, we present the experimental details behind this approach. |
Photosensitized oxidative addition to gold(i) enables alkynylative cyclization of o-alkylnylphenols with iodoalkynes Article de journal Zhonghua Xia; Vincent Corcé; Fen Zhao; Cédric Przybylski; Agathe Espagne; Ludovic Jullien; Thomas Le Saux; Yves Gimbert; Héloïse Dossmann; Virginie Mouriès-Mansuy; Cyril Ollivier; Louis Fensterbank Nature Chemistry, 11 (9), p. 797-805, 2019, ISSN: 1755-4349. @article{RN1_28, title = {Photosensitized oxidative addition to gold(i) enables alkynylative cyclization of o-alkylnylphenols with iodoalkynes}, author = {Zhonghua Xia and Vincent Corc\'{e} and Fen Zhao and C\'{e}dric Przybylski and Agathe Espagne and Ludovic Jullien and Thomas Le Saux and Yves Gimbert and H\'{e}lo\"{i}se Dossmann and Virginie Mouri\`{e}s-Mansuy and Cyril Ollivier and Louis Fensterbank}, url = {https://doi.org/10.1038/s41557-019-0295-9}, doi = {10.1038/s41557-019-0295-9}, issn = {1755-4349}, year = {2019}, date = {2019-01-01}, journal = {Nature Chemistry}, volume = {11}, number = {9}, pages = {797-805}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Photosensitized oxidative addition to gold(I) enables alkynylative cyclization of o-alkylnylphenols with iodoalkynes Article de journal Z H Xia; V Corce; F Zhao; C Przybylski; A Espagne; L Jullien; T Le Saux; Y Gimbert; H Dossmann; V Mouries-Mansuy; C Ollivier; L Fensterbank Nature Chemistry, 11 (9), p. 797-805, 2019, ISSN: 1755-4330. @article{RN3s, title = {Photosensitized oxidative addition to gold(I) enables alkynylative cyclization of o-alkylnylphenols with iodoalkynes}, author = {Z H Xia and V Corce and F Zhao and C Przybylski and A Espagne and L Jullien and T Le Saux and Y Gimbert and H Dossmann and V Mouries-Mansuy and C Ollivier and L Fensterbank}, url = {<Go to ISI>://WOS:000483307000010}, doi = {10.1038/s41557-019-0295-9}, issn = {1755-4330}, year = {2019}, date = {2019-01-01}, journal = {Nature Chemistry}, volume = {11}, number = {9}, pages = {797-805}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
2018 |
A chemically encoded timer for dual molecular delivery at tailored ranges and concentrations Article de journal S Serra; A Alouane; T Le Saux; S Huvelle; R Plasson; F Schmidt; L Jullien; R Labruère Chemical Communications, 54 (49), p. 6396–6399, 2018. @article{Serra:2018, title = {A chemically encoded timer for dual molecular delivery at tailored ranges and concentrations}, author = {S Serra and A Alouane and T Le Saux and S Huvelle and R Plasson and F Schmidt and L Jullien and R Labru\`{e}re}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85048683206&doi=10.1039%2fc8cc03253j&partnerID=40&md5=6b7d3eaf2fac02d48f0cfa34e3b730b9}, doi = {10.1039/c8cc03253j}, year = {2018}, date = {2018-01-01}, journal = {Chemical Communications}, volume = {54}, number = {49}, pages = {6396--6399}, abstract = {Spatiotemporal control of molecular distribution is much in demand in many fields of chemistry. To address this goal, we exploit a low molecular weight branched self-immolative architecture, which acts as a triggerable chemically encoded timer for autonomous sequential release of two chemicals. Using a light-activated model liberating two distinct fluorophores, we generated a tunable spatially contrasted molecular distribution. © 2018 The Royal Society of Chemistry.}, keywords = {}, pubstate = {published}, tppubtype = {article} } Spatiotemporal control of molecular distribution is much in demand in many fields of chemistry. To address this goal, we exploit a low molecular weight branched self-immolative architecture, which acts as a triggerable chemically encoded timer for autonomous sequential release of two chemicals. Using a light-activated model liberating two distinct fluorophores, we generated a tunable spatially contrasted molecular distribution. © 2018 The Royal Society of Chemistry. |
