[{"day":"01","scopus_import":1,"date_published":"2014-07-01T00:00:00Z","publication":"EMBO Journal","citation":{"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","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.","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","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.","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.","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.","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."},"page":"1713 - 1726","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"}],"issue":"15","type":"journal_article","oa_version":"Submitted Version","user_id":"4435EBFC-F248-11E8-B48F-1D18A9856A87","_id":"2084","title":"Spatio-temporally precise activation of engineered receptor tyrosine kinases by light","status":"public","intvolume":" 33","month":"07","doi":"10.15252/embj.201387695","language":[{"iso":"eng"}],"main_file_link":[{"url":"http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4194103/","open_access":"1"}],"oa":1,"quality_controlled":"1","publist_id":"4953","author":[{"full_name":"Grusch, Michael","first_name":"Michael","last_name":"Grusch"},{"first_name":"Karin","last_name":"Schelch","full_name":"Schelch, Karin"},{"last_name":"Riedler","first_name":"Robert","full_name":"Riedler, Robert"},{"last_name":"Gschaider-Reichhart","first_name":"Eva","orcid":"0000-0002-7218-7738","id":"3FEE232A-F248-11E8-B48F-1D18A9856A87","full_name":"Gschaider-Reichhart, Eva"},{"full_name":"Differ, Christopher","last_name":"Differ","first_name":"Christopher"},{"full_name":"Berger, Walter","last_name":"Berger","first_name":"Walter"},{"full_name":"Inglés Prieto, Álvaro","id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-5409-8571","first_name":"Álvaro","last_name":"Inglés Prieto"},{"first_name":"Harald L","last_name":"Janovjak","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L"}],"related_material":{"record":[{"status":"public","relation":"dissertation_contains","id":"418"}]},"date_updated":"2023-09-07T12:49:09Z","date_created":"2018-12-11T11:55:37Z","volume":33,"year":"2014","acknowledgement":"European Union Seventh Framework Programme; Human Frontier Science Program; Oesterreichische Nationalbank Anniversary Fund 14211; Austrian Research Promotion Agency; FemTech","publication_status":"published","department":[{"_id":"HaJa"}],"publisher":"Wiley-Blackwell"},{"file_date_updated":"2020-07-14T12:45:41Z","publist_id":"4430","license":"https://creativecommons.org/licenses/by/4.0/","article_number":"e70013","author":[{"full_name":"Sanchez Romero, Inmaculada","id":"3D9C5D30-F248-11E8-B48F-1D18A9856A87","first_name":"Inmaculada","last_name":"Sanchez Romero"},{"last_name":"Ariza","first_name":"Antonio","full_name":"Ariza, Antonio"},{"full_name":"Wilson, Keith","last_name":"Wilson","first_name":"Keith"},{"full_name":"Skjøt, Michael","first_name":"Michael","last_name":"Skjøt"},{"full_name":"Vind, Jesper","last_name":"Vind","first_name":"Jesper"},{"last_name":"De Maria","first_name":"Leonardo","full_name":"De Maria, Leonardo"},{"last_name":"Skov","first_name":"Lars","full_name":"Skov, Lars"},{"full_name":"Sánchez Ruiz, Jose","last_name":"Sánchez Ruiz","first_name":"Jose"}],"date_created":"2018-12-11T11:57:51Z","date_updated":"2021-01-12T06:57:41Z","volume":8,"year":"2013","publication_status":"published","department":[{"_id":"HaJa"}],"publisher":"Public Library of Science","month":"07","doi":"10.1371/journal.pone.0070013","language":[{"iso":"eng"}],"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","short":"CC BY (4.0)","image":"/images/cc_by.png"},"oa":1,"quality_controlled":"1","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."}],"issue":"7","type":"journal_article","pubrep_id":"414","oa_version":"Published Version","file":[{"creator":"system","content_type":"application/pdf","file_size":1323666,"access_level":"open_access","file_name":"IST-2016-414-v1+1_journal.pone.0070013.pdf","checksum":"c0c96cc76ed7ef0d036a31a7e33c9a37","date_updated":"2020-07-14T12:45:41Z","date_created":"2018-12-12T10:15:07Z","file_id":"5124","relation":"main_file"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"2471","title":"Mechanism of protein kinetic stabilization by engineered disulfide crosslinks","status":"public","ddc":["570"],"intvolume":" 8","day":"30","has_accepted_license":"1","scopus_import":1,"date_published":"2013-07-30T00:00:00Z","publication":"PLoS One","citation":{"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.","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","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.","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","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.","short":"I. Sanchez-Romero, A. Ariza, K. Wilson, M. Skjøt, J. Vind, L. De Maria, L. Skov, J. Sánchez Ruiz, PLoS One 8 (2013).","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."