[{"year":"2019","isi":1,"external_id":{"isi":["000456220900013"],"pmid":["30496761"]},"ec_funded":1,"pmid":1,"date_published":"2019-01-15T00:00:00Z","status":"public","publication":"Journal of Neuroscience Methods","project":[{"_id":"25548C20-B435-11E9-9278-68D0E5697425","name":"Microbial Ion Channels for Synthetic Neurobiology","grant_number":"303564","call_identifier":"FP7"},{"grant_number":"I03630","name":"Molecular mechanisms of endocytic cargo recognition in plants","call_identifier":"FWF","_id":"26538374-B435-11E9-9278-68D0E5697425"},{"_id":"2548AE96-B435-11E9-9278-68D0E5697425","name":"Molecular Drug Targets","grant_number":"W1232-B24","call_identifier":"FWF"}],"_id":"7406","date_updated":"2023-09-06T15:27:29Z","type":"journal_article","article_processing_charge":"No","doi":"10.1016/j.jneumeth.2018.11.018","publisher":"Elsevier","quality_controlled":"1","page":"114-121","department":[{"_id":"HaJa"},{"_id":"Bio"}],"month":"01","citation":{"ama":"Mckenzie C, Spanova M, Johnson AJ, et al. Isolation of synaptic vesicles from genetically engineered cultured neurons. <i>Journal of Neuroscience Methods</i>. 2019;312:114-121. doi:<a href=\"https://doi.org/10.1016/j.jneumeth.2018.11.018\">10.1016/j.jneumeth.2018.11.018</a>","short":"C. Mckenzie, M. Spanova, A.J. Johnson, S. Kainrath, V. Zheden, H.H. Sitte, H.L. Janovjak, Journal of Neuroscience Methods 312 (2019) 114–121.","ieee":"C. Mckenzie <i>et al.</i>, “Isolation of synaptic vesicles from genetically engineered cultured neurons,” <i>Journal of Neuroscience Methods</i>, vol. 312. Elsevier, pp. 114–121, 2019.","ista":"Mckenzie C, Spanova M, Johnson AJ, Kainrath S, Zheden V, Sitte HH, Janovjak HL. 2019. Isolation of synaptic vesicles from genetically engineered cultured neurons. Journal of Neuroscience Methods. 312, 114–121.","chicago":"Mckenzie, Catherine, Miroslava Spanova, Alexander J Johnson, Stephanie Kainrath, Vanessa Zheden, Harald H. Sitte, and Harald L Janovjak. “Isolation of Synaptic Vesicles from Genetically Engineered Cultured Neurons.” <i>Journal of Neuroscience Methods</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.jneumeth.2018.11.018\">https://doi.org/10.1016/j.jneumeth.2018.11.018</a>.","mla":"Mckenzie, Catherine, et al. “Isolation of Synaptic Vesicles from Genetically Engineered Cultured Neurons.” <i>Journal of Neuroscience Methods</i>, vol. 312, Elsevier, 2019, pp. 114–21, doi:<a href=\"https://doi.org/10.1016/j.jneumeth.2018.11.018\">10.1016/j.jneumeth.2018.11.018</a>.","apa":"Mckenzie, C., Spanova, M., Johnson, A. J., Kainrath, S., Zheden, V., Sitte, H. H., &#38; Janovjak, H. L. (2019). Isolation of synaptic vesicles from genetically engineered cultured neurons. <i>Journal of Neuroscience Methods</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jneumeth.2018.11.018\">https://doi.org/10.1016/j.jneumeth.2018.11.018</a>"},"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","language":[{"iso":"eng"}],"volume":312,"date_created":"2020-01-30T09:12:19Z","article_type":"original","scopus_import":"1","day":"15","author":[{"first_name":"Catherine","id":"3EEDE19A-F248-11E8-B48F-1D18A9856A87","full_name":"Mckenzie, Catherine","last_name":"Mckenzie"},{"first_name":"Miroslava","last_name":"Spanova","full_name":"Spanova, Miroslava","id":"44A924DC-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Johnson","id":"46A62C3A-F248-11E8-B48F-1D18A9856A87","full_name":"Johnson, Alexander J","orcid":"0000-0002-2739-8843","first_name":"Alexander J"},{"first_name":"Stephanie","last_name":"Kainrath","id":"32CFBA64-F248-11E8-B48F-1D18A9856A87","full_name":"Kainrath, Stephanie"},{"last_name":"Zheden","full_name":"Zheden, Vanessa","id":"39C5A68A-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-9438-4783","first_name":"Vanessa"},{"full_name":"Sitte, Harald H.","last_name":"Sitte","first_name":"Harald H."},{"full_name":"Janovjak, Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","last_name":"Janovjak","orcid":"0000-0002-8023-9315","first_name":"Harald L"}],"oa_version":"None","title":"Isolation of synaptic vesicles from genetically engineered cultured neurons","publication_identifier":{"issn":["0165-0270"]},"publication_status":"published","acknowledged_ssus":[{"_id":"Bio"},{"_id":"EM-Fac"}],"abstract":[{"text":"Background\r\nSynaptic vesicles (SVs) are an integral part of the neurotransmission machinery, and isolation of SVs from their host neuron is necessary to reveal their most fundamental biochemical and functional properties in in vitro assays. Isolated SVs from neurons that have been genetically engineered, e.g. to introduce genetically encoded indicators, are not readily available but would permit new insights into SV structure and function. Furthermore, it is unclear if cultured neurons can provide sufficient starting material for SV isolation procedures.\r\n\r\nNew method\r\nHere, we demonstrate an efficient ex vivo procedure to obtain functional SVs from cultured rat cortical neurons after genetic engineering with a lentivirus.\r\n\r\nResults\r\nWe show that ∼108 plated cortical neurons allow isolation of suitable SV amounts for functional analysis and imaging. We found that SVs isolated from cultured neurons have neurotransmitter uptake comparable to that of SVs isolated from intact cortex. Using total internal reflection fluorescence (TIRF) microscopy, we visualized an exogenous SV-targeted marker protein and demonstrated the high efficiency of SV modification.