[{"publist_id":"6451","author":[{"full_name":"Clifton, Ben","last_name":"Clifton","first_name":"Ben"},{"first_name":"Jason","full_name":"Whitfield, Jason","last_name":"Whitfield"},{"first_name":"Inmaculada","id":"3D9C5D30-F248-11E8-B48F-1D18A9856A87","full_name":"Sanchez Romero, Inmaculada","last_name":"Sanchez Romero"},{"first_name":"Michel","last_name":"Herde","full_name":"Herde, Michel"},{"first_name":"Christian","last_name":"Henneberger","full_name":"Henneberger, Christian"},{"orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L","last_name":"Janovjak","first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Jackson, Colin","last_name":"Jackson","first_name":"Colin"}],"title":"Ancestral protein reconstruction and circular permutation for improving the stability and dynamic range of FRET sensors","editor":[{"first_name":"Viktor","full_name":"Stein, Viktor","last_name":"Stein"}],"citation":{"ista":"Clifton B, Whitfield J, Sanchez-Romero I, Herde M, Henneberger C, Janovjak HL, Jackson C. 2017.Ancestral protein reconstruction and circular permutation for improving the stability and dynamic range of FRET sensors. In: Synthetic Protein Switches. Methods in Molecular Biology, vol. 1596, 71–87.","chicago":"Clifton, Ben, Jason Whitfield, Inmaculada Sanchez-Romero, Michel Herde, Christian Henneberger, Harald L Janovjak, and Colin Jackson. “Ancestral Protein Reconstruction and Circular Permutation for Improving the Stability and Dynamic Range of FRET Sensors.” In Synthetic Protein Switches, edited by Viktor Stein, 1596:71–87. Synthetic Protein Switches. Springer, 2017. https://doi.org/10.1007/978-1-4939-6940-1_5.","ama":"Clifton B, Whitfield J, Sanchez-Romero I, et al. Ancestral protein reconstruction and circular permutation for improving the stability and dynamic range of FRET sensors. In: Stein V, ed. Synthetic Protein Switches. Vol 1596. Synthetic Protein Switches. Springer; 2017:71-87. doi:10.1007/978-1-4939-6940-1_5","apa":"Clifton, B., Whitfield, J., Sanchez-Romero, I., Herde, M., Henneberger, C., Janovjak, H. L., & Jackson, C. (2017). Ancestral protein reconstruction and circular permutation for improving the stability and dynamic range of FRET sensors. In V. Stein (Ed.), Synthetic Protein Switches (Vol. 1596, pp. 71–87). Springer. https://doi.org/10.1007/978-1-4939-6940-1_5","ieee":"B. Clifton et al., “Ancestral protein reconstruction and circular permutation for improving the stability and dynamic range of FRET sensors,” in Synthetic Protein Switches, vol. 1596, V. Stein, Ed. Springer, 2017, pp. 71–87.","short":"B. Clifton, J. Whitfield, I. Sanchez-Romero, M. Herde, C. Henneberger, H.L. Janovjak, C. Jackson, in:, V. Stein (Ed.), Synthetic Protein Switches, Springer, 2017, pp. 71–87.","mla":"Clifton, Ben, et al. “Ancestral Protein Reconstruction and Circular Permutation for Improving the Stability and Dynamic Range of FRET Sensors.” Synthetic Protein Switches, edited by Viktor Stein, vol. 1596, Springer, 2017, pp. 71–87, doi:10.1007/978-1-4939-6940-1_5."},"user_id":"4435EBFC-F248-11E8-B48F-1D18A9856A87","project":[{"_id":"255BFFFA-B435-11E9-9278-68D0E5697425","grant_number":"RGY0084/2012","name":"In situ real-time imaging of neurotransmitter signaling using designer optical sensors (HFSP Young Investigator)"}],"page":"71 - 87","date_created":"2018-12-11T11:49:24Z","date_published":"2017-03-15T00:00:00Z","doi":"10.1007/978-1-4939-6940-1_5","year":"2017","publication":"Synthetic Protein Switches","day":"15","quality_controlled":"1","publisher":"Springer","department":[{"_id":"HaJa"}],"date_updated":"2021-01-12T08:22:13Z","type":"book_chapter","status":"public","_id":"957","series_title":"Synthetic Protein Switches","volume":1596,"publication_status":"published","publication_identifier":{"issn":["10643745"]},"language":[{"iso":"eng"}],"scopus_import":1,"alternative_title":["Methods in Molecular Biology"],"intvolume":" 1596","month":"03","abstract":[{"lang":"eng","text":"Small molecule biosensors based on Forster resonance energy transfer (FRET) enable small molecule signaling to be monitored with high spatial and temporal resolution in complex cellular environments. FRET sensors can be constructed by fusing a pair of fluorescent proteins to a suitable recognition domain, such as a member of the solute-binding protein (SBP) superfamily. However, naturally occurring SBPs may be unsuitable for incorporation into FRET sensors due to their low thermostability, which may preclude imaging under physiological conditions, or because the positions of their N- and C-termini may be suboptimal for fusion of fluorescent proteins, which may limit the dynamic range of the resulting sensors. Here, we show how these problems can be overcome using ancestral protein reconstruction and circular permutation. Ancestral protein reconstruction, used as a protein engineering strategy, leverages phylogenetic information to improve the thermostability of proteins, while circular permutation enables the termini of an SBP to be repositioned to maximize the dynamic range of the resulting FRET sensor. We also provide a protocol for cloning the engineered SBPs into FRET sensor constructs using Golden Gate assembly and discuss considerations for in situ characterization of the FRET sensors."}],"oa_version":"None"},{"publisher":"Springer","quality_controlled":"1","year":"2017","day":"15","publication":"Synthetic Protein Switches","page":"89 - 99","date_published":"2017-05-15T00:00:00Z","doi":"10.1007/978-1-4939-6940-1_6","date_created":"2018-12-11T11:49:24Z","citation":{"mla":"Mitchell, Joshua, et al. “Method for Developing Optical Sensors Using a Synthetic Dye Fluorescent Protein FRET Pair and Computational Modeling and Assessment.” Synthetic Protein Switches, edited by Viktor Stein, vol. 1596, Springer, 2017, pp. 89–99, doi:10.1007/978-1-4939-6940-1_6.","apa":"Mitchell, J., Zhang, W., Herde, M., Henneberger, C., Janovjak, H. L., O’Mara, M., & Jackson, C. (2017). Method for developing optical sensors using a synthetic dye fluorescent protein FRET pair and computational modeling and assessment. In V. Stein (Ed.), Synthetic Protein Switches (Vol. 1596, pp. 89–99). Springer. https://doi.org/10.1007/978-1-4939-6940-1_6","ama":"Mitchell J, Zhang W, Herde M, et al. Method for developing optical sensors using a synthetic dye fluorescent protein FRET pair and computational modeling and assessment. In: Stein V, ed. Synthetic Protein Switches. Vol 1596. Synthetic Protein Switches. Springer; 2017:89-99. doi:10.1007/978-1-4939-6940-1_6","ieee":"J. Mitchell et al., “Method for developing optical sensors using a synthetic dye fluorescent protein FRET pair and computational modeling and assessment,” in Synthetic Protein Switches, vol. 1596, V. Stein, Ed. Springer, 2017, pp. 89–99.","short":"J. Mitchell, W. Zhang, M. Herde, C. Henneberger, H.L. Janovjak, M. O’Mara, C. Jackson, in:, V. Stein (Ed.), Synthetic Protein Switches, Springer, 2017, pp. 89–99.","chicago":"Mitchell, Joshua, William Zhang, Michel Herde, Christian Henneberger, Harald L Janovjak, Megan O’Mara, and Colin Jackson. “Method for Developing Optical Sensors Using a Synthetic Dye Fluorescent Protein FRET Pair and Computational Modeling and Assessment.” In Synthetic Protein Switches, edited by Viktor Stein, 1596:89–99. Synthetic Protein Switches. Springer, 2017. https://doi.org/10.1007/978-1-4939-6940-1_6.","ista":"Mitchell J, Zhang W, Herde M, Henneberger C, Janovjak HL, O’Mara M, Jackson C. 2017.Method for developing optical sensors using a synthetic dye fluorescent protein FRET pair and computational modeling and assessment. In: Synthetic Protein Switches. Methods in Molecular Biology, vol. 1596, 89–99."},"user_id":"4435EBFC-F248-11E8-B48F-1D18A9856A87","publist_id":"6450","author":[{"first_name":"Joshua","full_name":"Mitchell, Joshua","last_name":"Mitchell"},{"first_name":"William","last_name":"Zhang","full_name":"Zhang, William"},{"last_name":"Herde","full_name":"Herde, Michel","first_name":"Michel"},{"full_name":"Henneberger, Christian","last_name":"Henneberger","first_name":"Christian"},{"full_name":"Janovjak, Harald L","orcid":"0000-0002-8023-9315","last_name":"Janovjak","first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87"},{"full_name":"O'Mara, Megan","last_name":"O'Mara","first_name":"Megan"},{"last_name":"Jackson","full_name":"Jackson, Colin","first_name":"Colin"}],"title":"Method for developing optical sensors using a synthetic dye fluorescent protein FRET pair and computational modeling and assessment","editor":[{"last_name":"Stein","full_name":"Stein, Viktor","first_name":"Viktor"}],"abstract":[{"text":"Biosensors that exploit Forster resonance energy transfer (FRET) can be used to visualize biological and physiological processes and are capable of providing detailed information in both spatial and temporal dimensions. In a FRET-based biosensor, substrate binding is associated with a change in the relative positions of two fluorophores, leading to a change in FRET efficiency that may be observed in the fluorescence spectrum. As a result, their design requires a ligand-binding protein that exhibits a conformational change upon binding. However, not all ligand-binding proteins produce responsive sensors upon conjugation to fluorescent proteins or dyes, and identifying the optimum locations for the fluorophores often involves labor-intensive iterative design or high-throughput screening. Combining the genetic fusion of a fluorescent protein to the ligand-binding protein with site-specific covalent attachment of a fluorescent dye can allow fine control over the positions of the two fluorophores, allowing the construction of very sensitive sensors. This relies upon the accurate prediction of the locations of the two fluorophores in bound and unbound states. In this chapter, we describe a method for computational identification of dye-attachment sites that allows the use of cysteine modification to attach synthetic dyes that can be paired with a fluorescent protein for the purposes of creating FRET sensors.","lang":"eng"}],"oa_version":"None","alternative_title":["Methods in Molecular Biology"],"scopus_import":1,"month":"05","intvolume":" 1596","publication_identifier":{"issn":["10643745"]},"publication_status":"published","language":[{"iso":"eng"}],"volume":1596,"_id":"958","series_title":"Synthetic Protein Switches","type":"book_chapter","status":"public","date_updated":"2021-01-12T08:22:13Z","department":[{"_id":"HaJa"}]},{"_id":"1026","status":"public","type":"journal_article","article_type":"original","date_updated":"2023-09-22T09:26:06Z","department":[{"_id":"HaJa"}],"oa_version":"None","abstract":[{"lang":"eng","text":"The optogenetic revolution enabled spatially-precise and temporally-precise control over protein function, signaling pathway activation, and animal behavior with tremendous success in the dissection of signaling networks and neural circuits. Very recently, optogenetic methods have been paired with optical reporters in novel drug screening platforms. In these all-optical platforms, light remotely activated ion channels and kinases thereby obviating the use of electrophysiology or reagents. Consequences were remarkable operational simplicity, throughput, and cost-effectiveness that culminated in the identification of new drug candidates. These blueprints for all-optical assays also revealed potential pitfalls and inspire all-optical variants of other screens, such as those that aim at better understanding dynamic drug action or orphan protein function."