}},{"year":"2013","publication_status":"published","publisher":"Springer","department":[{"_id":"HaJa"}],"author":[{"last_name":"Szobota","first_name":"Stephanie","full_name":"Szobota, Stephanie"},{"full_name":"Mckenzie, Catherine","id":"3EEDE19A-F248-11E8-B48F-1D18A9856A87","first_name":"Catherine","last_name":"Mckenzie"},{"full_name":"Janovjak, Harald L","orcid":"0000-0002-8023-9315","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","last_name":"Janovjak","first_name":"Harald L"}],"date_updated":"2021-01-12T07:00:17Z","date_created":"2018-12-11T11:59:57Z","volume":998,"file_date_updated":"2020-07-14T12:45:51Z","ec_funded":1,"publist_id":"3932","oa":1,"quality_controlled":"1","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","name":"Microbial Ion Channels for Synthetic Neurobiology","grant_number":"303564","_id":"25548C20-B435-11E9-9278-68D0E5697425"}],"doi":"10.1007/978-1-62703-351-0_32","language":[{"iso":"eng"}],"month":"02","_id":"2857","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","title":"Optical control of ligand-gated ion channels","ddc":["570"],"intvolume":" 998","pubrep_id":"834","file":[{"date_updated":"2020-07-14T12:45:51Z","date_created":"2018-12-12T10:12:34Z","checksum":"1701f0d989f27ddac471b19a894ec0d1","file_id":"4952","relation":"main_file","creator":"system","content_type":"application/pdf","file_size":336734,"file_name":"IST-2017-834-v1+1_szobota.pdf","access_level":"open_access"}],"oa_version":"Submitted Version","type":"journal_article","alternative_title":["MIMB"],"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"}],"publication":"Methods in Molecular Biology","citation":{"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.","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","ista":"Szobota S, Mckenzie C, Janovjak HL. 2013. Optical control of ligand-gated ion channels. Methods in Molecular Biology. 998, 417–435.","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","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.","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."},"page":"417 - 435","date_published":"2013-02-22T00:00:00Z","scopus_import":1,"day":"22","has_accepted_license":"1"},{"publisher":"Nature Publishing Group","department":[{"_id":"HaJa"}],"publication_status":"published","pmid":1,"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.)","year":"2013","volume":16,"date_created":"2018-12-11T11:59:57Z","date_updated":"2021-01-12T07:00:16Z","author":[{"full_name":"Levitz, Joshua","last_name":"Levitz","first_name":"Joshua"},{"first_name":"Carlos","last_name":"Pantoja","full_name":"Pantoja, Carlos"},{"full_name":"Gaub, Benjamin","last_name":"Gaub","first_name":"Benjamin"},{"last_name":"Janovjak","first_name":"Harald L","orcid":"0000-0002-8023-9315","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Janovjak, Harald L"},{"first_name":"Andreas","last_name":"Reiner","full_name":"Reiner, Andreas"},{"last_name":"Hoagland","first_name":"Adam","full_name":"Hoagland, Adam"},{"full_name":"Schoppik, David","last_name":"Schoppik","first_name":"David"},{"last_name":"Kane","first_name":"Brian","full_name":"Kane, Brian"},{"first_name":"Philipp","last_name":"Stawski","full_name":"Stawski, Philipp"},{"first_name":"Alexander","last_name":"Schier","full_name":"Schier, Alexander"},{"first_name":"Dirk","last_name":"Trauner","full_name":"Trauner, Dirk"},{"last_name":"Isacoff","first_name":"Ehud","full_name":"Isacoff, Ehud"}],"publist_id":"3936","quality_controlled":"1","oa":1,"external_id":{"pmid":["23455609"]},"main_file_link":[{"open_access":"1","url":"http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3681425/"}],"language":[{"iso":"eng"}],"doi":"10.1038/nn.3346","month":"03","intvolume":" 16","title":"Optical control of metabotropic glutamate receptors","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"2856","oa_version":"Submitted Version","type":"journal_article","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."}],"page":"507 - 516","citation":{"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.","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.","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.","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","ieee":"J. Levitz et al., “Optical control of metabotropic glutamate receptors,” Nature Neuroscience, vol. 16. Nature Publishing Group, pp. 507–516, 2013.","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"},"publication":"Nature Neuroscience","date_published":"2013-03-03T00:00:00Z","scopus_import":1,"day":"03"},{"scopus_import":1,"day":"01","month":"02","quality_controlled":"1","page":"381 - 388","publication":"Green Chemistry","citation":{"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.","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","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.","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","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.","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."