\r\n\r\nComparison with existing methods\r\nObtaining SVs from genetically engineered neurons currently generally requires the availability of transgenic animals, which is constrained by technical (e.g. cost and time) and biological (e.g. developmental defects and lethality) limitations.\r\n\r\nConclusions\r\nThese results demonstrate the modification and isolation of functional SVs using cultured neurons and viral transduction. The ability to readily obtain SVs from genetically engineered neurons will permit linking in situ studies to in vitro experiments in a variety of genetic contexts.","lang":"eng"}],"intvolume":"       312"},{"external_id":{"isi":["000432280000006"]},"isi":1,"year":"2018","publication":"Nature Communications","status":"public","project":[{"grant_number":"303564","name":"Microbial Ion Channels for Synthetic Neurobiology","call_identifier":"FP7","_id":"25548C20-B435-11E9-9278-68D0E5697425"},{"_id":"255A6082-B435-11E9-9278-68D0E5697425","grant_number":"W1232-B24","name":"Molecular Drug Targets","call_identifier":"FWF"}],"date_published":"2018-12-01T00:00:00Z","ec_funded":1,"publisher":"Springer Nature","article_processing_charge":"No","doi":"10.1038/s41467-018-04342-1","type":"journal_article","_id":"5984","date_updated":"2023-09-19T14:29:32Z","ddc":["570"],"quality_controlled":"1","month":"12","file":[{"file_name":"2018_Springer_Morri.pdf","access_level":"open_access","content_type":"application/pdf","relation":"main_file","checksum":"8325fcc194264af4749e662a73bf66b5","date_created":"2019-02-14T10:58:29Z","file_size":1349914,"creator":"kschuh","date_updated":"2020-07-14T12:47:14Z","file_id":"5985"}],"article_number":"1950","department":[{"_id":"HaJa"},{"_id":"CaGu"},{"_id":"MiSi"}],"language":[{"iso":"eng"}],"oa":1,"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","citation":{"short":"M. Morri, I. Sanchez-Romero, A.-M. Tichy, S. Kainrath, E.J. Gerrard, P. Hirschfeld, J. Schwarz, H.L. Janovjak, Nature Communications 9 (2018).","ieee":"M. Morri <i>et al.</i>, “Optical functionalization of human class A orphan G-protein-coupled receptors,” <i>Nature Communications</i>, vol. 9, no. 1. Springer Nature, 2018.","ama":"Morri M, Sanchez-Romero I, Tichy A-M, et al. Optical functionalization of human class A orphan G-protein-coupled receptors. <i>Nature Communications</i>. 2018;9(1). doi:<a href=\"https://doi.org/10.1038/s41467-018-04342-1\">10.1038/s41467-018-04342-1</a>","mla":"Morri, Maurizio, et al. “Optical Functionalization of Human Class A Orphan G-Protein-Coupled Receptors.” <i>Nature Communications</i>, vol. 9, no. 1, 1950, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41467-018-04342-1\">10.1038/s41467-018-04342-1</a>.","apa":"Morri, M., Sanchez-Romero, I., Tichy, A.-M., Kainrath, S., Gerrard, E. J., Hirschfeld, P., … Janovjak, H. L. (2018). Optical functionalization of human class A orphan G-protein-coupled receptors. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-018-04342-1\">https://doi.org/10.1038/s41467-018-04342-1</a>","chicago":"Morri, Maurizio, Inmaculada Sanchez-Romero, Alexandra-Madelaine Tichy, Stephanie Kainrath, Elliot J. Gerrard, Priscila Hirschfeld, Jan Schwarz, and Harald L Janovjak. “Optical Functionalization of Human Class A Orphan G-Protein-Coupled Receptors.” <i>Nature Communications</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41467-018-04342-1\">https://doi.org/10.1038/s41467-018-04342-1</a>.","ista":"Morri M, Sanchez-Romero I, Tichy A-M, Kainrath S, Gerrard EJ, Hirschfeld P, Schwarz J, Janovjak HL. 2018. Optical functionalization of human class A orphan G-protein-coupled receptors. Nature Communications. 9(1), 1950."},"issue":"1","title":"Optical functionalization of human class A orphan G-protein-coupled receptors","oa_version":"Published Version","day":"01","scopus_import":"1","author":[{"first_name":"Maurizio","last_name":"Morri","id":"4863116E-F248-11E8-B48F-1D18A9856A87","full_name":"Morri, Maurizio"},{"first_name":"Inmaculada","last_name":"Sanchez-Romero","full_name":"Sanchez-Romero, Inmaculada","id":"3D9C5D30-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Alexandra-Madelaine","id":"29D8BB2C-F248-11E8-B48F-1D18A9856A87","full_name":"Tichy, Alexandra-Madelaine","last_name":"Tichy"},{"full_name":"Kainrath, Stephanie","id":"32CFBA64-F248-11E8-B48F-1D18A9856A87","last_name":"Kainrath","first_name":"Stephanie"},{"full_name":"Gerrard, Elliot J.","last_name":"Gerrard","first_name":"Elliot J."},{"last_name":"Hirschfeld","id":"435ACB3A-F248-11E8-B48F-1D18A9856A87","full_name":"Hirschfeld, Priscila","first_name":"Priscila"},{"first_name":"Jan","full_name":"Schwarz, Jan","id":"346C1EC6-F248-11E8-B48F-1D18A9856A87","last_name":"Schwarz"},{"id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Janovjak, Harald L","last_name":"Janovjak","orcid":"0000-0002-8023-9315","first_name":"Harald L"}],"date_created":"2019-02-14T10:50:24Z","volume":9,"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)"},"abstract":[{"text":"G-protein-coupled receptors (GPCRs) form the largest receptor family, relay environmental stimuli to changes in cell behavior and represent prime drug targets. Many GPCRs are classified as orphan receptors because of the limited knowledge on their ligands and coupling to cellular signaling machineries. Here, we engineer a library of 63 chimeric receptors that contain the signaling domains of human orphan and understudied GPCRs functionally linked to the light-sensing domain of rhodopsin. Upon stimulation with visible light, we identify activation of canonical cell signaling pathways, including cAMP-, Ca2+-, MAPK/ERK-, and Rho-dependent pathways, downstream of the