}],"intvolume":" 48","month":"12","scopus_import":"1","language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["09581669"]},"ec_funded":1,"volume":48,"project":[{"_id":"255BFFFA-B435-11E9-9278-68D0E5697425","grant_number":"RGY0084/2012","name":"In situ real-time imaging of neurotransmitter signaling using designer optical sensors (HFSP Young Investigator)"},{"call_identifier":"FP7","_id":"25548C20-B435-11E9-9278-68D0E5697425","name":"Microbial Ion Channels for Synthetic Neurobiology","grant_number":"303564"},{"grant_number":"W1232-B24","name":"Molecular Drug Targets","_id":"255A6082-B435-11E9-9278-68D0E5697425","call_identifier":"FWF"}],"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","citation":{"ieee":"V. Agus and H. L. Janovjak, “Optogenetic methods in drug screening: Technologies and applications,” Current Opinion in Biotechnology, vol. 48. Elsevier, pp. 8–14, 2017.","short":"V. Agus, H.L. Janovjak, Current Opinion in Biotechnology 48 (2017) 8–14.","apa":"Agus, V., & Janovjak, H. L. (2017). Optogenetic methods in drug screening: Technologies and applications. Current Opinion in Biotechnology. Elsevier. https://doi.org/10.1016/j.copbio.2017.02.006","ama":"Agus V, Janovjak HL. Optogenetic methods in drug screening: Technologies and applications. Current Opinion in Biotechnology. 2017;48:8-14. doi:10.1016/j.copbio.2017.02.006","mla":"Agus, Viviana, and Harald L. Janovjak. “Optogenetic Methods in Drug Screening: Technologies and Applications.” Current Opinion in Biotechnology, vol. 48, Elsevier, 2017, pp. 8–14, doi:10.1016/j.copbio.2017.02.006.","ista":"Agus V, Janovjak HL. 2017. Optogenetic methods in drug screening: Technologies and applications. Current Opinion in Biotechnology. 48, 8–14.","chicago":"Agus, Viviana, and Harald L Janovjak. “Optogenetic Methods in Drug Screening: Technologies and Applications.” Current Opinion in Biotechnology. Elsevier, 2017. https://doi.org/10.1016/j.copbio.2017.02.006."},"title":"Optogenetic methods in drug screening: Technologies and applications","external_id":{"isi":["000418313200003"]},"article_processing_charge":"No","publist_id":"6365","author":[{"last_name":"Agus","full_name":"Agus, Viviana","first_name":"Viviana"},{"last_name":"Janovjak","full_name":"Janovjak, Harald L","orcid":"0000-0002-8023-9315","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","first_name":"Harald L"}],"acknowledgement":"This work was supported by grants of the European Union Seventh Framework Programme (CIG-303564), the Human Frontier Science Program (RGY0084_2012), and the Austrian Science Fund FWF (W1232 MolecularDrugTargets).","publisher":"Elsevier","quality_controlled":"1","publication":"Current Opinion in Biotechnology","day":"01","year":"2017","isi":1,"date_created":"2018-12-11T11:49:45Z","doi":"10.1016/j.copbio.2017.02.006","date_published":"2017-12-01T00:00:00Z","page":"8 - 14"},{"related_material":{"record":[{"relation":"dissertation_contains","status":"public","id":"418"},{"id":"7680","status":"public","relation":"part_of_dissertation"}]},"volume":56,"issue":"16","ec_funded":1,"file":[{"file_name":"2017_communications_Kainrath.pdf","date_created":"2019-01-18T09:39:55Z","file_size":2614942,"date_updated":"2019-01-18T09:39:55Z","creator":"dernst","success":1,"file_id":"5845","content_type":"application/pdf","relation":"main_file","access_level":"open_access"}],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["14337851"]},"publication_status":"published","month":"03","intvolume":" 56","scopus_import":"1","oa_version":"Published Version","abstract":[{"lang":"eng","text":"Optogenetics and photopharmacology provide spatiotemporally precise control over protein interactions and protein function in cells and animals. Optogenetic methods that are sensitive to green light and can be used to break protein complexes are not broadly available but would enable multichromatic experiments with previously inaccessible biological targets. Herein, we repurposed cobalamin (vitamin B12) binding domains of bacterial CarH transcription factors for green-light-induced receptor dissociation. In cultured cells, we observed oligomerization-induced cell signaling for the fibroblast growth factor receptor 1 fused to cobalamin-binding domains in the dark that was rapidly eliminated upon illumination. In zebrafish embryos expressing fusion receptors, green light endowed control over aberrant fibroblast growth factor signaling during development. Green-light-induced domain dissociation and light-inactivated receptors will critically expand the optogenetic toolbox for control of biological processes."}],"department":[{"_id":"CaGu"},{"_id":"HaJa"}],"file_date_updated":"2019-01-18T09:39:55Z","ddc":["540"],"date_updated":"2024-03-27T23:30:13Z","status":"public","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"_id":"1028","doi":"10.1002/anie.201611998","date_published":"2017-03-20T00:00:00Z","date_created":"2018-12-11T11:49:46Z","page":"4608-4611","day":"20","publication":"Angewandte Chemie - International Edition","has_accepted_license":"1","isi":1,"year":"2017","quality_controlled":"1","publisher":"Wiley-Blackwell","oa":1,"acknowledgement":"This work was supported by a grant from the European Unions Seventh Framework Programme (CIG-303564). E.R. was supported by the graduate program MolecularDrugTargets (Austrian Science Fund (FWF), W1232) and a FemTech fellowship (Austrian Research Promotion Agency, 3580812)","title":"Green-light-induced inactivation of receptor signaling using cobalamin-binding domains","author":[{"last_name":"Kainrath","full_name":"Kainrath, Stephanie","first_name":"Stephanie","id":"32CFBA64-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Manuela","full_name":"Stadler, Manuela","last_name":"Stadler"},{"last_name":"Gschaider-Reichhart","orcid":"0000-0002-7218-7738","full_name":"Gschaider-Reichhart, Eva","first_name":"Eva","id":"3FEE232A-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Martin","last_name":"Distel","full_name":"Distel, Martin"},{"first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L","last_name":"Janovjak"}],"publist_id":"6362","article_processing_charge":"No","external_id":{"isi":["000398154000038"]},"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","citation":{"mla":"Kainrath, Stephanie, et al. “Green-Light-Induced Inactivation of Receptor Signaling Using Cobalamin-Binding Domains.” Angewandte Chemie - International Edition, vol. 56, no. 16, Wiley-Blackwell, 2017, pp. 4608–11, doi:10.1002/anie.201611998.","apa":"Kainrath, S., Stadler, M., Gschaider-Reichhart, E., Distel, M., & Janovjak, H. L. (2017). Green-light-induced inactivation of receptor signaling using cobalamin-binding domains. Angewandte Chemie - International Edition. Wiley-Blackwell. https://doi.org/10.1002/anie.201611998","ama":"Kainrath S, Stadler M, Gschaider-Reichhart E, Distel M, Janovjak HL. Green-light-induced inactivation of receptor signaling using cobalamin-binding domains. Angewandte Chemie - International Edition. 2017;56(16):4608-4611. doi:10.1002/anie.201611998","short":"S. Kainrath, M. Stadler, E. Gschaider-Reichhart, M. Distel, H.L. Janovjak, Angewandte Chemie - International Edition 56 (2017) 4608–4611.","ieee":"S. Kainrath, M. Stadler, E. Gschaider-Reichhart, M. Distel, and H. L. Janovjak, “Green-light-induced inactivation of receptor signaling using cobalamin-binding domains,” Angewandte Chemie - International Edition, vol. 56, no. 16. Wiley-Blackwell, pp. 4608–4611, 2017.","chicago":"Kainrath, Stephanie, Manuela Stadler, Eva Gschaider-Reichhart, Martin Distel, and Harald L Janovjak. “Green-Light-Induced Inactivation of Receptor Signaling Using Cobalamin-Binding Domains.” Angewandte Chemie - International Edition. Wiley-Blackwell, 2017. https://doi.org/10.1002/anie.201611998.","ista":"Kainrath S, Stadler M, Gschaider-Reichhart E, Distel M, Janovjak HL. 2017. Green-light-induced inactivation of receptor signaling using cobalamin-binding domains. Angewandte Chemie - International Edition. 56(16), 4608–4611."},"project":[{"name":"Microbial Ion Channels for Synthetic Neurobiology","grant_number":"303564","call_identifier":"FP7","_id":"25548C20-B435-11E9-9278-68D0E5697425"},{"grant_number":"W1232-B24","name":"Molecular Drug Targets [do not use to be deleted]","_id":"26AA4EF2-B435-11E9-9278-68D0E5697425","call_identifier":"FWF"}]},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2021-01-12T06:50:46Z","citation":{"ieee":"H. L. Janovjak, “Light at the end of the protein: Crystal structure of a C-terminal light-sensing domain,” Structure, vol. 24, no. 2. Cell Press, pp. 213–215, 2016.","short":"H.L. Janovjak, Structure 24 (2016) 213–215.","apa":"Janovjak, H. L. (2016). Light at the end of the protein: Crystal structure of a C-terminal light-sensing domain. Structure. Cell Press. https://doi.org/10.1016/j.str.2016.01.002","ama":"Janovjak HL. Light at the end of the protein: Crystal structure of a C-terminal light-sensing domain. Structure. 2016;24(2):213-215. doi:10.1016/j.str.2016.01.002","mla":"Janovjak, Harald L. “Light at the End of the Protein: Crystal Structure of a C-Terminal Light-Sensing Domain.” Structure, vol. 24, no. 2, Cell Press, 2016, pp. 213–15, doi:10.1016/j.str.2016.01.002.","ista":"Janovjak HL. 2016. Light at the end of the protein: Crystal structure of a C-terminal light-sensing domain. Structure. 24(2), 213–215.","chicago":"Janovjak, Harald L. “Light at the End of the Protein: Crystal Structure of a C-Terminal Light-Sensing Domain.” Structure. Cell Press, 2016. https://doi.org/10.1016/j.str.2016.01.002."},"department":[{"_id":"HaJa"}],"title":"Light at the end of the protein: Crystal structure of a C-terminal light-sensing domain","publist_id":"5756","author":[{"last_name":"Janovjak","orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L","first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87"}],"_id":"1440","project":[{"_id":"255BFFFA-B435-11E9-9278-68D0E5697425","name":"In situ real-time imaging of neurotransmitter signaling using designer optical sensors (HFSP Young Investigator)","grant_number":"RGY0084/2012"},{"grant_number":"303564","name":"Microbial Ion Channels for Synthetic Neurobiology","call_identifier":"FP7","_id":"25548C20-B435-11E9-9278-68D0E5697425"},{"call_identifier":"FWF","_id":"255A6082-B435-11E9-9278-68D0E5697425","name":"Molecular Drug Targets","grant_number":"W1232-B24"}],"status":"public","type":"journal_article","publication":"Structure","language":[{"iso":"eng"}],"day":"02","publication_status":"published","year":"2016","date_created":"2018-12-11T11:52:02Z","ec_funded":1,"issue":"2","doi":"10.1016/j.str.2016.01.002","volume":24,"date_published":"2016-02-02T00:00:00Z","page":"213 - 215","acknowledgement":"The author thanks Banerjee et al. (2016) for providing coordinates prior to public release and apologizes to colleagues whose work was not cited or discussed due to the limited space available. The author is supported by grants from EU FP7 (CIG-303564), HFSP (RGY0084_2012), and FWF (W1232).","oa_version":"None","intvolume":" 24","month":"02","publisher":"Cell Press","scopus_import":1,"quality_controlled":"1"},{"title":"Rangefinder: A semisynthetic FRET sensor design algorithm","department":[{"_id":"HaJa"}],"author":[{"last_name":"Mitchell","full_name":"Mitchell, Joshua","first_name":"Joshua"},{"first_name":"Jason","full_name":"Whitfield, Jason","last_name":"Whitfield"},{"first_name":"William","full_name":"Zhang, William","last_name":"Zhang"},{"first_name":"Christian","last_name":"Henneberger","full_name":"Henneberger, Christian"},{"id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","first_name":"Harald L","orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L","last_name":"Janovjak"},{"first_name":"Megan","last_name":"O'Mara","full_name":"O'Mara, Megan"},{"last_name":"Jackson","full_name":"Jackson, Colin","first_name":"Colin"}],"publist_id":"6274","article_processing_charge":"No","user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","date_updated":"2023-03-30T11:32:33Z","citation":{"chicago":"Mitchell, Joshua, Jason Whitfield, William Zhang, Christian Henneberger, Harald L Janovjak, Megan O’Mara, and Colin Jackson. “Rangefinder: A Semisynthetic FRET Sensor Design Algorithm.” ACS SENSORS. American Chemical Society, 2016. https://doi.org/10.1021/acssensors.6b00576.","ista":"Mitchell J, Whitfield J, Zhang W, Henneberger C, Janovjak HL, O’Mara M, Jackson C. 2016. Rangefinder: A semisynthetic FRET sensor design algorithm. ACS SENSORS. 