Post-doctorante
ENS – Département de chimie
24 rue Lhomond, 75005 Paris
Email: alison.tebo@ens.psl.eu
Phone: 0144322410
Office: ES129b
Short bio
Education and professional experience
- 2010 – B.S. UCLA, Biochemistry
- 2015 – Ph.D. University of Michigan, Chemical Biology
Research interests
- List of keywords and themes
Awards and distinctions
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Supervised students and post-doctorants
- Currents and formers
Significant publications
- You can choose the full list of publications (below) or only selected ones
Publications
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. |
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. |
Development of a Rubredoxin-Type Center Embedded in a de Dovo-Designed Three-Helix Bundle Article de journal Alison G Tebo; Tyler B J Pinter; Ricardo García-Serres; Amy L Speelman; Cédric Tard; Olivier Sénèque; Geneviève Blondin; Jean-Marc Latour; James Penner-Hahn; Nicolai Lehnert; Vincent L Pecoraro Biochemistry, 57 (16), p. 2308-2316, 2018. @article{Tebo:2018b, title = {Development of a Rubredoxin-Type Center Embedded in a de Dovo-Designed Three-Helix Bundle}, author = {Alison G Tebo and Tyler B J Pinter and Ricardo {García-Serres} and Amy L Speelman and Cédric Tard and Olivier Sénèque and Geneviève Blondin and Jean-Marc Latour and James {Penner-Hahn} and Nicolai Lehnert and Vincent L Pecoraro}, doi = {10.1021/acs.biochem.8b00091}, year = {2018}, date = {2018-03-01}, journal = {Biochemistry}, volume = {57}, number = {16}, pages = {2308-2316}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
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). |
Modifying the Steric Properties in the Second Coordination Sphere of Designed Peptides Leads to Enhancement of Nitrite Reductase Activity Article de journal Karl J Koebke; Fangting Yu; Elvin Salerno; Casey Van Stappen; Alison G Tebo; James E Penner-Hahn; Vincent L Pecoraro Angewandte Chemie International Edition, 57 (15), p. 3954-3957, 2018. @article{Koebke:2018a, title = {Modifying the Steric Properties in the Second Coordination Sphere of Designed Peptides Leads to Enhancement of Nitrite Reductase Activity}, author = {Karl J Koebke and Fangting Yu and Elvin Salerno and Casey Van Stappen and Alison G Tebo and James E {Penner-Hahn} and Vincent L Pecoraro}, doi = {10.1002/anie.201712757}, year = {2018}, date = {2018-01-01}, journal = {Angewandte Chemie International Edition}, volume = {57}, number = {15}, pages = {3954-3957}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
2017 |
Discovery of Chemoautotrophic Symbiosis in the Giant Shipworm Kuphus Polythalamia(Bivalvia: Teredinidae) Extends Wooden-Steps Theory Article de journal Daniel L Distel; Marvin A Altamia; Zhenjian Lin; Reuben J Shipway; Andrew Han; Imelda Forteza; Rowena Antemano; Ma Gwen Pe~naflor J Limbaco; Alison G Tebo; Rande Dechavez; Julie Albano; Gary Rosenberg; Gisela P Concepcion; Eric W Schmidt; Margo G Haygood Proceedings of the National Academy of Sciences, 114 (18), p. E3652-E3658, 2017. @article{Distel:2017, title = {Discovery of Chemoautotrophic Symbiosis in the Giant Shipworm Kuphus Polythalamia(Bivalvia: Teredinidae) Extends Wooden-Steps Theory}, author = {Daniel L Distel and Marvin A Altamia and Zhenjian Lin and Reuben J Shipway and Andrew Han and Imelda Forteza and Rowena Antemano and Ma Gwen Pe{~n}aflor J Limbaco and Alison G Tebo and Rande Dechavez and Julie Albano and Gary Rosenberg and Gisela P Concepcion and Eric W Schmidt and Margo G Haygood}, doi = {10.1073/pnas.1620470114}, year = {2017}, date = {2017-05-01}, journal = {Proceedings of the National Academy of Sciences}, volume = {114}, number = {18}, pages = {E3652-E3658}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
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. |
Intramolecular Photogeneration of a Tyrosine Radical in a Designed Protein Article de journal Alison G Tebo; Annamaria Quaranta; Christian Herrero; Vincent L Pecoraro; Ally Aukauloo ChemPhotoChem, 1 (3), p. 89-92, 2017. @article{Tebo:2017, title = {Intramolecular Photogeneration of a Tyrosine Radical in a Designed Protein}, author = {Alison G Tebo and Annamaria Quaranta and Christian Herrero and Vincent L Pecoraro and Ally Aukauloo}, doi = {10.1002/cptc.201600044}, year = {2017}, date = {2017-02-01}, journal = {ChemPhotoChem}, volume = {1}, number = {3}, pages = {89-92}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
2015 |