engineered receptors. For the human pseudogene GPR33, we resurrect a signaling function that supports its hypothesized role as a pathogen entry site. These results demonstrate that substituting unknown chemical activators with a light switch can reveal information about protein function and provide an optically controlled protein library for exploring the physiology and therapeutic potential of understudied GPCRs.","lang":"eng"}],"intvolume":"         9","has_accepted_license":"1","file_date_updated":"2020-07-14T12:47:14Z","publication_identifier":{"issn":["2041-1723"]},"publication_status":"published"},{"page":"4679 - 4682","ddc":["571"],"quality_controlled":"1","doi":"10.1002/ange.201611998","publisher":"Wiley","date_updated":"2021-01-12T08:01:33Z","_id":"538","type":"journal_article","project":[{"call_identifier":"FP7","name":"Microbial Ion Channels for Synthetic Neurobiology","grant_number":"303564","_id":"25548C20-B435-11E9-9278-68D0E5697425"},{"call_identifier":"FWF","name":"Molecular Drug Targets","grant_number":"W1232-B24","_id":"255A6082-B435-11E9-9278-68D0E5697425"}],"publication":"Angewandte Chemie","status":"public","ec_funded":1,"date_published":"2017-05-20T00:00:00Z","year":"2017","publist_id":"7279","has_accepted_license":"1","intvolume":"       129","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)"},"abstract":[{"lang":"ger","text":"Optogenetik und Photopharmakologie ermöglichen präzise räumliche und zeitliche Kontrolle von Proteinwechselwirkung und -funktion in Zellen und Tieren. Optogenetische Methoden, die auf grünes Licht ansprechen und zum Trennen von Proteinkomplexen geeignet sind, sind nichtweitläufig verfügbar, würden jedoch mehrfarbige Experimente zur Beantwortung von biologischen Fragestellungen ermöglichen. Hier demonstrieren wir die Verwendung von Cobalamin(Vitamin B12)-bindenden Domänen von bakteriellen CarH-Transkriptionsfaktoren zur Grünlicht-induzierten Dissoziation von Rezeptoren. Fusioniert mit dem Fibroblasten-W achstumsfaktor-Rezeptor 1 führten diese im Dunkeln in kultivierten Zellen zu Signalaktivität durch Oligomerisierung, welche durch Beleuchten umgehend aufgehoben wurde. In Zebrafischembryonen, die einen derartigen Rezeptor exprimieren, ermöglichte grünes Licht die Kontrolle über abnormale Signalaktivität während der Embryonalentwicklung. "}],"publication_status":"published","file_date_updated":"2020-07-14T12:46:39Z","author":[{"last_name":"Kainrath","id":"32CFBA64-F248-11E8-B48F-1D18A9856A87","full_name":"Kainrath, Stephanie","first_name":"Stephanie"},{"first_name":"Manuela","last_name":"Stadler","full_name":"Stadler, Manuela"},{"last_name":"Gschaider-Reichhart","full_name":"Gschaider-Reichhart, Eva","id":"3FEE232A-F248-11E8-B48F-1D18A9856A87","first_name":"Eva","orcid":"0000-0002-7218-7738"},{"first_name":"Martin","full_name":"Distel, Martin","last_name":"Distel"},{"last_name":"Janovjak","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Janovjak, Harald L","first_name":"Harald L","orcid":"0000-0002-8023-9315"}],"day":"20","oa_version":"Published Version","title":"Grünlicht-induzierte Rezeptorinaktivierung durch Cobalamin-bindende Domänen","volume":129,"date_created":"2018-12-11T11:47:02Z","oa":1,"pubrep_id":"932","language":[{"iso":"eng"}],"issue":"16","citation":{"ama":"Kainrath S, Stadler M, Gschaider-Reichhart E, Distel M, Janovjak HL. Grünlicht-induzierte Rezeptorinaktivierung durch Cobalamin-bindende Domänen. <i>Angewandte Chemie</i>. 2017;129(16):4679-4682. doi:<a href=\"https://doi.org/10.1002/ange.201611998\">10.1002/ange.201611998</a>","ieee":"S. Kainrath, M. Stadler, E. Gschaider-Reichhart, M. Distel, and H. L. Janovjak, “Grünlicht-induzierte Rezeptorinaktivierung durch Cobalamin-bindende Domänen,” <i>Angewandte Chemie</i>, vol. 129, no. 16. Wiley, pp. 4679–4682, 2017.","short":"S. Kainrath, M. Stadler, E. Gschaider-Reichhart, M. Distel, H.L. Janovjak, Angewandte Chemie 129 (2017) 4679–4682.","chicago":"Kainrath, Stephanie, Manuela Stadler, Eva Gschaider-Reichhart, Martin Distel, and Harald L Janovjak. “Grünlicht-Induzierte Rezeptorinaktivierung Durch Cobalamin-Bindende Domänen.” <i>Angewandte Chemie</i>. Wiley, 2017. <a href=\"https://doi.org/10.1002/ange.201611998\">https://doi.org/10.1002/ange.201611998</a>.","ista":"Kainrath S, Stadler M, Gschaider-Reichhart E, Distel M, Janovjak HL. 2017. Grünlicht-induzierte Rezeptorinaktivierung durch Cobalamin-bindende Domänen. Angewandte Chemie. 129(16), 4679–4682.","apa":"Kainrath, S., Stadler, M., Gschaider-Reichhart, E., Distel, M., &#38; Janovjak, H. L. (2017). Grünlicht-induzierte Rezeptorinaktivierung durch Cobalamin-bindende Domänen. <i>Angewandte Chemie</i>. Wiley. <a href=\"https://doi.org/10.1002/ange.201611998\">https://doi.org/10.1002/ange.201611998</a>","mla":"Kainrath, Stephanie, et al. “Grünlicht-Induzierte Rezeptorinaktivierung Durch Cobalamin-Bindende Domänen.” <i>Angewandte Chemie</i>, vol. 129, no. 16, Wiley, 2017, pp. 4679–82, doi:<a href=\"https://doi.org/10.1002/ange.201611998\">10.1002/ange.201611998</a>."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","month":"05","department":[{"_id":"CaGu"},{"_id":"HaJa"}],"file":[{"date_created":"2018-12-12T10:13:24Z","file_size":1668557,"creator":"system","date_updated":"2020-07-14T12:46:39Z","file_id":"5007","file_name":"IST-2018-932-v1+1_Kainrath_et_al-2017-Angewandte_Chemie.pdf","content_type":"application/pdf","access_level":"open_access","relation":"main_file","checksum":"d66fee867e7cdbfa3fe276c2fb0778bb"}]},{"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","citation":{"ama":"Agus V, Janovjak HL. Optogenetic methods in drug screening: Technologies and applications. <i>Current Opinion in Biotechnology</i>. 