1(11), 1286–1290.","mla":"Mitchell, Joshua, et al. “Rangefinder: A Semisynthetic FRET Sensor Design Algorithm.” ACS SENSORS, vol. 1, no. 11, American Chemical Society, 2016, pp. 1286–90, doi:10.1021/acssensors.6b00576.","ama":"Mitchell J, Whitfield J, Zhang W, et al. Rangefinder: A semisynthetic FRET sensor design algorithm. ACS SENSORS. 2016;1(11):1286-1290. doi:10.1021/acssensors.6b00576","apa":"Mitchell, J., Whitfield, J., Zhang, W., Henneberger, C., Janovjak, H. L., O’Mara, M., & Jackson, C. (2016). Rangefinder: A semisynthetic FRET sensor design algorithm. ACS SENSORS. American Chemical Society. https://doi.org/10.1021/acssensors.6b00576","short":"J. Mitchell, J. Whitfield, W. Zhang, C. Henneberger, H.L. Janovjak, M. O’Mara, C. Jackson, ACS SENSORS 1 (2016) 1286–1290.","ieee":"J. Mitchell et al., “Rangefinder: A semisynthetic FRET sensor design algorithm,” ACS SENSORS, vol. 1, no. 11. American Chemical Society, pp. 1286–1290, 2016."},"status":"public","type":"journal_article","_id":"1101","date_published":"2016-11-10T00:00:00Z","volume":1,"doi":"10.1021/acssensors.6b00576","issue":"11","date_created":"2018-12-11T11:50:09Z","page":"1286 - 1290","day":"10","language":[{"iso":"eng"}],"publication":"ACS SENSORS","year":"2016","publication_status":"published","month":"11","intvolume":" 1","publisher":"American Chemical Society","quality_controlled":"1","scopus_import":"1","oa_version":"None","acknowledgement":"J.A.M., J.H.W., and W.H.Z. were supported by Australian\r\nPostgraduate Awards (APA), AS Sargeson Supplementary\r\nscholarships, and RSC supplementary scholarships. C.J.J.\r\nacknowledges support from a Human Frontiers in Science\r\nYoung Investigator Award and a Discovery Project and Future\r\nFellowship from the Australian Research Council. M.L.O. is\r\nsupported by an Australian Research Council Discovery Project\r\n(DP130102153) and the Merit Allocation Scheme of the\r\nNational Computational Infrastructure.","abstract":[{"text":"Optical sensors based on the phenomenon of Förster resonance energy transfer (FRET) are powerful tools that have advanced the study of small molecules in biological systems. However, sensor construction is not trivial and often requires multiple rounds of engineering or an ability to screen large numbers of variants. A method that would allow the accurate rational design of FRET sensors would expedite the production of biologically useful sensors. Here, we present Rangefinder, a computational algorithm that allows rapid in silico screening of dye attachment sites in a ligand-binding protein for the conjugation of a dye molecule to act as a Förster acceptor for a fused fluorescent protein. We present three ratiometric fluorescent sensors designed with Rangefinder, including a maltose sensor with a dynamic range of >300% and the first sensors for the most abundant sialic acid in human cells, N-acetylneuraminic acid. Provided a ligand-binding protein exists, it is our expectation that this model will facilitate the design of an optical sensor for any small molecule of interest.","lang":"eng"}]},{"_id":"1124","type":"dissertation","status":"public","supervisor":[{"orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L","last_name":"Janovjak","first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87"}],"date_updated":"2023-09-07T11:43:03Z","citation":{"short":"M. Morri, Optical Functionalization of Human Class A Orphan G-Protein Coupled Receptors, Institute of Science and Technology Austria, 2016.","ieee":"M. Morri, “Optical functionalization of human class A orphan G-protein coupled receptors,” Institute of Science and Technology Austria, 2016.","apa":"Morri, M. (2016). Optical functionalization of human class A orphan G-protein coupled receptors. Institute of Science and Technology Austria.","ama":"Morri M. Optical functionalization of human class A orphan G-protein coupled receptors. 2016.","mla":"Morri, Maurizio. Optical Functionalization of Human Class A Orphan G-Protein Coupled Receptors. Institute of Science and Technology Austria, 2016.","ista":"Morri M. 2016. Optical functionalization of human class A orphan G-protein coupled receptors. Institute of Science and Technology Austria.","chicago":"Morri, Maurizio. “Optical Functionalization of Human Class A Orphan G-Protein Coupled Receptors.” Institute of Science and Technology Austria, 2016."},"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","ddc":["570"],"publist_id":"6236","author":[{"last_name":"Morri","full_name":"Morri, Maurizio","first_name":"Maurizio","id":"4863116E-F248-11E8-B48F-1D18A9856A87"}],"article_processing_charge":"No","department":[{"_id":"HaJa"}],"title":"Optical functionalization of human class A orphan G-protein coupled receptors","file_date_updated":"2021-02-22T11:42:06Z","oa_version":"Published Version","alternative_title":["ISTA Thesis"],"publisher":"Institute of Science and Technology Austria","oa":1,"month":"03","publication_identifier":{"issn":["2663-337X"]},"has_accepted_license":"1","year":"2016","publication_status":"published","degree_awarded":"PhD","day":"01","file":[{"creator":"dernst","file_size":4785167,"date_updated":"2019-08-13T10:50:00Z","file_name":"MORRI_PhD_thesis_FINALPLUSSIGNATURES (2).pdf","date_created":"2019-08-13T10:50:00Z","relation":"main_file","access_level":"closed","content_type":"application/pdf","file_id":"6812","checksum":"b439803ac0827cdddd56562a54e3b53b"},{"success":1,"checksum":"dd4136247fe472e7d47880ec68ac8de0","file_id":"9180","content_type":"application/pdf","relation":"main_file","access_level":"open_access","file_name":"2016_MORRI_Thesis.pdf","date_created":"2021-02-22T11:42:06Z","file_size":4495669,"date_updated":"2021-02-22T11:42:06Z","creator":"dernst"}],"language":[{"iso":"eng"}],"page":"129","date_published":"2016-03-01T00:00:00Z","date_created":"2018-12-11T11:50:17Z"},{"type":"journal_article","status":"public","pubrep_id":"840","_id":"1441","file_date_updated":"2020-07-14T12:44:55Z","department":[{"_id":"HaJa"}],"date_updated":"2023-09-07T12:49:08Z","ddc":["571","576"],"scopus_import":1,"month":"05","intvolume":" 55","abstract":[{"lang":"eng","text":"Optogenetics and photopharmacology enable the spatio-temporal control of cell and animal behavior by light. Although red light offers deep-tissue penetration and minimal phototoxicity, very few red-light-sensitive optogenetic methods are currently available. We have now developed a red-light-induced homodimerization domain. We first showed that an optimized sensory domain of the cyanobacterial phytochrome 1 can be expressed robustly and without cytotoxicity in human cells. We then applied this domain to induce the dimerization of two receptor tyrosine kinases—the fibroblast growth factor receptor 1 and the neurotrophin receptor trkB. This new optogenetic method was then used to activate the MAPK/ERK pathway non-invasively in mammalian tissue and in multicolor cell-signaling experiments. The light-controlled dimerizer and red-light-activated receptor tyrosine kinases will prove useful to regulate a variety of cellular processes with light. Go deep with red: The sensory domain (S) of the cyanobacterial phytochrome 1 (CPH1) was repurposed to induce the homodimerization of proteins in living cells by red light. By using this domain, light-activated protein kinases were engineered that can be activated orthogonally from many fluorescent proteins and through mammalian tissue. Pr/Pfr=red-/far-red-absorbing state of CPH1."}],"oa_version":"Submitted Version","related_material":{"record":[{"id":"418","status":"public","relation":"dissertation_contains"}]},"volume":55,"issue":"21","ec_funded":1,"publication_status":"published","file":[{"file_name":"IST-2017-840-v1+1_reichhart.pdf","date_created":"2018-12-12T10:17:03Z","file_size":1268662,"date_updated":"2020-07-14T12:44:55Z","creator":"system","file_id":"5255","checksum":"26da07960e57ac4750b54179197ce57f","content_type":"application/pdf","relation":"main_file","access_level":"open_access"}],"language":[{"iso":"eng"}],"project":[{"call_identifier":"FP7","_id":"25548C20-B435-11E9-9278-68D0E5697425","name":"Microbial Ion Channels for Synthetic Neurobiology","grant_number":"303564"},{"call_identifier":"FWF","_id":"255A6082-B435-11E9-9278-68D0E5697425","name":"Molecular Drug Targets","grant_number":"W1232-B24"}],"publist_id":"5755","author":[{"first_name":"Eva","id":"3FEE232A-F248-11E8-B48F-1D18A9856A87","last_name":"Gschaider-Reichhart","full_name":"Gschaider-Reichhart, Eva","orcid":"0000-0002-7218-7738"},{"id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","first_name":"Álvaro","full_name":"Inglés Prieto, Álvaro","orcid":"0000-0002-5409-8571","last_name":"Inglés Prieto"},{"id":"29D8BB2C-F248-11E8-B48F-1D18A9856A87","first_name":"Alexandra-Madelaine","last_name":"Tichy","full_name":"Tichy, Alexandra-Madelaine"},{"id":"3EEDE19A-F248-11E8-B48F-1D18A9856A87","first_name":"Catherine","full_name":"Mckenzie, Catherine","last_name":"Mckenzie"},{"last_name":"Janovjak","orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","first_name":"Harald L"}],"title":"A phytochrome sensory domain permits receptor activation by red light","citation":{"ieee":"E. Gschaider-Reichhart, Á. Inglés Prieto, A.-M. Tichy, C. Mckenzie, and H. L. Janovjak, “A phytochrome sensory domain permits receptor activation by red light,” Angewandte Chemie - International Edition, vol. 55, no. 21. Wiley, pp. 6339–6342, 2016.","short":"E. Gschaider-Reichhart, Á. Inglés Prieto, A.-M. Tichy, C. Mckenzie, H.L. Janovjak, Angewandte Chemie - International Edition 55 (2016) 6339–6342.","apa":"Gschaider-Reichhart, E., Inglés Prieto, Á., Tichy, A.-M., Mckenzie, C., & Janovjak, H. L. (2016). A phytochrome sensory domain permits receptor activation by red light. Angewandte Chemie - International Edition. Wiley. https://doi.org/10.1002/anie.201601736","ama":"Gschaider-Reichhart E, Inglés Prieto Á, Tichy A-M, Mckenzie C, Janovjak HL. A phytochrome sensory domain permits receptor activation by red light. Angewandte Chemie - International Edition. 2016;55(21):6339-6342. doi:10.1002/anie.201601736","mla":"Gschaider-Reichhart, Eva, et al. “A Phytochrome Sensory Domain Permits Receptor Activation by Red Light.” Angewandte Chemie - International Edition, vol. 55, no. 21, Wiley, 2016, pp. 6339–42, doi:10.1002/anie.201601736.","ista":"Gschaider-Reichhart E, Inglés Prieto Á, Tichy A-M, Mckenzie C, Janovjak HL. 2016. A phytochrome sensory domain permits receptor activation by red light. Angewandte Chemie - International Edition. 55(21), 6339–6342.","chicago":"Gschaider-Reichhart, Eva, Álvaro Inglés Prieto, Alexandra-Madelaine Tichy, Catherine Mckenzie, and Harald L Janovjak. “A Phytochrome Sensory Domain Permits Receptor Activation by Red Light.” Angewandte Chemie - International Edition. Wiley, 2016. https://doi.org/10.1002/anie.201601736."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Wiley","quality_controlled":"1","oa":1,"acknowledgement":"A.I.