Control of Protein Activity and Gene Expression by Cyclofen-OH Uncaging Article de journal W Zhang; F Hamouri; Z Feng; I Aujard; B Ducos; S Ye; S Weiss; M Volovitch; S Vriz; L Jullien; D Bensimon ChemBioChem, 19 (12), p. 1232–1238, 2018. @article{Zhang:2018, title = {Control of Protein Activity and Gene Expression by Cyclofen-OH Uncaging}, author = {W Zhang and F Hamouri and Z Feng and I Aujard and B Ducos and S Ye and S Weiss and M Volovitch and S Vriz and L Jullien and D Bensimon}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85042596408&doi=10.1002%2fcbic.201700630&partnerID=40&md5=e4da60b83f338aba093989913695947b}, doi = {10.1002/cbic.201700630}, year = {2018}, date = {2018-01-01}, journal = {ChemBioChem}, volume = {19}, number = {12}, pages = {1232--1238}, abstract = {The use of light to control the expression of genes and the activity of proteins is a rapidly expanding field. Whereas many of these approaches use fusion between a light-activable protein and the protein of interest to control the activity of the latter, it is also possible to control the activity of a protein by uncaging a specific ligand. In that context, controlling the activation of a protein fused to the modified estrogen receptor (ERT) by uncaging its ligand cyclofen-OH has emerged as a generic and versatile method to control the activation of proteins quantitatively, quickly, and locally in a live organism. We present that approach and its uses in a variety of physiological contexts. © 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim}, keywords = {}, pubstate = {published}, tppubtype = {article} } The use of light to control the expression of genes and the activity of proteins is a rapidly expanding field. Whereas many of these approaches use fusion between a light-activable protein and the protein of interest to control the activity of the latter, it is also possible to control the activity of a protein by uncaging a specific ligand. In that context, controlling the activation of a protein fused to the modified estrogen receptor (ERT) by uncaging its ligand cyclofen-OH has emerged as a generic and versatile method to control the activation of proteins quantitatively, quickly, and locally in a live organism. We present that approach and its uses in a variety of physiological contexts. © 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim |
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. |
Light-assisted dynamic titration: from theory to an experimental protocol Article de journal A Pellissier-Tanon; R Chouket; T Le Saux; L Jullien; A Lemarchand Physical Chemistry Chemical Physics, 20 (37), p. 23998–24010, 2018. @article{Pellissier-Tanon:2018, title = {Light-assisted dynamic titration: from theory to an experimental protocol}, author = {A Pellissier-Tanon and R Chouket and T Le Saux and L Jullien and A Lemarchand}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85054097721&doi=10.1039%2fc8cp03953d&partnerID=40&md5=782f885754810c59f73c4a3134f6355f}, doi = {10.1039/c8cp03953d}, year = {2018}, date = {2018-01-01}, journal = {Physical Chemistry Chemical Physics}, volume = {20}, number = {37}, pages = {23998--24010}, abstract = {In order to design a dynamic titration method, we propose a theoretical model harnessing the kinetic properties of the complexation of the titrated species with a titrating photoswitchable reagent. Forced oscillations of illumination are imposed and concentration oscillations of the targeted species are deduced from the equations of chemical kinetics. We determine analytical expressions of the resonance conditions on the control parameters, angular frequency, mean light intensity, and total concentration of the photoswitchable reagent, which optimize the out-of-phase amplitude of concentration oscillations. A user-friendly protocol of dynamic titration is proposed. © the Owner Societies.}, keywords = {}, pubstate = {published}, tppubtype = {article} } In order to design a dynamic titration method, we propose a theoretical model harnessing the kinetic properties of the complexation of the titrated species with a titrating photoswitchable reagent. Forced oscillations of illumination are imposed and concentration oscillations of the targeted species are deduced from the equations of chemical kinetics. We determine analytical expressions of the resonance conditions on the control parameters, angular frequency, mean light intensity, and total concentration of the photoswitchable reagent, which optimize the out-of-phase amplitude of concentration oscillations. A user-friendly protocol of dynamic titration is proposed. © the Owner Societies. |
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). |
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. |