2017;48:8-14. doi:<a href=\"https://doi.org/10.1016/j.copbio.2017.02.006\">10.1016/j.copbio.2017.02.006</a>","ieee":"V. Agus and H. L. Janovjak, “Optogenetic methods in drug screening: Technologies and applications,” <i>Current Opinion in Biotechnology</i>, vol. 48. Elsevier, pp. 8–14, 2017.","short":"V. Agus, H.L. Janovjak, Current Opinion in Biotechnology 48 (2017) 8–14.","chicago":"Agus, Viviana, and Harald L Janovjak. “Optogenetic Methods in Drug Screening: Technologies and Applications.” <i>Current Opinion in Biotechnology</i>. Elsevier, 2017. <a href=\"https://doi.org/10.1016/j.copbio.2017.02.006\">https://doi.org/10.1016/j.copbio.2017.02.006</a>.","ista":"Agus V, Janovjak HL. 2017. Optogenetic methods in drug screening: Technologies and applications. Current Opinion in Biotechnology. 48, 8–14.","apa":"Agus, V., &#38; Janovjak, H. L. (2017). Optogenetic methods in drug screening: Technologies and applications. <i>Current Opinion in Biotechnology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.copbio.2017.02.006\">https://doi.org/10.1016/j.copbio.2017.02.006</a>","mla":"Agus, Viviana, and Harald L. Janovjak. “Optogenetic Methods in Drug Screening: Technologies and Applications.” <i>Current Opinion in Biotechnology</i>, vol. 48, Elsevier, 2017, pp. 8–14, doi:<a href=\"https://doi.org/10.1016/j.copbio.2017.02.006\">10.1016/j.copbio.2017.02.006</a>."},"language":[{"iso":"eng"}],"department":[{"_id":"HaJa"}],"month":"12","publication_status":"published","publication_identifier":{"issn":["09581669"]},"abstract":[{"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.","lang":"eng"}],"intvolume":"        48","date_created":"2018-12-11T11:49:45Z","article_type":"original","volume":48,"title":"Optogenetic methods in drug screening: Technologies and applications","oa_version":"None","scopus_import":"1","day":"01","author":[{"first_name":"Viviana","last_name":"Agus","full_name":"Agus, Viviana"},{"full_name":"Janovjak, Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","last_name":"Janovjak","first_name":"Harald L","orcid":"0000-0002-8023-9315"}],"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).","date_published":"2017-12-01T00:00:00Z","ec_funded":1,"status":"public","publication":"Current Opinion in Biotechnology","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"},{"grant_number":"W1232-B24","name":"Molecular Drug Targets","call_identifier":"FWF","_id":"255A6082-B435-11E9-9278-68D0E5697425"}],"publist_id":"6365","external_id":{"isi":["000418313200003"]},"year":"2017","isi":1,"quality_controlled":"1","page":"8 - 14","type":"journal_article","_id":"1026","date_updated":"2023-09-22T09:26:06Z","publisher":"Elsevier","article_processing_charge":"No","doi":"10.1016/j.copbio.2017.02.006"},{"file":[{"relation":"main_file","content_type":"application/pdf","access_level":"open_access","file_name":"2017_communications_Kainrath.pdf","success":1,"file_id":"5845","creator":"dernst","date_updated":"2019-01-18T09:39:55Z","file_size":2614942,"date_created":"2019-01-18T09:39:55Z"}],"department":[{"_id":"CaGu"},{"_id":"HaJa"}],"month":"03","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","issue":"16","citation":{"ama":"Kainrath S, Stadler M, Gschaider-Reichhart E, Distel M, Janovjak HL. Green-light-induced inactivation of receptor signaling using cobalamin-binding domains. <i>Angewandte Chemie - International Edition</i>. 2017;56(16):4608-4611. doi:<a href=\"https://doi.org/10.1002/anie.201611998\">10.1002/anie.201611998</a>","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,” <i>Angewandte Chemie - International Edition</i>, vol. 56, no. 16. Wiley-Blackwell, pp. 4608–4611, 2017.","short":"S. Kainrath, M. Stadler, E. Gschaider-Reichhart, M. Distel, H.L. Janovjak, Angewandte Chemie - International Edition 56 (2017) 4608–4611.","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.” <i>Angewandte Chemie - International Edition</i>. Wiley-Blackwell, 2017. <a href=\"https://doi.org/10.1002/anie.201611998\">https://doi.org/10.1002/anie.201611998</a>.","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.","apa":"Kainrath, S., Stadler, M., Gschaider-Reichhart, E., Distel, M., &#38; Janovjak, H. L. (2017). Green-light-induced inactivation of receptor signaling using cobalamin-binding domains. <i>Angewandte Chemie - International Edition</i>. Wiley-Blackwell. <a href=\"https://doi.org/10.1002/anie.201611998\">https://doi.org/10.1002/anie.201611998</a>","mla":"Kainrath, Stephanie, et al. “Green-Light-Induced Inactivation of Receptor Signaling Using Cobalamin-Binding Domains.” <i>Angewandte Chemie - International Edition</i>, vol. 56, no. 16, Wiley-Blackwell, 2017, pp. 4608–11, doi:<a href=\"https://doi.org/10.1002/anie.201611998\">10.1002/anie.201611998</a>."