-P. was supported by a Ramon Areces fellowship, and E.R. by the graduate program MolecularDrugTargets (Austrian Science Fund (FWF): W1232) and a FemTech fellowship (Austrian Research Promotion Agency: 3580812).","page":"6339 - 6342","doi":"10.1002/anie.201601736","date_published":"2016-05-17T00:00:00Z","date_created":"2018-12-11T11:52:02Z","has_accepted_license":"1","year":"2016","day":"17","publication":"Angewandte Chemie - International Edition"},{"_id":"1100","status":"public","pubrep_id":"754","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"ddc":["570","576"],"date_updated":"2024-03-27T23:30:25Z","department":[{"_id":"CaHe"},{"_id":"HaJa"}],"file_date_updated":"2018-12-12T10:11:04Z","oa_version":"Published Version","acknowledged_ssus":[{"_id":"SSU"}],"abstract":[{"lang":"eng","text":"During metazoan development, the temporal pattern of morphogen signaling is critical for organizing cell fates in space and time. Yet, tools for temporally controlling morphogen signaling within the embryo are still scarce. Here, we developed a photoactivatable Nodal receptor to determine how the temporal pattern of Nodal signaling affects cell fate specification during zebrafish gastrulation. By using this receptor to manipulate the duration of Nodal signaling in vivo by light, we show that extended Nodal signaling within the organizer promotes prechordal plate specification and suppresses endoderm differentiation. Endoderm differentiation is suppressed by extended Nodal signaling inducing expression of the transcriptional repressor goosecoid (gsc) in prechordal plate progenitors, which in turn restrains Nodal signaling from upregulating the endoderm differentiation gene sox17 within these cells. Thus, optogenetic manipulation of Nodal signaling identifies a critical role of Nodal signaling duration for organizer cell fate specification during gastrulation."}],"month":"07","intvolume":" 16","scopus_import":1,"file":[{"file_id":"4857","relation":"main_file","access_level":"open_access","content_type":"application/pdf","file_name":"IST-2017-754-v1+1_1-s2.0-S2211124716307768-main.pdf","date_created":"2018-12-12T10:11:04Z","creator":"system","file_size":3921947,"date_updated":"2018-12-12T10:11:04Z"}],"language":[{"iso":"eng"}],"publication_status":"published","volume":16,"related_material":{"record":[{"status":"public","id":"961","relation":"dissertation_contains"},{"id":"50","status":"public","relation":"dissertation_contains"}]},"issue":"3","ec_funded":1,"project":[{"name":"Cell- and Tissue Mechanics in Zebrafish Germ Layer Formation","grant_number":"T 560-B17","_id":"2529486C-B435-11E9-9278-68D0E5697425","call_identifier":"FWF"},{"grant_number":"I 812-B12","name":"Cell Cortex and Germ Layer Formation in Zebrafish Gastrulation","call_identifier":"FWF","_id":"2527D5CC-B435-11E9-9278-68D0E5697425"},{"name":"Microbial Ion Channels for Synthetic Neurobiology","grant_number":"303564","call_identifier":"FP7","_id":"25548C20-B435-11E9-9278-68D0E5697425"}],"user_id":"4435EBFC-F248-11E8-B48F-1D18A9856A87","citation":{"apa":"Sako, K., Pradhan, S., Barone, V., Inglés Prieto, Á., Mueller, P., Ruprecht, V., … Heisenberg, C.-P. J. (2016). Optogenetic control of nodal signaling reveals a temporal pattern of nodal signaling regulating cell fate specification during gastrulation. Cell Reports. Cell Press. https://doi.org/10.1016/j.celrep.2016.06.036","ama":"Sako K, Pradhan S, Barone V, et al. Optogenetic control of nodal signaling reveals a temporal pattern of nodal signaling regulating cell fate specification during gastrulation. Cell Reports. 2016;16(3):866-877. doi:10.1016/j.celrep.2016.06.036","ieee":"K. Sako et al., “Optogenetic control of nodal signaling reveals a temporal pattern of nodal signaling regulating cell fate specification during gastrulation,” Cell Reports, vol. 16, no. 3. Cell Press, pp. 866–877, 2016.","short":"K. Sako, S. Pradhan, V. Barone, Á. Inglés Prieto, P. Mueller, V. Ruprecht, D. Capek, S. Galande, H.L. Janovjak, C.-P.J. Heisenberg, Cell Reports 16 (2016) 866–877.","mla":"Sako, Keisuke, et al. “Optogenetic Control of Nodal Signaling Reveals a Temporal Pattern of Nodal Signaling Regulating Cell Fate Specification during Gastrulation.” Cell Reports, vol. 16, no. 3, Cell Press, 2016, pp. 866–77, doi:10.1016/j.celrep.2016.06.036.","ista":"Sako K, Pradhan S, Barone V, Inglés Prieto Á, Mueller P, Ruprecht V, Capek D, Galande S, Janovjak HL, Heisenberg C-PJ. 2016. Optogenetic control of nodal signaling reveals a temporal pattern of nodal signaling regulating cell fate specification during gastrulation. Cell Reports. 16(3), 866–877.","chicago":"Sako, Keisuke, Saurabh Pradhan, Vanessa Barone, Álvaro Inglés Prieto, Patrick Mueller, Verena Ruprecht, Daniel Capek, Sanjeev Galande, Harald L Janovjak, and Carl-Philipp J Heisenberg. “Optogenetic Control of Nodal Signaling Reveals a Temporal Pattern of Nodal Signaling Regulating Cell Fate Specification during Gastrulation.” Cell Reports. Cell Press, 2016. https://doi.org/10.1016/j.celrep.2016.06.036."},"title":"Optogenetic control of nodal signaling reveals a temporal pattern of nodal signaling regulating cell fate specification during gastrulation","author":[{"id":"3BED66BE-F248-11E8-B48F-1D18A9856A87","first_name":"Keisuke","last_name":"Sako","orcid":"0000-0002-6453-8075","full_name":"Sako, Keisuke"},{"first_name":"Saurabh","full_name":"Pradhan, Saurabh","last_name":"Pradhan"},{"last_name":"Barone","orcid":"0000-0003-2676-3367","full_name":"Barone, Vanessa","id":"419EECCC-F248-11E8-B48F-1D18A9856A87","first_name":"Vanessa"},{"id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","first_name":"Álvaro","last_name":"Inglés Prieto","full_name":"Inglés Prieto, Álvaro","orcid":"0000-0002-5409-8571"},{"first_name":"Patrick","full_name":"Mueller, Patrick","last_name":"Mueller"},{"last_name":"Ruprecht","full_name":"Ruprecht, Verena","orcid":"0000-0003-4088-8633","id":"4D71A03A-F248-11E8-B48F-1D18A9856A87","first_name":"Verena"},{"first_name":"Daniel","id":"31C42484-F248-11E8-B48F-1D18A9856A87","last_name":"Capek","orcid":"0000-0001-5199-9940","full_name":"Capek, Daniel"},{"first_name":"Sanjeev","full_name":"Galande, Sanjeev","last_name":"Galande"},{"first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Janovjak, Harald L","orcid":"0000-0002-8023-9315","last_name":"Janovjak"},{"last_name":"Heisenberg","full_name":"Heisenberg, Carl-Philipp J","orcid":"0000-0002-0912-4566","id":"39427864-F248-11E8-B48F-1D18A9856A87","first_name":"Carl-Philipp J"}],"publist_id":"6275","acknowledgement":"We are grateful to members of the C.-P.H. and H.J. labs for discussions, R. Hauschild and the different Scientific Service Units at IST Austria for technical help, M. Dravecka for performing initial experiments, A. Schier for reading an earlier version of the manuscript, K.W. Rogers for technical help, and C. Hill, A. Bruce, and L. Solnica-Krezel for sending plasmids. This work was supported by grants from the Austrian Science Foundation (FWF): (T560-B17) and (I 812-B12) to V.R. and C.-P.H., and from the European Union (EU FP7): (6275) to H.J. A.I.-P. is supported by a Ramon Areces fellowship.","publisher":"Cell Press","quality_controlled":"1","oa":1,"day":"19","publication":"Cell Reports","has_accepted_license":"1","year":"2016","doi":"10.1016/j.celrep.2016.06.036","date_published":"2016-07-19T00:00:00Z","date_created":"2018-12-11T11:50:08Z","page":"866 - 877"},{"citation":{"chicago":"Mckenzie, Catherine, Inmaculada Sanchez-Romero, and Harald L Janovjak. “Flipping the Photoswitch: Ion Channels under Light Control.” In Novel Chemical Tools to Study Ion Channel Biology, 869:101–17. Advances in Experimental Medicine and Biology. Springer, 2015. https://doi.org/10.1007/978-1-4939-2845-3_6.","ista":"Mckenzie C, Sanchez-Romero I, Janovjak HL. 2015.Flipping the photoswitch: Ion channels under light control. In: Novel chemical tools to study ion channel biology. vol. 869, 101–117.","mla":"Mckenzie, Catherine, et al. “Flipping the Photoswitch: Ion Channels under Light Control.” Novel Chemical Tools to Study Ion Channel Biology, vol. 869, Springer, 2015, pp. 101–17, doi:10.1007/978-1-4939-2845-3_6.","ama":"Mckenzie C, Sanchez-Romero I, Janovjak HL. Flipping the photoswitch: Ion channels under light control. In: Novel Chemical Tools to Study Ion Channel Biology. Vol 869. Advances in Experimental Medicine and Biology. Springer; 2015:101-117. doi:10.1007/978-1-4939-2845-3_6","apa":"Mckenzie, C., Sanchez-Romero, I., & Janovjak, H. L. (2015). Flipping the photoswitch: Ion channels under light control. In Novel chemical tools to study ion channel biology (Vol. 869, pp. 101–117). Springer. https://doi.org/10.1007/978-1-4939-2845-3_6","ieee":"C. Mckenzie, I. Sanchez-Romero, and H. L. Janovjak, “Flipping the photoswitch: Ion channels under light control,” in Novel chemical tools to study ion channel biology, vol. 869, Springer, 2015, pp. 101–117.","short":"C. Mckenzie, I. Sanchez-Romero, H.L. Janovjak, in:, Novel Chemical Tools to Study Ion Channel Biology, Springer, 2015, pp. 101–117."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publist_id":"5622","author":[{"full_name":"Mckenzie, Catherine","last_name":"Mckenzie","id":"3EEDE19A-F248-11E8-B48F-1D18A9856A87","first_name":"Catherine"},{"last_name":"Sanchez Romero","full_name":"Sanchez Romero, Inmaculada","id":"3D9C5D30-F248-11E8-B48F-1D18A9856A87","first_name":"Inmaculada"},{"id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","first_name":"Harald L","last_name":"Janovjak","full_name":"Janovjak, Harald L","orcid":"0000-0002-8023-9315"}],"title":"Flipping the photoswitch: Ion channels under light control","quality_controlled":"1","publisher":"Springer","oa":1,"has_accepted_license":"1","year":"2015","day":"18","publication":"Novel chemical tools to study ion channel biology","page":"101 - 117","date_published":"2015-09-18T00:00:00Z","doi":"10.1007/978-1-4939-2845-3_6","date_created":"2018-12-11T11:52:39Z","series_title":"Advances in Experimental Medicine and Biology","_id":"1549","type":"book_chapter","status":"public","pubrep_id":"839","date_updated":"2021-01-12T06:51:32Z","ddc":["571","576"],"file_date_updated":"2020-07-14T12:45:01Z","department":[{"_id":"HaJa"}],"abstract":[{"text":"Nature has incorporated small photochromic molecules, colloquially termed 'photoswitches', in photoreceptor proteins to sense optical cues in photo-taxis and vision. While Nature's ability to employ light-responsive functionalities has long been recognized, it was not until recently that scientists designed, synthesized and applied synthetic photochromes to manipulate many of which open rapidly and locally in their native cell types, biological processes with the temporal and spatial resolution of light. Ion channels in particular have come to the forefront of proteins that can be put under the designer control of synthetic photochromes. Photochromic ion channel controllers are comprised of three classes, photochromic soluble ligands (PCLs), photochromic tethered ligands (PTLs) and photochromic crosslinkers (PXs), and in each class ion channel functionality is controlled through reversible changes in photochrome structure. By acting as light-dependent ion channel agonists, antagonist or modulators, photochromic controllers effectively converted a wide range of ion channels, including voltage-gated ion channels, 'leak channels', tri-, tetra- and pentameric ligand-gated ion channels, and temperaturesensitive ion channels, into man-made photoreceptors. Control by photochromes can be reversible, unlike in the case of 'caged' compounds, and non-invasive with high spatial precision, unlike pharmacology and electrical manipulation. Here, we introduce design principles of emerging photochromic molecules that act on ion channels and discuss the impact that these molecules are beginning to have on ion channel biophysics and neuronal physiology.","lang":"eng"}],"oa_version":"Submitted Version","scopus_import":1,"month":"09","intvolume":" 869","publication_identifier":{"isbn":["978-1-4939-2844-6"]},"publication_status":"published","file":[{"file_name":"IST-2017-839-v1+1_mckenzie.pdf","date_created":"2018-12-12T10:11:02Z","creator":"system","file_size":1919655,"date_updated":"2020-07-14T12:45:01Z","checksum":"bd1bfdf2423a0c3b6e7cabfa8b44bc0f","file_id":"4854","relation":"main_file","access_level":"open_access","content_type":"application/pdf"}],"language":[{"iso":"eng"}],"volume":869},{"publication_status":"published","language":[{"iso":"eng"}],"issue":"9","volume":24,"abstract":[{"lang":"eng","text":"Biosensors for signaling molecules allow the study of physiological processes by bringing together the fields of protein engineering, fluorescence imaging, and cell biology. Construction of genetically encoded biosensors generally relies on the availability of a binding "core" that is both specific and stable, which can then be combined with fluorescent molecules to create a sensor. However, binding proteins with the desired properties are often not available in nature and substantial improvement to sensors can be required, particularly with regard to their durability. Ancestral protein reconstruction is a powerful protein-engineering tool able to generate highly stable and functional proteins. In this work, we sought to establish the utility of ancestral protein reconstruction to biosensor development, beginning with the construction of an l-arginine biosensor. l-arginine, as the immediate precursor to nitric oxide, is an important molecule in many physiological contexts including brain function. Using a combination of ancestral reconstruction and circular permutation, we constructed a Förster resonance energy transfer (FRET) biosensor for l-arginine (cpFLIPR). cpFLIPR displays high sensitivity and specificity, with a Kd of ∼14 μM and a maximal dynamic range of 35%. Importantly, cpFLIPR was highly robust, enabling accurate l-arginine measurement at physiological temperatures. We established that cpFLIPR is compatible with two-photon excitation fluorescence microscopy and report l-arginine concentrations in brain tissue."