Artificial Metalloenzymes Derived from Three-Helix Bundles. Article de journal Alison G Tebo; Vincent L Pecoraro Current Opinion in Chemical Biology, 25C , p. 65-70, 2015. @article{Tebo:2015a, title = {Artificial Metalloenzymes Derived from Three-Helix Bundles.}, author = {Alison G Tebo and Vincent L Pecoraro}, doi = {10.1016/j.cbpa.2014.12.034}, year = {2015}, date = {2015-01-01}, journal = {Current Opinion in Chemical Biology}, volume = {25C}, pages = {65-70}, abstract = {Three-helix bundles and coiled-coil motifs are well-established de novo designed scaffolds that have been investigated for their metal-binding and catalytic properties. Satisfaction of the primary coordination sphere for a given metal is sufficient to introduce catalytic activity and a given structure may catalyze different reactions dependent on the identity of the incorporated metal. Here we describe recent contributions in the de novo design of metalloenzymes based on three-helix bundles and coiled-coil motifs, focusing on non-heme systems for hydrolytic and redox chemistry.}, keywords = {}, pubstate = {published}, tppubtype = {article} } Three-helix bundles and coiled-coil motifs are well-established de novo designed scaffolds that have been investigated for their metal-binding and catalytic properties. Satisfaction of the primary coordination sphere for a given metal is sufficient to introduce catalytic activity and a given structure may catalyze different reactions dependent on the identity of the incorporated metal. Here we describe recent contributions in the de novo design of metalloenzymes based on three-helix bundles and coiled-coil motifs, focusing on non-heme systems for hydrolytic and redox chemistry. |
Variable Primary Coordination Environments of Cd(II) Binding to Three Helix Bundles Provide a Pathway for Rapid Metal Exchange. Article de journal Alison G Tebo; Lars Hemmingsen; Vincent L Pecoraro Metallomics, 7 (12), p. 1555-1561, 2015. @article{Tebo:2015, title = {Variable Primary Coordination Environments of Cd(II) Binding to Three Helix Bundles Provide a Pathway for Rapid Metal Exchange.}, author = {Alison G Tebo and Lars Hemmingsen and Vincent L Pecoraro}, doi = {10.1039/c5mt00228a}, year = {2015}, date = {2015-01-01}, journal = {Metallomics}, volume = {7}, number = {12}, pages = {1555-1561}, abstract = {Members of the ArsR/SmtB family of transcriptional repressors, such as CadC, regulate the intracellular levels of heavy metals like Cd(II), Hg(II), and Pb(II). These metal sensing proteins bind their target metals with high specificity and affinity, however, a lack of structural information about these proteins makes defining the coordination sphere of the target metal difficult. Lingering questions as to the identity of Cd(II) coordination in CadC are addressed via protein design techniques. Two designed peptides with tetrathiolate metal binding sites were prepared and characterized, revealing fast exchange between CdS3O and CdS4 coordination spheres. Correlation of (111m)Cd PAC spectroscopy and (113)Cd NMR spectroscopy suggests that Cd(II) coordinated to CadC is in fast exchange between CdS3O and CdS4 forms, which may provide a mechanism for rapid sensing of heavy metal contaminants by this regulatory protein.}, keywords = {}, pubstate = {published}, tppubtype = {article} } Members of the ArsR/SmtB family of transcriptional repressors, such as CadC, regulate the intracellular levels of heavy metals like Cd(II), Hg(II), and Pb(II). These metal sensing proteins bind their target metals with high specificity and affinity, however, a lack of structural information about these proteins makes defining the coordination sphere of the target metal difficult. Lingering questions as to the identity of Cd(II) coordination in CadC are addressed via protein design techniques. Two designed peptides with tetrathiolate metal binding sites were prepared and characterized, revealing fast exchange between CdS3O and CdS4 coordination spheres. Correlation of (111m)Cd PAC spectroscopy and (113)Cd NMR spectroscopy suggests that Cd(II) coordinated to CadC is in fast exchange between CdS3O and CdS4 forms, which may provide a mechanism for rapid sensing of heavy metal contaminants by this regulatory protein. |
2014 |
Porphyrins and Metalloporphyrins at Components in Artificial Photosynthesis Research incollection A Tebo; C Herrero; A Aukauloo Kadish, Karl M; Smith, Kevin M; Guilard, Roger (Ed.): Handbook of Porphyrin Science, 34 , p. 196-233, World Scientific Pulishing, Singapore, 2014, ISBN: 978-981-4425-10-0. @incollection{Tebo:2014, title = {Porphyrins and Metalloporphyrins at Components in Artificial Photosynthesis Research}, author = {A Tebo and C Herrero and A Aukauloo}, editor = {Karl M Kadish and Kevin M Smith and Roger Guilard}, doi = {10.1142/9789814417297_0016}, isbn = {978-981-4425-10-0}, year = {2014}, date = {2014-01-01}, booktitle = {Handbook of Porphyrin Science}, volume = {34}, pages = {196-233}, publisher = {World Scientific Pulishing}, address = {Singapore}, keywords = {}, pubstate = {published}, tppubtype = {incollection} } |
Protein Design: Toward Functional Metalloenzymes. Article de journal Fangting Yu; Virginia M Cangelosi; Melissa L Zastrow; Matteo Tegoni; Jefferson S Plegaria; Alison G Tebo; Catherine S Mocny; Leela Ruckthong; Hira Qayyum; Vincent L Pecoraro Chemical reviews, 114 (7), p. 3495-3578, 2014. @article{Yu:2014, title = {Protein Design: Toward Functional Metalloenzymes.}, author = {Fangting Yu and Virginia M Cangelosi and Melissa L Zastrow and Matteo Tegoni and Jefferson S Plegaria and Alison G Tebo and Catherine S Mocny and Leela Ruckthong and Hira Qayyum and Vincent L Pecoraro}, doi = {10.1021/cr400458x}, year = {2014}, date = {2014-04-01}, journal = {Chemical reviews}, volume = {114}, number = {7}, pages = {3495-3578}, keywords = {}, pubstate = {published}, tppubtype = {article} } |