},"language":[{"iso":"eng"}],"oa":1,"date_created":"2018-12-11T11:49:46Z","volume":56,"title":"Green-light-induced inactivation of receptor signaling using cobalamin-binding domains","oa_version":"Published Version","author":[{"first_name":"Stephanie","id":"32CFBA64-F248-11E8-B48F-1D18A9856A87","full_name":"Kainrath, Stephanie","last_name":"Kainrath"},{"first_name":"Manuela","last_name":"Stadler","full_name":"Stadler, Manuela"},{"first_name":"Eva","orcid":"0000-0002-7218-7738","last_name":"Gschaider-Reichhart","id":"3FEE232A-F248-11E8-B48F-1D18A9856A87","full_name":"Gschaider-Reichhart, Eva"},{"first_name":"Martin","full_name":"Distel, Martin","last_name":"Distel"},{"orcid":"0000-0002-8023-9315","first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Janovjak, Harald L","last_name":"Janovjak"}],"day":"20","scopus_import":"1","publication_status":"published","publication_identifier":{"issn":["14337851"]},"file_date_updated":"2019-01-18T09:39:55Z","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)"},"abstract":[{"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.","lang":"eng"}],"intvolume":"        56","has_accepted_license":"1","publist_id":"6362","external_id":{"isi":["000398154000038"]},"related_material":{"record":[{"relation":"dissertation_contains","status":"public","id":"418"},{"id":"7680","status":"public","relation":"part_of_dissertation"}]},"isi":1,"year":"2017","date_published":"2017-03-20T00:00:00Z","acknowledgement":"This work was supported by a grant from the European Union􏰝s 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)","ec_funded":1,"project":[{"_id":"25548C20-B435-11E9-9278-68D0E5697425","call_identifier":"FP7","grant_number":"303564","name":"Microbial Ion Channels for Synthetic Neurobiology"},{"call_identifier":"FWF","grant_number":"W1232-B24","name":"Molecular Drug Targets [do not use to be deleted]","_id":"26AA4EF2-B435-11E9-9278-68D0E5697425"}],"status":"public","publication":"Angewandte Chemie - International Edition","type":"journal_article","date_updated":"2024-03-25T23:30:08Z","_id":"1028","publisher":"Wiley-Blackwell","doi":"10.1002/anie.201611998","article_processing_charge":"No","quality_controlled":"1","ddc":["540"],"page":"4608-4611"},{"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.","date_published":"2016-07-19T00:00:00Z","ec_funded":1,"project":[{"_id":"2529486C-B435-11E9-9278-68D0E5697425","call_identifier":"FWF","grant_number":"T 560-B17","name":"Cell- and Tissue Mechanics in Zebrafish Germ Layer Formation"},{"_id":"2527D5CC-B435-11E9-9278-68D0E5697425","grant_number":"I 812-B12","name":"Cell Cortex and Germ Layer Formation in Zebrafish Gastrulation","call_identifier":"FWF"},{"call_identifier":"FP7","grant_number":"303564","name":"Microbial Ion Channels for Synthetic Neurobiology","_id":"25548C20-B435-11E9-9278-68D0E5697425"}],"status":"public","publication":"Cell Reports","publist_id":"6275","related_material":{"record":[{"id":"961","relation":"dissertation_contains","status":"public"},{"relation":"dissertation_contains","status":"public","id":"50"}]},"year":"2016","quality_controlled":"1","ddc":["570","576"],"page":"866 - 877","type":"journal_article","date_updated":"2024-03-25T23:30:13Z","_id":"1100","publisher":"Cell Press","doi":"10.1016/j.celrep.2016.06.036","user_id":"4435EBFC-F248-11E8-B48F-1D18A9856A87","issue":"3","citation":{"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.","ieee":"K. Sako <i>et al.</i>, “Optogenetic control of nodal signaling reveals a temporal pattern of nodal signaling regulating cell fate specification during gastrulation,” <i>Cell Reports</i>, vol. 16, no. 3. Cell Press, pp. 866–877, 2016.","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. <i>Cell Reports</i>. 2016;16(3):866-877. doi:<a href=\"https://doi.org/10.1016/j.celrep.2016.06.036\">10.1016/j.celrep.2016.06.036</a>","mla":"Sako, Keisuke, et al. “Optogenetic Control of Nodal Signaling Reveals a Temporal Pattern of Nodal Signaling Regulating Cell Fate Specification during Gastrulation.” <i>Cell Reports</i>, vol. 16, no. 3, Cell Press, 2016, pp. 866–77, doi:<a href=\"https://doi.org/10.1016/j.celrep.2016.06.036\">10.1016/j.celrep.2016.06.036</a>.","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. <i>Cell Reports</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.celrep.2016.06.036\">https://doi.org/10.1016/j.celrep.2016.06.036</a>","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.” <i>Cell Reports</i>. Cell Press, 2016. <a href=\"https://doi.org/10.1016/j.celrep.2016.06.036\">https://doi.org/10.1016/j.celrep.2016.06.036</a>.","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."},"pubrep_id":"754","language":[{"iso":"eng"}],"oa":1,"file":[{"file_id":"4857","creator":"system","date_updated":"2018-12-12T10:11:04Z","date_created":"2018-12-12T10:11:04Z","file_size":3921947,"relation":"main_file","content_type":"application/pdf","access_level":"open_access","file_name":"IST-2017-754-v1+1_1-s2.0-S2211124716307768-main.pdf"}],"department":[{"_id":"CaHe"},{"_id":"HaJa"}],"month":"07","publication_status":"published","file_date_updated":"2018-12-12T10:11:04Z","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)"},"intvolume":"        16","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."}],"acknowledged_ssus":[{"_id":"SSU"}],"has_accepted_license":"1","date_created":"2018-12-11T11:50:08Z","volume":16,"oa_version":"Published Version","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","full_name":"Sako, Keisuke","last_name":"Sako","first_name":"Keisuke","orcid":"0000-0002-6453-8075"},{"full_name":"Pradhan, Saurabh","last_name":"Pradhan","first_name":"Saurabh"},{"last_name":"Barone","full_name":"Barone, Vanessa","id":"419EECCC-F248-11E8-B48F-1D18A9856A87","first_name":"Vanessa","orcid":"0000-0003-2676-3367"},{"orcid":"0000-0002-5409-8571","first_name":"Álvaro","full_name":"Inglés Prieto, Álvaro","id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","last_name":"Inglés