}],"pmid":1,"oa_version":"Submitted Version","main_file_link":[{"open_access":"1","url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4570536/"}],"scopus_import":1,"intvolume":" 24","month":"09","date_updated":"2021-01-12T06:52:00Z","department":[{"_id":"HaJa"}],"_id":"1611","type":"journal_article","status":"public","year":"2015","publication":"Protein Science","day":"01","page":"1412 - 1422","date_created":"2018-12-11T11:53:01Z","date_published":"2015-09-01T00:00:00Z","doi":"10.1002/pro.2721","oa":1,"quality_controlled":"1","publisher":"Wiley","citation":{"ista":"Whitfield J, Zhang W, Herde M, Clifton B, Radziejewski J, Janovjak HL, Henneberger C, Jackson C. 2015. Construction of a robust and sensitive arginine biosensor through ancestral protein reconstruction. Protein Science. 24(9), 1412–1422.","chicago":"Whitfield, Jason, William Zhang, Michel Herde, Ben Clifton, Johanna Radziejewski, Harald L Janovjak, Christian Henneberger, and Colin Jackson. “Construction of a Robust and Sensitive Arginine Biosensor through Ancestral Protein Reconstruction.” Protein Science. Wiley, 2015. https://doi.org/10.1002/pro.2721.","ama":"Whitfield J, Zhang W, Herde M, et al. Construction of a robust and sensitive arginine biosensor through ancestral protein reconstruction. Protein Science. 2015;24(9):1412-1422. doi:10.1002/pro.2721","apa":"Whitfield, J., Zhang, W., Herde, M., Clifton, B., Radziejewski, J., Janovjak, H. L., … Jackson, C. (2015). Construction of a robust and sensitive arginine biosensor through ancestral protein reconstruction. Protein Science. Wiley. https://doi.org/10.1002/pro.2721","short":"J. Whitfield, W. Zhang, M. Herde, B. Clifton, J. Radziejewski, H.L. Janovjak, C. Henneberger, C. Jackson, Protein Science 24 (2015) 1412–1422.","ieee":"J. Whitfield et al., “Construction of a robust and sensitive arginine biosensor through ancestral protein reconstruction,” Protein Science, vol. 24, no. 9. Wiley, pp. 1412–1422, 2015.","mla":"Whitfield, Jason, et al. “Construction of a Robust and Sensitive Arginine Biosensor through Ancestral Protein Reconstruction.” Protein Science, vol. 24, no. 9, Wiley, 2015, pp. 1412–22, doi:10.1002/pro.2721."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"pmid":["26061224"]},"author":[{"first_name":"Jason","last_name":"Whitfield","full_name":"Whitfield, Jason"},{"full_name":"Zhang, William","last_name":"Zhang","first_name":"William"},{"full_name":"Herde, Michel","last_name":"Herde","first_name":"Michel"},{"first_name":"Ben","last_name":"Clifton","full_name":"Clifton, Ben"},{"last_name":"Radziejewski","full_name":"Radziejewski, Johanna","first_name":"Johanna"},{"orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L","last_name":"Janovjak","first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Henneberger, Christian","last_name":"Henneberger","first_name":"Christian"},{"first_name":"Colin","last_name":"Jackson","full_name":"Jackson, Colin"}],"publist_id":"5555","title":"Construction of a robust and sensitive arginine biosensor through ancestral protein reconstruction","project":[{"_id":"255BFFFA-B435-11E9-9278-68D0E5697425","name":"In situ real-time imaging of neurotransmitter signaling using designer optical sensors (HFSP Young Investigator)","grant_number":"RGY0084/2012"}]},{"publisher":"Wiley","quality_controlled":"1","page":"518 - 525","date_created":"2018-12-11T11:54:26Z","doi":"10.1002/elps.201400451","date_published":"2015-02-01T00:00:00Z","year":"2015","publication":"Electrophoresis","day":"01","project":[{"_id":"25548C20-B435-11E9-9278-68D0E5697425","call_identifier":"FP7","name":"Microbial Ion Channels for Synthetic Neurobiology","grant_number":"303564"},{"_id":"255BFFFA-B435-11E9-9278-68D0E5697425","name":"In situ real-time imaging of neurotransmitter signaling using designer optical sensors (HFSP Young Investigator)","grant_number":"RGY0084/2012"}],"author":[{"full_name":"Hühner, Jens","last_name":"Hühner","first_name":"Jens"},{"id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","first_name":"Álvaro","orcid":"0000-0002-5409-8571","full_name":"Inglés Prieto, Álvaro","last_name":"Inglés Prieto"},{"last_name":"Neusüß","full_name":"Neusüß, Christian","first_name":"Christian"},{"full_name":"Lämmerhofer, Michael","last_name":"Lämmerhofer","first_name":"Michael"},{"last_name":"Janovjak","full_name":"Janovjak, Harald L","orcid":"0000-0002-8023-9315","first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87"}],"publist_id":"5230","title":"Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence detection","citation":{"mla":"Hühner, Jens, et al. “Quantification of Riboflavin, Flavin Mononucleotide, and Flavin Adenine Dinucleotide in Mammalian Model Cells by CE with LED-Induced Fluorescence Detection.” Electrophoresis, vol. 36, no. 4, Wiley, 2015, pp. 518–25, doi:10.1002/elps.201400451.","apa":"Hühner, J., Inglés Prieto, Á., Neusüß, C., Lämmerhofer, M., & Janovjak, H. L. (2015). Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence detection. Electrophoresis. Wiley. https://doi.org/10.1002/elps.201400451","ama":"Hühner J, Inglés Prieto Á, Neusüß C, Lämmerhofer M, Janovjak HL. Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence detection. Electrophoresis. 2015;36(4):518-525. doi:10.1002/elps.201400451","ieee":"J. Hühner, Á. Inglés Prieto, C. Neusüß, M. Lämmerhofer, and H. L. Janovjak, “Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence detection,” Electrophoresis, vol. 36, no. 4. Wiley, pp. 518–525, 2015.","short":"J. Hühner, Á. Inglés Prieto, C. Neusüß, M. Lämmerhofer, H.L. Janovjak, Electrophoresis 36 (2015) 518–525.","chicago":"Hühner, Jens, Álvaro Inglés Prieto, Christian Neusüß, Michael Lämmerhofer, and Harald L Janovjak. “Quantification of Riboflavin, Flavin Mononucleotide, and Flavin Adenine Dinucleotide in Mammalian Model Cells by CE with LED-Induced Fluorescence Detection.” Electrophoresis. Wiley, 2015. https://doi.org/10.1002/elps.201400451.","ista":"Hühner J, Inglés Prieto Á, Neusüß C, Lämmerhofer M, Janovjak HL. 2015. Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence detection. Electrophoresis. 36(4), 518–525."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":1,"intvolume":" 36","month":"02","abstract":[{"text":"Cultured mammalian cells essential are model systems in basic biology research, production platforms of proteins for medical use, and testbeds in synthetic biology. Flavin cofactors, in particular flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), are critical for cellular redox reactions and sense light in naturally occurring photoreceptors and optogenetic tools. Here, we quantified flavin contents of commonly used mammalian cell lines. We first compared three procedures for extraction of free and noncovalently protein-bound flavins and verified extraction using fluorescence spectroscopy. For separation, two CE methods with different BGEs were established, and detection was performed by LED-induced fluorescence with limit of detections (LODs 0.5-3.8 nM). We found that riboflavin (RF), FMN, and FAD contents varied significantly between cell lines. RF (3.1-14 amol/cell) and FAD (2.2-17.0 amol/cell) were the predominant flavins, while FMN (0.46-3.4 amol/cell) was found at markedly lower levels. Observed flavin contents agree with those previously extracted from mammalian tissues, yet reduced forms of RF were detected that were not described previously. Quantification of flavins in mammalian cell lines will allow a better understanding of cellular redox reactions and optogenetic tools.","lang":"eng"}],"oa_version":"None","ec_funded":1,"issue":"4","volume":36,"publication_status":"published","language":[{"iso":"eng"}],"type":"journal_article","pubrep_id":"836","status":"public","_id":"1867","department":[{"_id":"HaJa"}],"date_updated":"2021-01-12T06:53:43Z"},{"project":[{"call_identifier":"FP7","_id":"25548C20-B435-11E9-9278-68D0E5697425","name":"Microbial Ion Channels for Synthetic Neurobiology","grant_number":"303564"},{"grant_number":"RGY0084/2012","name":"In situ real-time imaging of neurotransmitter signaling using designer optical sensors (HFSP Young Investigator)","_id":"255BFFFA-B435-11E9-9278-68D0E5697425"},{"name":"Molecular Drug Targets","grant_number":"W1232-B24","call_identifier":"FWF","_id":"255A6082-B435-11E9-9278-68D0E5697425"}],"title":"Light-assisted small-molecule screening against protein kinases","publist_id":"5471","author":[{"full_name":"Inglés Prieto, Álvaro","orcid":"0000-0002-5409-8571","last_name":"Inglés Prieto","first_name":"Álvaro","id":"2A9DB292-F248-11E8-B48F-1D18A9856A87"},{"orcid":"0000-0002-7218-7738","full_name":"Gschaider-Reichhart, Eva","last_name":"Gschaider-Reichhart","id":"3FEE232A-F248-11E8-B48F-1D18A9856A87","first_name":"Eva"},{"last_name":"Muellner","full_name":"Muellner, Markus","first_name":"Markus"},{"id":"30845DAA-F248-11E8-B48F-1D18A9856A87","first_name":"Matthias","last_name":"Nowak","full_name":"Nowak, Matthias"},{"first_name":"Sebastian","last_name":"Nijman","full_name":"Nijman, Sebastian"},{"full_name":"Grusch, Michael","last_name":"Grusch","first_name":"Michael"},{"first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Janovjak, Harald L","orcid":"0000-0002-8023-9315","last_name":"Janovjak"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"chicago":"Inglés Prieto, Álvaro, Eva Gschaider-Reichhart, Markus Muellner, Matthias Nowak, Sebastian Nijman, Michael Grusch, and Harald L Janovjak. “Light-Assisted Small-Molecule Screening against Protein Kinases.” Nature Chemical Biology. Nature Publishing Group, 2015. https://doi.org/10.1038/nchembio.1933.","ista":"Inglés Prieto Á, Gschaider-Reichhart E, Muellner M, Nowak M, Nijman S, Grusch M, Janovjak HL. 2015. Light-assisted small-molecule screening against protein kinases. Nature Chemical Biology. 11(12), 952–954.","mla":"Inglés Prieto, Álvaro, et al. “Light-Assisted Small-Molecule Screening against Protein Kinases.” Nature Chemical Biology, vol. 11, no. 12, Nature Publishing Group, 2015, pp. 952–54, doi:10.1038/nchembio.1933.","apa":"Inglés Prieto, Á., Gschaider-Reichhart, E., Muellner, M., Nowak, M., Nijman, S., Grusch, M., & Janovjak, H. L. (2015). Light-assisted small-molecule screening against protein kinases. Nature Chemical Biology. Nature Publishing Group. https://doi.org/10.1038/nchembio.1933","ama":"Inglés Prieto Á, Gschaider-Reichhart E, Muellner M, et al. Light-assisted small-molecule screening against protein kinases. Nature Chemical Biology. 2015;11(12):952-954. doi:10.1038/nchembio.1933","short":"Á. Inglés Prieto, E. Gschaider-Reichhart, M. Muellner, M. Nowak, S. Nijman, M. Grusch, H.L. Janovjak, Nature Chemical Biology 11 (2015) 952–954.","ieee":"Á. Inglés Prieto et al., “Light-assisted small-molecule screening against protein kinases,” Nature Chemical Biology, vol. 11, no. 12. Nature Publishing Group, pp. 952–954, 2015."