Prieto"},{"first_name":"Patrick","full_name":"Mueller, Patrick","last_name":"Mueller"},{"full_name":"Ruprecht, Verena","id":"4D71A03A-F248-11E8-B48F-1D18A9856A87","last_name":"Ruprecht","first_name":"Verena","orcid":"0000-0003-4088-8633"},{"last_name":"Capek","full_name":"Capek, Daniel","id":"31C42484-F248-11E8-B48F-1D18A9856A87","first_name":"Daniel","orcid":"0000-0001-5199-9940"},{"first_name":"Sanjeev","last_name":"Galande","full_name":"Galande, Sanjeev"},{"last_name":"Janovjak","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Janovjak, Harald L","orcid":"0000-0002-8023-9315","first_name":"Harald L"},{"last_name":"Heisenberg","id":"39427864-F248-11E8-B48F-1D18A9856A87","full_name":"Heisenberg, Carl-Philipp J","orcid":"0000-0002-0912-4566","first_name":"Carl-Philipp J"}],"scopus_import":1,"day":"19"},{"doi":"10.1016/j.str.2016.01.002","author":[{"orcid":"0000-0002-8023-9315","first_name":"Harald L","full_name":"Janovjak, Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","last_name":"Janovjak"}],"day":"02","scopus_import":1,"oa_version":"None","title":"Light at the end of the protein: Crystal structure of a C-terminal light-sensing domain","publisher":"Cell Press","date_updated":"2021-01-12T06:50:46Z","volume":24,"_id":"1440","type":"journal_article","date_created":"2018-12-11T11:52:02Z","page":"213 - 215","intvolume":"        24","quality_controlled":"1","publication_status":"published","year":"2016","month":"02","department":[{"_id":"HaJa"}],"publist_id":"5756","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)"},{"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","call_identifier":"FWF","_id":"255A6082-B435-11E9-9278-68D0E5697425"}],"status":"public","language":[{"iso":"eng"}],"publication":"Structure","issue":"2","citation":{"ama":"Janovjak HL. Light at the end of the protein: Crystal structure of a C-terminal light-sensing domain. <i>Structure</i>. 2016;24(2):213-215. doi:<a href=\"https://doi.org/10.1016/j.str.2016.01.002\">10.1016/j.str.2016.01.002</a>","ieee":"H. L. Janovjak, “Light at the end of the protein: Crystal structure of a C-terminal light-sensing domain,” <i>Structure</i>, vol. 24, no. 2. Cell Press, pp. 213–215, 2016.","short":"H.L. Janovjak, Structure 24 (2016) 213–215.","chicago":"Janovjak, Harald L. “Light at the End of the Protein: Crystal Structure of a C-Terminal Light-Sensing Domain.” <i>Structure</i>. Cell Press, 2016. <a href=\"https://doi.org/10.1016/j.str.2016.01.002\">https://doi.org/10.1016/j.str.2016.01.002</a>.","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.","apa":"Janovjak, H. L. (2016). Light at the end of the protein: Crystal structure of a C-terminal light-sensing domain. <i>Structure</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.str.2016.01.002\">https://doi.org/10.1016/j.str.2016.01.002</a>","mla":"Janovjak, Harald L. “Light at the End of the Protein: Crystal Structure of a C-Terminal Light-Sensing Domain.” <i>Structure</i>, vol. 24, no. 2, Cell Press, 2016, pp. 213–15, doi:<a href=\"https://doi.org/10.1016/j.str.2016.01.002\">10.1016/j.str.2016.01.002</a>."},"ec_funded":1,"date_published":"2016-02-02T00:00:00Z","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).","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87"},{"type":"journal_article","_id":"1441","date_updated":"2023-09-07T12:49:08Z","publisher":"Wiley","doi":"10.1002/anie.201601736","quality_controlled":"1","ddc":["571","576"],"page":"6339 - 6342","publist_id":"5755","related_material":{"record":[{"id":"418","status":"public","relation":"dissertation_contains"}]},"year":"2016","date_published":"2016-05-17T00:00:00Z","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).","ec_funded":1,"publication":"Angewandte Chemie - International Edition","status":"public","project":[{"call_identifier":"FP7","grant_number":"303564","name":"Microbial Ion Channels for Synthetic Neurobiology","_id":"25548C20-B435-11E9-9278-68D0E5697425"},{"_id":"255A6082-B435-11E9-9278-68D0E5697425","call_identifier":"FWF","name":"Molecular Drug Targets","grant_number":"W1232-B24"}],"date_created":"2018-12-11T11:52:02Z","volume":55,"oa_version":"Submitted Version","title":"A phytochrome sensory domain permits receptor activation by red light","day":"17","scopus_import":1,"author":[{"full_name":"Gschaider-Reichhart, Eva","id":"3FEE232A-F248-11E8-B48F-1D18A9856A87","last_name":"Gschaider-Reichhart","orcid":"0000-0002-7218-7738","first_name":"Eva"},{"first_name":"Álvaro","orcid":"0000-0002-5409-8571","full_name":"Inglés Prieto, Álvaro","id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","last_name":"Inglés Prieto"},{"first_name":"Alexandra-Madelaine","last_name":"Tichy","id":"29D8BB2C-F248-11E8-B48F-1D18A9856A87","full_name":"Tichy, Alexandra-Madelaine"},{"last_name":"Mckenzie","full_name":"Mckenzie, Catherine","id":"3EEDE19A-F248-11E8-B48F-1D18A9856A87","first_name":"Catherine"},{"full_name":"Janovjak, Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","last_name":"Janovjak","orcid":"0000-0002-8023-9315","first_name":"Harald L"}],"file_date_updated":"2020-07-14T12:44:55Z","publication_status":"published","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."}],"has_accepted_license":"1","file":[{"date_updated":"2020-07-14T12:44:55Z","creator":"system","date_created":"2018-12-12T10:17:03Z","file_size":1268662,"file_id":"5255","content_type":"application/pdf","access_level":"open_access","file_name":"IST-2017-840-v1+1_reichhart.pdf","checksum":"26da07960e57ac4750b54179197ce57f","relation":"main_file"}],"department":[{"_id":"HaJa"}],"month":"05","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"short":"E. Gschaider-Reichhart, Á. Inglés Prieto, A.-M. Tichy, C. Mckenzie, H.L. Janovjak, Angewandte Chemie - International Edition 55 (2016) 6339–6342.","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,” <i>Angewandte Chemie - International Edition</i>, vol. 55, no. 21. Wiley, pp. 6339–6342, 2016.","ama":"Gschaider-Reichhart E, Inglés Prieto Á, Tichy A-M, Mckenzie C, Janovjak HL. A phytochrome sensory domain permits receptor activation by red light. <i>Angewandte Chemie - International Edition</i>. 2016;55(21):6339-6342. doi:<a href=\"https://doi.org/10.1002/anie.201601736\">10.1002/anie.201601736</a>","mla":"Gschaider-Reichhart, Eva, et al. “A Phytochrome Sensory Domain Permits Receptor Activation by Red Light.” <i>Angewandte Chemie - International Edition</i>, vol. 55, no. 21, Wiley, 2016, pp. 6339–42, doi:<a href=\"https://doi.org/10.1002/anie.201601736\">10.1002/anie.201601736</a>.","apa":"Gschaider-Reichhart, E., Inglés Prieto, Á., Tichy, A.-M., Mckenzie, C., &#38; Janovjak, H. L. (2016). A phytochrome sensory domain permits receptor activation by red light. <i>Angewandte Chemie - International Edition</i>. Wiley. <a href=\"https://doi.org/10.1002/anie.201601736\">https://doi.org/10.1002/anie.201601736</a>","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.” <i>Angewandte Chemie - International Edition</i>. Wiley, 2016. <a href=\"https://doi.org/10.1002/anie.201601736\">https://doi.org/10.1002/anie.201601736</a>."},"issue":"21","pubrep_id":"840","language":[{"iso":"eng"}],"oa":1},{"page":"952 - 954","ddc":["571"],"quality_controlled":"1","doi":"10.1038/nchembio.1933","publisher":"Nature Publishing Group","date_updated":"2023-09-07T12:49:09Z","_id":"1678","type":"journal_article","project":[{"_id":"25548C20-B435-11E9-9278-68D0E5697425","grant_number":"303564","name":"Microbial Ion Channels for Synthetic Neurobiology","call_identifier":"FP7"},{"_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)"},{"grant_number":"W1232-B24","name":"Molecular Drug Targets","call_identifier":"FWF","_id":"255A6082-B435-11E9-9278-68D0E5697425"}],"status":"public","publication":"Nature Chemical Biology","ec_funded":1,"date_published":"2015-10-12T00:00:00Z","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).","year":"2015","related_material":{"record":[{"relation":"dissertation_contains","status":"public","id":"418"}]},"publist_id":"5471","has_accepted_license":"1","intvolume":"        11","abstract":[{"lang":"eng","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."}],"publication_status":"published","file_date_updated":"2020-07-14T12:45:12Z","author":[{"orcid":"0000-0002-5409-8571","first_name":"Álvaro","full_name":"Inglés Prieto, Álvaro","id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","last_name":"Inglés Prieto"},{"last_name":"Gschaider-Reichhart","full_name":"Gschaider-Reichhart, Eva","id":"3FEE232A-F248-11E8-B48F-1D18A9856A87","first_name":"Eva","orcid":"0000-0002-7218-7738"},{"first_name":"Markus","last_name":"Muellner","full_name":"Muellner, Markus"},{"full_name":"Nowak, Matthias","id":"30845DAA-F248-11E8-B48F-1D18A9856A87","last_name":"Nowak","first_name":"Matthias"},{"first_name":"Sebastian","full_name":"Nijman, Sebastian","last_name":"Nijman"},{"first_name":"Michael","full_name":"Grusch, Michael","last_name":"Grusch"},{"first_name":"Harald L","orcid":"0000-0002-8023-9315","last_name":"Janovjak","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Janovjak, Harald L"}],"scopus_import":1,"day":"12","oa_version":"Submitted Version","title":"Light-assisted small-molecule screening against protein kinases","volume":11,"date_created":"2018-12-11T11:53:25Z","oa":1,"pubrep_id":"837","language":[{"iso":"eng"}],"issue":"12","citation":{"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.","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.” <i>Nature Chemical Biology</i>. Nature Publishing Group, 2015. <a href=\"https://doi.org/10.1038/nchembio.1933\">https://doi.org/10.1038/nchembio.1933</a>.","mla":"Inglés Prieto, Álvaro, et al. “Light-Assisted Small-Molecule Screening against Protein Kinases.” <i>Nature Chemical Biology</i>, vol. 11, no. 12, Nature Publishing Group, 2015, pp. 952–54, doi:<a href=\"https://doi.org/10.1038/nchembio.1933\">10.1038/nchembio.1933</a>.","apa":"Inglés Prieto, Á., Gschaider-Reichhart, E., Muellner, M., Nowak, M., Nijman, S., Grusch, M., &#38; Janovjak, H. L. (2015). Light-assisted small-molecule screening against protein kinases. <i>Nature Chemical Biology</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/nchembio.1933\">https://doi.org/10.1038/nchembio.1933</a>","ama":"Inglés Prieto Á, Gschaider-Reichhart E, Muellner M, et al. Light-assisted small-molecule screening against protein kinases. <i>Nature Chemical Biology</i>. 2015;11(12):952-954. doi:<a href=\"https://doi.org/10.1038/nchembio.1933\">10.1038/nchembio.1933</a>","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 <i>et al.</i>, “Light-assisted small-molecule screening against protein kinases,” <i>Nature Chemical Biology</i>, vol. 11, no. 12. Nature Publishing Group, pp. 952–954, 2015."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","month":"10","department":[{"_id":"HaJa"},{"_id":"LifeSc"}],"file":[{"date_created":"2018-12-12T10:10:51Z","file_size":1308364,"creator":"system","date_updated":"2020-07-14T12:45:12Z","file_id":"4842","file_name":"IST-2017-837-v1+1_ingles-prieto.pdf","content_type":"application/pdf","access_level":"open_access","relation":"main_file","checksum":"e9fb251dfcb7cd209b83f17867e61321"}]},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"short":"J. Hühner, Á. Inglés Prieto, C. Neusüß, M. Lämmerhofer, H.L. Janovjak, Electrophoresis 36 (2015) 518–525.","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,” <i>Electrophoresis</i>, vol. 36, no. 4. Wiley, pp. 518–525, 2015.","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. <i>Electrophoresis</i>. 