},"oa":1,"quality_controlled":"1","publisher":"Nature Publishing Group","acknowledgement":"This work was supported by grants from the European Union Seventh Framework Programme (CIG-303564 to H.J. and ERC-StG-311166 to S.M.B.N.), the Human Frontier Science Program (RGY0084_2012 to H.J.) and the Herzfelder Foundation (to M.G.). A.I.-P. was supported by a Ramon Areces fellowship, and E.R. by the graduate program MolecularDrugTargets (Austrian Science Fund (FWF): W 1232) and a FemTech fellowship (3580812 Austrian Research Promotion Agency).","date_created":"2018-12-11T11:53:25Z","date_published":"2015-10-12T00:00:00Z","doi":"10.1038/nchembio.1933","page":"952 - 954","publication":"Nature Chemical Biology","day":"12","year":"2015","has_accepted_license":"1","pubrep_id":"837","status":"public","type":"journal_article","_id":"1678","file_date_updated":"2020-07-14T12:45:12Z","department":[{"_id":"HaJa"},{"_id":"LifeSc"}],"ddc":["571"],"date_updated":"2023-09-07T12:49:09Z","intvolume":" 11","month":"10","scopus_import":1,"oa_version":"Submitted Version","abstract":[{"text":"High-throughput live-cell screens are intricate elements of systems biology studies and drug discovery pipelines. Here, we demonstrate an optogenetics-assisted method that avoids the need for chemical activators and reporters, reduces the number of operational steps and increases information content in a cell-based small-molecule screen against human protein kinases, including an orphan receptor tyrosine kinase. This blueprint for all-optical screening can be adapted to many drug targets and cellular processes.","lang":"eng"}],"ec_funded":1,"issue":"12","related_material":{"record":[{"relation":"dissertation_contains","status":"public","id":"418"}]},"volume":11,"language":[{"iso":"eng"}],"file":[{"file_name":"IST-2017-837-v1+1_ingles-prieto.pdf","date_created":"2018-12-12T10:10:51Z","creator":"system","file_size":1308364,"date_updated":"2020-07-14T12:45:12Z","file_id":"4842","checksum":"e9fb251dfcb7cd209b83f17867e61321","relation":"main_file","access_level":"open_access","content_type":"application/pdf"}],"publication_status":"published"},{"_id":"1844","pubrep_id":"430","status":"public","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)"},"type":"journal_article","ddc":["571"],"date_updated":"2021-01-12T06:53:34Z","file_date_updated":"2020-07-14T12:45:19Z","department":[{"_id":"HaJa"}],"oa_version":"Published Version","abstract":[{"lang":"eng","text":"Local protein interactions ("molecular context" effects) dictate amino acid replacements and can be described in terms of site-specific, energetic preferences for any different amino acid. It has been recently debated whether these preferences remain approximately constant during evolution or whether, due to coevolution of sites, they change strongly. Such research highlights an unresolved and fundamental issue with far-reaching implications for phylogenetic analysis and molecular evolution modeling. Here, we take advantage of the recent availability of phenotypically supported laboratory resurrections of Precambrian thioredoxins and β-lactamases to experimentally address the change of site-specific amino acid preferences over long geological timescales. Extensive mutational analyses support the notion that evolutionary adjustment to a new amino acid may occur, but to a large extent this is insufficient to erase the primitive preference for amino acid replacements. Generally, site-specific amino acid preferences appear to remain conserved throughout evolutionary history despite local sequence divergence. We show such preference conservation to be readily understandable in molecular terms and we provide crystallographic evidence for an intriguing structural-switch mechanism: Energetic preference for an ancestral amino acid in a modern protein can be linked to reorganization upon mutation to the ancestral local structure around the mutated site. Finally, we point out that site-specific preference conservation naturally leads to one plausible evolutionary explanation for the existence of intragenic global suppressor mutations."}],"intvolume":" 32","month":"11","scopus_import":1,"language":[{"iso":"eng"}],"file":[{"access_level":"open_access","relation":"main_file","content_type":"application/pdf","file_id":"5247","checksum":"06215318e66be8f3e0c33abb07e9d3da","creator":"system","date_updated":"2020-07-14T12:45:19Z","file_size":1545246,"date_created":"2018-12-12T10:16:56Z","file_name":"IST-2016-430-v1+1_Mol_Biol_Evol-2015-Risso-440-55.pdf"}],"publication_status":"published","license":"https://creativecommons.org/licenses/by-nc/4.0/","volume":32,"issue":"2","user_id":"4435EBFC-F248-11E8-B48F-1D18A9856A87","citation":{"ista":"Risso V, Manssour Triedo F, Delgado Delgado A, Arco R, Barroso Deljesús A, Inglés Prieto Á, Godoy Ruiz R, Gavira J, Gaucher E, Ibarra Molero B, Sánchez Ruiz J. 2014. Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history. Molecular Biology and Evolution. 32(2), 440–455.","chicago":"Risso, Valeria, Fadia Manssour Triedo, Asuncion Delgado Delgado, Rocio Arco, Alicia Barroso Deljesús, Álvaro Inglés Prieto, Raquel Godoy Ruiz, et al. “Mutational Studies on Resurrected Ancestral Proteins Reveal Conservation of Site-Specific Amino Acid Preferences throughout Evolutionary History.” Molecular Biology and Evolution. Oxford University Press, 2014. https://doi.org/10.1093/molbev/msu312.","short":"V. Risso, F. Manssour Triedo, A. Delgado Delgado, R. Arco, A. Barroso Deljesús, Á. Inglés Prieto, R. Godoy Ruiz, J. Gavira, E. Gaucher, B. Ibarra Molero, J. Sánchez Ruiz, Molecular Biology and Evolution 32 (2014) 440–455.","ieee":"V. Risso et al., “Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history,” Molecular Biology and Evolution, vol. 32, no. 2. Oxford University Press, pp. 440–455, 2014.","apa":"Risso, V., Manssour Triedo, F., Delgado Delgado, A., Arco, R., Barroso Deljesús, A., Inglés Prieto, Á., … Sánchez Ruiz, J. (2014). Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history. Molecular Biology and Evolution. Oxford University Press. https://doi.org/10.1093/molbev/msu312","ama":"Risso V, Manssour Triedo F, Delgado Delgado A, et al. Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history. Molecular Biology and Evolution. 2014;32(2):440-455. doi:10.1093/molbev/msu312","mla":"Risso, Valeria, et al. “Mutational Studies on Resurrected Ancestral Proteins Reveal Conservation of Site-Specific Amino Acid Preferences throughout Evolutionary History.” Molecular Biology and Evolution, vol. 32, no. 2, Oxford University Press, 2014, pp. 440–55, doi:10.1093/molbev/msu312."},"title":"Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history","author":[{"last_name":"Risso","full_name":"Risso, Valeria","first_name":"Valeria"},{"first_name":"Fadia","last_name":"Manssour Triedo","full_name":"Manssour Triedo, Fadia"},{"last_name":"Delgado Delgado","full_name":"Delgado Delgado, Asuncion","first_name":"Asuncion"},{"last_name":"Arco","full_name":"Arco, Rocio","first_name":"Rocio"},{"last_name":"Barroso Deljesús","full_name":"Barroso Deljesús, Alicia","first_name":"Alicia"},{"id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","first_name":"Álvaro","orcid":"0000-0002-5409-8571","full_name":"Inglés Prieto, Álvaro","last_name":"Inglés Prieto"},{"first_name":"Raquel","last_name":"Godoy Ruiz","full_name":"Godoy Ruiz, Raquel"},{"last_name":"Gavira","full_name":"Gavira, Josè","first_name":"Josè"},{"full_name":"Gaucher, Eric","last_name":"Gaucher","first_name":"Eric"},{"first_name":"Beatriz","last_name":"Ibarra Molero","full_name":"Ibarra Molero, Beatriz"},{"full_name":"Sánchez Ruiz, Jose","last_name":"Sánchez Ruiz","first_name":"Jose"}],"publist_id":"5257","oa":1,"publisher":"Oxford University Press","quality_controlled":"1","publication":"Molecular Biology and Evolution","day":"12","year":"2014","has_accepted_license":"1","date_created":"2018-12-11T11:54:19Z","date_published":"2014-11-12T00:00:00Z","doi":"10.1093/molbev/msu312","page":"440 - 455"},{"citation":{"mla":"Inglés Prieto, Álvaro, et al. “The Optogenetic Promise for Oncology: Episode I.” Molecular and Cellular Oncology, vol. 1, no. 4, e964045, Taylor & Francis, 2014, doi:10.4161/23723548.2014.964045.","ama":"Inglés Prieto Á, Gschaider-Reichhart E, Schelch K, Janovjak HL, Grusch M. The optogenetic promise for oncology: Episode I. Molecular and Cellular Oncology. 2014;1(4). doi:10.4161/23723548.2014.964045","apa":"Inglés Prieto, Á., Gschaider-Reichhart, E., Schelch, K., Janovjak, H. L., & Grusch, M. (2014). The optogenetic promise for oncology: Episode I. Molecular and Cellular Oncology. Taylor & Francis. https://doi.org/10.4161/23723548.2014.964045","ieee":"Á. Inglés Prieto, E. Gschaider-Reichhart, K. Schelch, H. L. Janovjak, and M. Grusch, “The optogenetic promise for oncology: Episode I,” Molecular and Cellular Oncology, vol. 1, no. 4. Taylor & Francis, 2014.","short":"Á. Inglés Prieto, E. Gschaider-Reichhart, K. Schelch, H.L. Janovjak, M. Grusch, Molecular and Cellular Oncology 1 (2014).","chicago":"Inglés Prieto, Álvaro, Eva Gschaider-Reichhart, Karin Schelch, Harald L Janovjak, and Michael Grusch. “The Optogenetic Promise for Oncology: Episode I.” Molecular and Cellular Oncology. Taylor & Francis, 2014. https://doi.org/10.4161/23723548.2014.964045.","ista":"Inglés Prieto Á, Gschaider-Reichhart E, Schelch K, Janovjak HL, Grusch M. 2014. The optogenetic promise for oncology: Episode I. Molecular and Cellular Oncology. 1(4), e964045."},"user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","author":[{"last_name":"Inglés Prieto","full_name":"Inglés Prieto, Álvaro","orcid":"0000-0002-5409-8571","id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","first_name":"Álvaro"},{"last_name":"Gschaider-Reichhart","full_name":"Gschaider-Reichhart, Eva","orcid":"0000-0002-7218-7738","first_name":"Eva","id":"3FEE232A-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Schelch","full_name":"Schelch, Karin","first_name":"Karin"},{"id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","first_name":"Harald L","last_name":"Janovjak","orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L"},{"full_name":"Grusch, Michael","last_name":"Grusch","first_name":"Michael"}],"publist_id":"5040","title":"The optogenetic promise for oncology: Episode I","article_number":"e964045","has_accepted_license":"1","year":"2014","day":"31","publication":"Molecular and Cellular Oncology","date_published":"2014-12-31T00:00:00Z","doi":"10.4161/23723548.2014.964045","date_created":"2018-12-11T11:55:19Z","quality_controlled":"1","publisher":"Taylor & Francis","oa":1,"date_updated":"2021-01-12T06:54:51Z","ddc":["570"],"file_date_updated":"2020-07-14T12:45:26Z","department":[{"_id":"HaJa"}],"_id":"2032","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)"},"status":"public","publication_status":"published","file":[{"file_id":"6464","checksum":"44e17ad40577ab46eb602e88a8b0b8fd","content_type":"application/pdf","access_level":"open_access","relation":"main_file","date_created":"2019-05-16T13:39:11Z","file_name":"2014_Taylor_Alvaro.pdf","date_updated":"2020-07-14T12:45:26Z","file_size":1765933,"creator":"kschuh"}],"language":[{"iso":"eng"}],"volume":1,"issue":"4","abstract":[{"text":"As light-based control of fundamental signaling pathways is becoming a reality, the field of optogenetics is rapidly moving beyond neuroscience. We have recently developed receptor tyrosine kinases that are activated by light and control cell proliferation, epithelial–mesenchymal transition, and angiogenic sprouting—cell behaviors central to cancer progression.","lang":"eng"}],"oa_version":"Published Version","scopus_import":1,"month":"12","intvolume":" 1"},{"department":[{"_id":"HaJa"}],"date_updated":"2023-09-07T12:49:09Z","status":"public","type":"journal_article","_id":"2084","related_material":{"record":[{"relation":"dissertation_contains","status":"public","id":"418"}]},"volume":33,"issue":"15","language":[{"iso":"eng"}],"publication_status":"published","intvolume":" 