2015;36(4):518-525. doi:<a href=\"https://doi.org/10.1002/elps.201400451\">10.1002/elps.201400451</a>","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.” <i>Electrophoresis</i>, vol. 36, no. 4, Wiley, 2015, pp. 518–25, doi:<a href=\"https://doi.org/10.1002/elps.201400451\">10.1002/elps.201400451</a>.","apa":"Hühner, J., Inglés Prieto, Á., Neusüß, C., Lämmerhofer, M., &#38; Janovjak, H. L. (2015). Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence detection. <i>Electrophoresis</i>. Wiley. <a href=\"https://doi.org/10.1002/elps.201400451\">https://doi.org/10.1002/elps.201400451</a>","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.” <i>Electrophoresis</i>. Wiley, 2015. <a href=\"https://doi.org/10.1002/elps.201400451\">https://doi.org/10.1002/elps.201400451</a>.","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."},"issue":"4","language":[{"iso":"eng"}],"pubrep_id":"836","department":[{"_id":"HaJa"}],"month":"02","publication_status":"published","abstract":[{"lang":"eng","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."}],"intvolume":"        36","date_created":"2018-12-11T11:54:26Z","volume":36,"oa_version":"None","title":"Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence detection","day":"01","scopus_import":1,"author":[{"first_name":"Jens","full_name":"Hühner, Jens","last_name":"Hühner"},{"orcid":"0000-0002-5409-8571","first_name":"Álvaro","full_name":"Inglés Prieto, Álvaro","id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","last_name":"Inglés Prieto"},{"full_name":"Neusüß, Christian","last_name":"Neusüß","first_name":"Christian"},{"first_name":"Michael","last_name":"Lämmerhofer","full_name":"Lämmerhofer, Michael"},{"last_name":"Janovjak","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Janovjak, Harald L","orcid":"0000-0002-8023-9315","first_name":"Harald L"}],"date_published":"2015-02-01T00:00:00Z","ec_funded":1,"status":"public","publication":"Electrophoresis","project":[{"call_identifier":"FP7","name":"Microbial Ion Channels for Synthetic Neurobiology","grant_number":"303564","_id":"25548C20-B435-11E9-9278-68D0E5697425"},{"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"}],"publist_id":"5230","year":"2015","quality_controlled":"1","page":"518 - 525","type":"journal_article","_id":"1867","date_updated":"2021-01-12T06:53:43Z","publisher":"Wiley","doi":"10.1002/elps.201400451"},{"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"},{"grant_number":"303564","name":"Microbial Ion Channels for Synthetic Neurobiology","call_identifier":"FP7","_id":"25548C20-B435-11E9-9278-68D0E5697425"}],"publication":"Methods in Molecular Biology","status":"public","date_published":"2013-02-22T00:00:00Z","ec_funded":1,"year":"2013","publist_id":"3932","ddc":["570"],"page":"417 - 435","quality_controlled":"1","publisher":"Springer","doi":"10.1007/978-1-62703-351-0_32","alternative_title":["MIMB"],"type":"journal_article","date_updated":"2021-01-12T07:00:17Z","_id":"2857","pubrep_id":"834","language":[{"iso":"eng"}],"oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"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.” <i>Methods in Molecular Biology</i>. Springer, 2013. <a href=\"https://doi.org/10.1007/978-1-62703-351-0_32\">https://doi.org/10.1007/978-1-62703-351-0_32</a>.","apa":"Szobota, S., Mckenzie, C., &#38; Janovjak, H. L. (2013). Optical control of ligand-gated ion channels. <i>Methods in Molecular Biology</i>. Springer. <a href=\"https://doi.org/10.1007/978-1-62703-351-0_32\">https://doi.org/10.1007/978-1-62703-351-0_32</a>","mla":"Szobota, Stephanie, et al. “Optical Control of Ligand-Gated Ion Channels.” <i>Methods in Molecular Biology</i>, vol. 998, Springer, 2013, pp. 417–35, doi:<a href=\"https://doi.org/10.1007/978-1-62703-351-0_32\">10.1007/978-1-62703-351-0_32</a>.","ama":"Szobota S, Mckenzie C, Janovjak HL. Optical control of ligand-gated ion channels. <i>Methods in Molecular Biology</i>. 2013;998:417-435. doi:<a href=\"https://doi.org/10.1007/978-1-62703-351-0_32\">10.1007/978-1-62703-351-0_32</a>","ieee":"S. Szobota, C. Mckenzie, and H. L. Janovjak, “Optical control of ligand-gated ion channels,” <i>Methods in Molecular Biology</i>, vol. 998. Springer, pp. 417–435, 2013.","short":"S. Szobota, C. Mckenzie, H.L. Janovjak, Methods in Molecular Biology 998 (2013) 417–435."},"month":"02","file":[{"checksum":"1701f0d989f27ddac471b19a894ec0d1","relation":"main_file","content_type":"application/pdf","access_level":"open_access","file_name":"IST-2017-834-v1+1_szobota.pdf","file_id":"4952","date_updated":"2020-07-14T12:45:51Z","creator":"system","file_size":336734,"date_created":"2018-12-12T10:12:34Z"}],"department":[{"_id":"HaJa"}],"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"}],"has_accepted_license":"1","publication_status":"published","file_date_updated":"2020-07-14T12:45:51Z","title":"Optical control of ligand-gated ion channels","oa_version":"Submitted Version","author":[{"first_name":"Stephanie","last_name":"Szobota","full_name":"Szobota, Stephanie"},{"last_name":"Mckenzie","full_name":"Mckenzie, Catherine","id":"3EEDE19A-F248-11E8-B48F-1D18A9856A87","first_name":"Catherine"},{"first_name":"Harald L","orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","last_name":"Janovjak"}],"scopus_import":1,"day":"22","date_created":"2018-12-11T11:59:57Z","volume":998}]