33","month":"07","main_file_link":[{"url":"http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4194103/","open_access":"1"}],"scopus_import":1,"oa_version":"Submitted Version","abstract":[{"text":"Receptor tyrosine kinases (RTKs) are a large family of cell surface receptors that sense growth factors and hormones and regulate a variety of cell behaviours in health and disease. Contactless activation of RTKs with spatial and temporal precision is currently not feasible. Here, we generated RTKs that are insensitive to endogenous ligands but can be selectively activated by low-intensity blue light. We screened light-oxygen-voltage (LOV)-sensing domains for their ability to activate RTKs by light-activated dimerization. Incorporation of LOV domains found in aureochrome photoreceptors of stramenopiles resulted in robust activation of the fibroblast growth factor receptor 1 (FGFR1), epidermal growth factor receptor (EGFR) and rearranged during transfection (RET). In human cancer and endothelial cells, light induced cellular signalling with spatial and temporal precision. Furthermore, light faithfully mimicked complex mitogenic and morphogenic cell behaviour induced by growth factors. RTKs under optical control (Opto-RTKs) provide a powerful optogenetic approach to actuate cellular signals and manipulate cell behaviour.","lang":"eng"}],"title":"Spatio-temporally precise activation of engineered receptor tyrosine kinases by light","publist_id":"4953","author":[{"first_name":"Michael","full_name":"Grusch, Michael","last_name":"Grusch"},{"first_name":"Karin","full_name":"Schelch, Karin","last_name":"Schelch"},{"first_name":"Robert","last_name":"Riedler","full_name":"Riedler, Robert"},{"orcid":"0000-0002-7218-7738","full_name":"Gschaider-Reichhart, Eva","last_name":"Gschaider-Reichhart","id":"3FEE232A-F248-11E8-B48F-1D18A9856A87","first_name":"Eva"},{"first_name":"Christopher","last_name":"Differ","full_name":"Differ, Christopher"},{"last_name":"Berger","full_name":"Berger, Walter","first_name":"Walter"},{"id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","first_name":"Álvaro","last_name":"Inglés Prieto","full_name":"Inglés Prieto, Álvaro","orcid":"0000-0002-5409-8571"},{"full_name":"Janovjak, Harald L","orcid":"0000-0002-8023-9315","last_name":"Janovjak","first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87"}],"user_id":"4435EBFC-F248-11E8-B48F-1D18A9856A87","citation":{"mla":"Grusch, Michael, et al. “Spatio-Temporally Precise Activation of Engineered Receptor Tyrosine Kinases by Light.” EMBO Journal, vol. 33, no. 15, Wiley-Blackwell, 2014, pp. 1713–26, doi:10.15252/embj.201387695.","ieee":"M. Grusch et al., “Spatio-temporally precise activation of engineered receptor tyrosine kinases by light,” EMBO Journal, vol. 33, no. 15. Wiley-Blackwell, pp. 1713–1726, 2014.","short":"M. Grusch, K. Schelch, R. Riedler, E. Gschaider-Reichhart, C. Differ, W. Berger, Á. Inglés Prieto, H.L. Janovjak, EMBO Journal 33 (2014) 1713–1726.","ama":"Grusch M, Schelch K, Riedler R, et al. Spatio-temporally precise activation of engineered receptor tyrosine kinases by light. EMBO Journal. 2014;33(15):1713-1726. doi:10.15252/embj.201387695","apa":"Grusch, M., Schelch, K., Riedler, R., Gschaider-Reichhart, E., Differ, C., Berger, W., … Janovjak, H. L. (2014). Spatio-temporally precise activation of engineered receptor tyrosine kinases by light. EMBO Journal. Wiley-Blackwell. https://doi.org/10.15252/embj.201387695","chicago":"Grusch, Michael, Karin Schelch, Robert Riedler, Eva Gschaider-Reichhart, Christopher Differ, Walter Berger, Álvaro Inglés Prieto, and Harald L Janovjak. “Spatio-Temporally Precise Activation of Engineered Receptor Tyrosine Kinases by Light.” EMBO Journal. Wiley-Blackwell, 2014. https://doi.org/10.15252/embj.201387695.","ista":"Grusch M, Schelch K, Riedler R, Gschaider-Reichhart E, Differ C, Berger W, Inglés Prieto Á, Janovjak HL. 2014. Spatio-temporally precise activation of engineered receptor tyrosine kinases by light. EMBO Journal. 33(15), 1713–1726."},"date_created":"2018-12-11T11:55:37Z","date_published":"2014-07-01T00:00:00Z","doi":"10.15252/embj.201387695","page":"1713 - 1726","publication":"EMBO Journal","day":"01","year":"2014","oa":1,"quality_controlled":"1","publisher":"Wiley-Blackwell","acknowledgement":"European Union Seventh Framework Programme; Human Frontier Science Program; Oesterreichische Nationalbank Anniversary Fund 14211; Austrian Research Promotion Agency; FemTech"},{"article_number":"e70013","citation":{"chicago":"Sanchez-Romero, Inmaculada, Antonio Ariza, Keith Wilson, Michael Skjøt, Jesper Vind, Leonardo De Maria, Lars Skov, and Jose Sánchez Ruiz. “Mechanism of Protein Kinetic Stabilization by Engineered Disulfide Crosslinks.” PLoS One. Public Library of Science, 2013. https://doi.org/10.1371/journal.pone.0070013.","ista":"Sanchez-Romero I, Ariza A, Wilson K, Skjøt M, Vind J, De Maria L, Skov L, Sánchez Ruiz J. 2013. Mechanism of protein kinetic stabilization by engineered disulfide crosslinks. PLoS One. 8(7), e70013.","mla":"Sanchez-Romero, Inmaculada, et al. “Mechanism of Protein Kinetic Stabilization by Engineered Disulfide Crosslinks.” PLoS One, vol. 8, no. 7, e70013, Public Library of Science, 2013, doi:10.1371/journal.pone.0070013.","ama":"Sanchez-Romero I, Ariza A, Wilson K, et al. Mechanism of protein kinetic stabilization by engineered disulfide crosslinks. PLoS One. 2013;8(7). doi:10.1371/journal.pone.0070013","apa":"Sanchez-Romero, I., Ariza, A., Wilson, K., Skjøt, M., Vind, J., De Maria, L., … Sánchez Ruiz, J. (2013). Mechanism of protein kinetic stabilization by engineered disulfide crosslinks. PLoS One. Public Library of Science. https://doi.org/10.1371/journal.pone.0070013","ieee":"I. Sanchez-Romero et al., “Mechanism of protein kinetic stabilization by engineered disulfide crosslinks,” PLoS One, vol. 8, no. 7. Public Library of Science, 2013.","short":"I. Sanchez-Romero, A. Ariza, K. Wilson, M. Skjøt, J. Vind, L. De Maria, L. Skov, J. Sánchez Ruiz, PLoS One 8 (2013)."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publist_id":"4430","author":[{"full_name":"Sanchez Romero, Inmaculada","last_name":"Sanchez Romero","id":"3D9C5D30-F248-11E8-B48F-1D18A9856A87","first_name":"Inmaculada"},{"first_name":"Antonio","last_name":"Ariza","full_name":"Ariza, Antonio"},{"first_name":"Keith","last_name":"Wilson","full_name":"Wilson, Keith"},{"full_name":"Skjøt, Michael","last_name":"Skjøt","first_name":"Michael"},{"first_name":"Jesper","last_name":"Vind","full_name":"Vind, Jesper"},{"last_name":"De Maria","full_name":"De Maria, Leonardo","first_name":"Leonardo"},{"full_name":"Skov, Lars","last_name":"Skov","first_name":"Lars"},{"first_name":"Jose","full_name":"Sánchez Ruiz, Jose","last_name":"Sánchez Ruiz"}],"title":"Mechanism of protein kinetic stabilization by engineered disulfide crosslinks","oa":1,"quality_controlled":"1","publisher":"Public Library of Science","year":"2013","has_accepted_license":"1","publication":"PLoS One","day":"30","date_created":"2018-12-11T11:57:51Z","doi":"10.1371/journal.pone.0070013","date_published":"2013-07-30T00:00:00Z","_id":"2471","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"type":"journal_article","pubrep_id":"414","status":"public","date_updated":"2021-01-12T06:57:41Z","ddc":["570"],"file_date_updated":"2020-07-14T12:45:41Z","department":[{"_id":"HaJa"}],"abstract":[{"lang":"eng","text":"The impact of disulfide bonds on protein stability goes beyond simple equilibrium thermodynamics effects associated with the conformational entropy of the unfolded state. Indeed, disulfide crosslinks may play a role in the prevention of dysfunctional association and strongly affect the rates of irreversible enzyme inactivation, highly relevant in biotechnological applications. While these kinetic-stability effects remain poorly understood, by analogy with proposed mechanisms for processes of protein aggregation and fibrillogenesis, we propose that they may be determined by the properties of sparsely-populated, partially-unfolded intermediates. Here we report the successful design, on the basis of high temperature molecular-dynamics simulations, of six thermodynamically and kinetically stabilized variants of phytase from Citrobacter braakii (a biotechnologically important enzyme) with one, two or three engineered disulfides. Activity measurements and 3D crystal structure determination demonstrate that the engineered crosslinks do not cause dramatic alterations in the native structure. The inactivation kinetics for all the variants displays a strongly non-Arrhenius temperature dependence, with the time-scale for the irreversible denaturation process reaching a minimum at a given temperature within the range of the denaturation transition. We show this striking feature to be a signature of a key role played by a partially unfolded, intermediate state/ensemble. Energetic and mutational analyses confirm that the intermediate is highly unfolded (akin to a proposed critical intermediate in the misfolding of the prion protein), a result that explains the observed kinetic stabilization. Our results provide a rationale for the kinetic-stability consequences of disulfide-crosslink engineering and an experimental methodology to arrive at energetic/structural descriptions of the sparsely populated and elusive intermediates that play key roles in irreversible protein denaturation."}],"oa_version":"Published Version","scopus_import":1,"intvolume":" 8","month":"07","publication_status":"published","language":[{"iso":"eng"}],"file":[{"content_type":"application/pdf","access_level":"open_access","relation":"main_file","file_id":"5124","checksum":"c0c96cc76ed7ef0d036a31a7e33c9a37","date_updated":"2020-07-14T12:45:41Z","file_size":1323666,"creator":"system","date_created":"2018-12-12T10:15:07Z","file_name":"IST-2016-414-v1+1_journal.pone.0070013.pdf"}],"volume":8,"issue":"7"},{"quality_controlled":"1","publisher":"Springer","oa":1,"page":"417 - 435","date_published":"2013-02-22T00:00:00Z","doi":"10.1007/978-1-62703-351-0_32","date_created":"2018-12-11T11:59:57Z","has_accepted_license":"1","year":"2013","day":"22","publication":"Methods in Molecular Biology","project":[{"name":"In situ real-time imaging of neurotransmitter signaling using designer optical sensors (HFSP Young Investigator)","grant_number":"RGY0084/2012","_id":"255BFFFA-B435-11E9-9278-68D0E5697425"},{"call_identifier":"FP7","_id":"25548C20-B435-11E9-9278-68D0E5697425","grant_number":"303564","name":"Microbial Ion Channels for Synthetic Neurobiology"}],"publist_id":"3932","author":[{"full_name":"Szobota, Stephanie","last_name":"Szobota","first_name":"Stephanie"},{"last_name":"Mckenzie","full_name":"Mckenzie, Catherine","id":"3EEDE19A-F248-11E8-B48F-1D18A9856A87","first_name":"Catherine"},{"first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","last_name":"Janovjak","full_name":"Janovjak, Harald L","orcid":"0000-0002-8023-9315"}],"title":"Optical control of ligand-gated ion channels","citation":{"ama":"Szobota S, Mckenzie C, Janovjak HL. Optical control of ligand-gated ion channels. Methods in Molecular Biology. 2013;998:417-435. doi:10.1007/978-1-62703-351-0_32","apa":"Szobota, S., Mckenzie, C., & Janovjak, H. L. (2013). Optical control of ligand-gated ion channels. Methods in Molecular Biology. Springer. https://doi.org/10.1007/978-1-62703-351-0_32","ieee":"S. Szobota, C. Mckenzie, and H. L. Janovjak, “Optical control of ligand-gated ion channels,” Methods in Molecular Biology, vol. 998. Springer, pp. 417–435, 2013.","short":"S. Szobota, C. Mckenzie, H.L. Janovjak, Methods in Molecular Biology 998 (2013) 417–435.","mla":"Szobota, Stephanie, et al. “Optical Control of Ligand-Gated Ion Channels.” Methods in Molecular Biology, vol. 998, Springer, 2013, pp. 417–35, doi:10.1007/978-1-62703-351-0_32.","ista":"Szobota S, Mckenzie C, Janovjak HL. 2013. Optical control of ligand-gated ion channels. Methods in Molecular Biology. 998, 417–435.","chicago":"Szobota, Stephanie, Catherine Mckenzie, and Harald L Janovjak. “Optical Control of Ligand-Gated Ion Channels.” Methods in Molecular Biology. Springer, 2013. https://doi.org/10.1007/978-1-62703-351-0_32."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","alternative_title":["MIMB"],"scopus_import":1,"month":"02","intvolume":" 998","abstract":[{"text":"In the vibrant field of optogenetics, optics and genetic targeting are combined to commandeer cellular functions, such as the neuronal action potential, by optically stimulating light-sensitive ion channels expressed in the cell membrane. One broadly applicable manifestation of this approach are covalently attached photochromic tethered ligands (PTLs) that allow activating ligand-gated ion channels with outstanding spatial and temporal resolution. Here, we describe all steps towards the successful development and application of PTL-gated ion channels in cell lines and primary cells. The basis for these experiments forms a combination of molecular modeling, genetic engineering, cell culture, and electrophysiology. The light-gated glutamate receptor (LiGluR), which consists of the PTL-functionalized GluK2 receptor, serves as a model.","lang":"eng"}],"oa_version":"Submitted Version","volume":998,"ec_funded":1,"publication_status":"published","file":[{"file_id":"4952","checksum":"1701f0d989f27ddac471b19a894ec0d1","content_type":"application/pdf","relation":"main_file","access_level":"open_access","file_name":"IST-2017-834-v1+1_szobota.pdf","date_created":"2018-12-12T10:12:34Z","file_size":336734,"date_updated":"2020-07-14T12:45:51Z","creator":"system"}],"language":[{"iso":"eng"}],"type":"journal_article","status":"public","pubrep_id":"834","_id":"2857","department":[{"_id":"HaJa"}],"file_date_updated":"2020-07-14T12:45:51Z","date_updated":"2021-01-12T07:00:17Z","ddc":["570"]},{"pmid":1,"oa_version":"Submitted Version","abstract":[{"lang":"eng","text":"G protein–coupled receptors (GPCRs), the largest family of membrane signaling proteins, respond to neurotransmitters, hormones and small environmental molecules. The neuronal function of many GPCRs has been difficult to resolve because of an inability to gate them with subtype specificity, spatial precision, speed and reversibility. To address this, we developed an approach for opto-chemical engineering of native GPCRs. We applied this to the metabotropic glutamate receptors (mGluRs) to generate light-agonized and light-antagonized mGluRs (LimGluRs). The light-agonized LimGluR2, on which we focused, was fast, bistable and supported multiple rounds of on/off switching. Light gated two of the primary neuronal functions of mGluR2: suppression of excitability and inhibition of neurotransmitter release. We found that the light-antagonized tool LimGluR2-block was able to manipulate negative feedback of synaptically released glutamate on transmitter release. We generalized the optical control to two additional family members: mGluR3 and mGluR6. This system worked in rodent brain slices and in zebrafish in vivo, where we found that mGluR2 modulated the threshold for escape behavior. These light-gated mGluRs pave the way for determining the roles of mGluRs in synaptic plasticity, memory and disease."}],"month":"03","intvolume":" 16","scopus_import":1,"main_file_link":[{"open_access":"1","url":"http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3681425/"}],"language":[{"iso":"eng"}],"publication_status":"published","volume":16,"_id":"2856","status":"public","type":"journal_article","date_updated":"2021-01-12T07:00:16Z","department":[{"_id":"HaJa"}],"acknowledgement":"National Science Foundation grants CHE-0233882 and CHE-0840505 (to the College of Chemistry at the University of California, Berkeley), a postdoctoral fellowship of the European Molecular Biology Organization (H.J.)","publisher":"Nature Publishing Group","quality_controlled":"1","oa":1,"day":"03","publication":"Nature Neuroscience","year":"2013","date_published":"2013-03-03T00:00:00Z","doi":"10.1038/nn.3346","date_created":"2018-12-11T11:59:57Z","page":"507 - 516","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"mla":"Levitz, Joshua, et al. “Optical Control of Metabotropic Glutamate Receptors.” Nature Neuroscience, vol. 16, Nature Publishing Group, 2013, pp. 507–16, doi:10.1038/nn.3346.","short":"J. Levitz, C. Pantoja, B. Gaub, H.L. Janovjak, A. Reiner, A. Hoagland, D. Schoppik, B. Kane, P. Stawski, A. Schier, D. Trauner, E. Isacoff, Nature Neuroscience 16 (2013) 507–516.","ieee":"J. Levitz et al., “Optical control of metabotropic glutamate receptors,” Nature Neuroscience, vol. 16. Nature Publishing Group, pp. 507–516, 2013.","apa":"Levitz, J., Pantoja, C., Gaub, B., Janovjak, H. L., Reiner, A., Hoagland, A., … Isacoff, E. (2013). Optical control of metabotropic glutamate receptors. Nature Neuroscience. Nature Publishing Group. https://doi.org/10.1038/nn.3346","ama":"Levitz J, Pantoja C, Gaub B, et al. Optical control of metabotropic glutamate receptors. Nature Neuroscience. 2013;16:507-516. doi:10.1038/nn.3346","chicago":"Levitz, Joshua, Carlos Pantoja, Benjamin Gaub, Harald L Janovjak, Andreas Reiner, Adam Hoagland, David Schoppik, et al. “Optical Control of Metabotropic Glutamate Receptors.” Nature Neuroscience. Nature Publishing Group, 2013. https://doi.org/10.1038/nn.3346.","ista":"Levitz J, Pantoja C, Gaub B, Janovjak HL, Reiner A, Hoagland A, Schoppik D, Kane B, Stawski P, Schier A, Trauner D, Isacoff E. 2013. Optical control of metabotropic glutamate receptors. Nature Neuroscience. 16, 507–516."},"title":"Optical control of metabotropic glutamate receptors","publist_id":"3936","author":[{"last_name":"Levitz","full_name":"Levitz, Joshua","first_name":"Joshua"},{"full_name":"Pantoja, Carlos","last_name":"Pantoja","first_name":"Carlos"},{"first_name":"Benjamin","full_name":"Gaub, Benjamin","last_name":"Gaub"},{"orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L","last_name":"Janovjak","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","first_name":"Harald L"},{"last_name":"Reiner","full_name":"Reiner, Andreas","first_name":"Andreas"},{"first_name":"Adam","last_name":"Hoagland","full_name":"Hoagland, Adam"},{"full_name":"Schoppik, David","last_name":"Schoppik","first_name":"David"},{"first_name":"Brian","last_name":"Kane","full_name":"Kane, Brian"},{"first_name":"Philipp","full_name":"Stawski, Philipp","last_name":"Stawski"},{"first_name":"Alexander","last_name":"Schier","full_name":"Schier, Alexander"},{"full_name":"Trauner, Dirk","last_name":"Trauner","first_name":"Dirk"},{"full_name":"Isacoff, Ehud","last_name":"Isacoff","first_name":"Ehud"}],"external_id":{"pmid":["23455609"]}},{"type":"journal_article","status":"public","_id":"505","author":[{"first_name":"Katrin","last_name":"Greimel","full_name":"Greimel, Katrin"},{"full_name":"Perz, Veronika","last_name":"Perz","first_name":"Veronika"},{"id":"382FBD6A-F248-11E8-B48F-1D18A9856A87","first_name":"Klaus","full_name":"Koren, Klaus","last_name":"Koren"},{"last_name":"Feola","full_name":"Feola, Roland","first_name":"Roland"},{"first_name":"Armin","full_name":"Temel, Armin","last_name":"Temel"},{"full_name":"Sohar, Christian","last_name":"Sohar","first_name":"Christian"},{"last_name":"Herrero Acero","full_name":"Herrero Acero, Enrique","first_name":"Enrique"},{"first_name":"Ingo","last_name":"Klimant","full_name":"Klimant, Ingo"},{"first_name":"Georg","full_name":"Guebitz, Georg","last_name":"Guebitz"}],"publist_id":"7313","title":"Banning toxic heavy-metal catalysts from paints: Enzymatic cross-linking of alkyd resins","department":[{"_id":"HaJa"}],"citation":{"ista":"Greimel K, Perz V, Koren K, Feola R, Temel A, Sohar C, Herrero Acero E, Klimant I, Guebitz G. 2013. Banning toxic heavy-metal catalysts from paints: Enzymatic cross-linking of alkyd resins. Green Chemistry. 15(2), 381–388.","chicago":"Greimel, Katrin, Veronika Perz, Klaus Koren, Roland Feola, Armin Temel, Christian Sohar, Enrique Herrero Acero, Ingo Klimant, and Georg Guebitz. “Banning Toxic Heavy-Metal Catalysts from Paints: Enzymatic Cross-Linking of Alkyd Resins.” Green Chemistry. Royal Society of Chemistry, 2013. https://doi.org/10.1039/c2gc36666e.","ama":"Greimel K, Perz V, Koren K, et al. Banning toxic heavy-metal catalysts from paints: Enzymatic cross-linking of alkyd resins. Green Chemistry. 2013;15(2):381-388. doi:10.1039/c2gc36666e","apa":"Greimel, K., Perz, V., Koren, K., Feola, R., Temel, A., Sohar, C., … Guebitz, G. (2013). Banning toxic heavy-metal catalysts from paints: Enzymatic cross-linking of alkyd resins. Green Chemistry. Royal Society of Chemistry. https://doi.org/10.1039/c2gc36666e","ieee":"K. Greimel et al., “Banning toxic heavy-metal catalysts from paints: Enzymatic cross-linking of alkyd resins,” Green Chemistry, vol. 15, no. 2. Royal Society of Chemistry, pp. 381–388, 2013.","short":"K. Greimel, V. Perz, K. Koren, R. Feola, A. Temel, C. Sohar, E. Herrero Acero, I. Klimant, G. Guebitz, Green Chemistry 15 (2013) 381–388.","mla":"Greimel, Katrin, et al. “Banning Toxic Heavy-Metal Catalysts from Paints: Enzymatic Cross-Linking of Alkyd Resins.” Green Chemistry, vol. 15, no. 2, Royal Society of Chemistry, 2013, pp. 381–88, doi:10.1039/c2gc36666e."},"date_updated":"2021-01-12T08:01:11Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Royal Society of Chemistry","scopus_import":1,"quality_controlled":"1","month":"02","intvolume":" 15","abstract":[{"lang":"eng","text":"Alkyd resins are polyesters containing unsaturated fatty acids that are used as binding agents in paints and coatings. Chemical drying of these polyesters is based on heavy metal catalyzed cross-linking of the unsaturated fatty acid moieties. Among the heavy-metal catalysts, cobalt complexes are the most effective, yet they have been proven to be carcinogenic. Therefore, strategies to replace the cobalt-based catalyst by environmentally friendlier and less toxic alternatives are under development. Here, we demonstrate for the first time that a laccase-mediator system can effectively replace the heavy-metal catalyst and cross-link alkyd resins. Interestingly, the biocatalytic reaction does not only work in aqueous media, but also in a solid film, where enzyme diffusion is limited. Within the catalytic cycle, the mediator oxidizes the alkyd resin and is regenerated by the laccase, which is uniformly distributed within the drying film as evidenced by confocal laser scanning microscopy. During gradual build-up of molecular weight, there is a concomitant decrease of the oxygen content in the film. A new optical sensor to follow oxygen consumption during the cross-linking reaction was developed and validated with state of the art techniques. A remarkable feature is the low sample amount required, which allows faster screening of new catalysts."}],"oa_version":"None","acknowledgement":"This study was performed within the Austrian Centre of Indus-\r\ntrial Biotechnology ACIB and the COST Action 868. This work\r\nhas been supported by the Federal Ministry of Economy,\r\nFamily and Youth (BMWFJ), the Federal Ministry of Tra\r\nffi\r\nc,\r\nInnovation and Technology (bmvit), the Styrian Business\r\nPromotion Agency SFG, the Standortagentur Tirol and ZIT\r\n–\r\nTechnology Agency of the City of Vienna through the\r\nCOMET-Funding Program managed by the Austrian Research\r\nPromotion Agency FFG. Dr Massimiliano Cardinale (Institute of\r\nEnvironmental Biotechnology, TU Graz) is gratefully acknowl-\r\nedged for technical support with the CLSM measurements.","page":"381 - 388","date_published":"2013-02-01T00:00:00Z","issue":"2","volume":15,"doi":"10.1039/c2gc36666e","date_created":"2018-12-11T11:46:51Z","publication_status":"published","year":"2013","day":"01","publication":"Green Chemistry","language":[{"iso":"eng"}]}]