},"language":[{"iso":"eng"}],"date_published":"2013-02-01T00:00:00Z","doi":"10.1039/c2gc36666e","type":"journal_article","abstract":[{"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.","lang":"eng"}],"publist_id":"7313","issue":"2","publication_status":"published","status":"public","title":"Banning toxic heavy-metal catalysts from paints: Enzymatic cross-linking of alkyd resins","intvolume":" 15","publisher":"Royal Society of Chemistry","department":[{"_id":"HaJa"}],"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.","_id":"505","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2013","date_created":"2018-12-11T11:46:51Z","date_updated":"2021-01-12T08:01:11Z","oa_version":"None","volume":15,"author":[{"last_name":"Greimel","first_name":"Katrin","full_name":"Greimel, Katrin"},{"first_name":"Veronika","last_name":"Perz","full_name":"Perz, Veronika"},{"full_name":"Koren, Klaus","id":"382FBD6A-F248-11E8-B48F-1D18A9856A87","first_name":"Klaus","last_name":"Koren"},{"last_name":"Feola","first_name":"Roland","full_name":"Feola, Roland"},{"last_name":"Temel","first_name":"Armin","full_name":"Temel, Armin"},{"last_name":"Sohar","first_name":"Christian","full_name":"Sohar, Christian"},{"full_name":"Herrero Acero, Enrique","last_name":"Herrero Acero","first_name":"Enrique"},{"full_name":"Klimant, Ingo","last_name":"Klimant","first_name":"Ingo"},{"full_name":"Guebitz, Georg","last_name":"Guebitz","first_name":"Georg"}]},{"date_updated":"2022-06-21T11:51:58Z","date_created":"2022-03-21T07:16:12Z","oa_version":"None","author":[{"id":"3C77F464-F248-11E8-B48F-1D18A9856A87","last_name":"zur Nedden","first_name":"Stephanie","full_name":"zur Nedden, Stephanie"},{"first_name":"Alexander S.","last_name":"Doney","full_name":"Doney, Alexander S."},{"first_name":"Bruno G.","last_name":"Frenguelli","full_name":"Frenguelli, Bruno G."}],"edition":"1","publication_status":"published","title":"The double-edged sword: Gaining Adenosine at the expense of ATP. How to balance the books","status":"public","publisher":"Springer","department":[{"_id":"HaJa"}],"editor":[{"first_name":"Susan","last_name":"Masino","full_name":"Masino, Susan"},{"full_name":"Boison, Detlev","first_name":"Detlev","last_name":"Boison"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"10896","year":"2012","acknowledgement":"We are grateful to Research into Ageing/Ageing UK and The Dunhill Trust for funding SzN’s graduate studies, and to Prof Nicholas Dale for his valuable input.","abstract":[{"lang":"eng","text":"Under physiological conditions the brain, via the purine salvage pathway, reuses the preformed purine bases hypoxanthine, derived from ATP degradation, and adenine (Ade), derived from polyamine synthesis, to restore its ATP pool. However, the massive degradation of ATP during ischemia, although providing valuable neuroprotective adenosine, results in the accumulation and loss of diffusible purine metabolites and thereby leads to a protracted reduction in the post-ischemic ATP pool size. In vivo, this may both limit the ability to deploy ATP-dependent reparative mechanisms and reduce the subsequent availability of adenosine, whilst in brain slices results in tissue with substantially lower levels of ATP than in vivo. In the present review, we describe the mechanisms by which brain tissue replenishes its ATP, how this can be improved with the clinically tolerated chemicals D-ribose and adenine, and the functional, and potential therapeutic, implications of doing so."}],"place":"New York","type":"book_chapter","language":[{"iso":"eng"}],"date_published":"2012-07-23T00:00:00Z","doi":"10.1007/978-1-4614-3903-5_6","quality_controlled":"1","page":"109-129","publication":"Adenosine","citation":{"ama":"zur Nedden S, Doney AS, Frenguelli BG. The double-edged sword: Gaining Adenosine at the expense of ATP. How to balance the books. In: Masino S, Boison D, eds. Adenosine. 1st ed. New York: Springer; 2012:109-129. doi:10.1007/978-1-4614-3903-5_6","ista":"zur Nedden S, Doney AS, Frenguelli BG. 2012.The double-edged sword: Gaining Adenosine at the expense of ATP. How to balance the books. In: Adenosine. , 109–129.","apa":"zur Nedden, S., Doney, A. S., & Frenguelli, B. G. (2012). The double-edged sword: Gaining Adenosine at the expense of ATP. How to balance the books. In S. Masino & D. Boison (Eds.), Adenosine (1st ed., pp. 109–129). New York: Springer. https://doi.org/10.1007/978-1-4614-3903-5_6","ieee":"S. zur Nedden, A. S. Doney, and B. G. Frenguelli, “The double-edged sword: Gaining Adenosine at the expense of ATP. How to balance the books,” in Adenosine, 1st ed., S. Masino and D. Boison, Eds. New York: Springer, 2012, pp. 109–129.","mla":"zur Nedden, Stephanie, et al. “The Double-Edged Sword: Gaining Adenosine at the Expense of ATP. How to Balance the Books.” Adenosine, edited by Susan Masino and Detlev Boison, 1st ed., Springer, 2012, pp. 109–29, doi:10.1007/978-1-4614-3903-5_6.","short":"S. zur Nedden, A.S. Doney, B.G. Frenguelli, in:, S. Masino, D. Boison (Eds.), Adenosine, 1st ed., Springer, New York, 2012, pp. 109–129.","chicago":"Nedden, Stephanie zur, Alexander S. Doney, and Bruno G. Frenguelli. “The Double-Edged Sword: Gaining Adenosine at the Expense of ATP. How to Balance the Books.” In Adenosine, edited by Susan Masino and Detlev Boison, 1st ed., 109–29. New York: Springer, 2012. https://doi.org/10.1007/978-1-4614-3903-5_6."},"day":"23","month":"07","publication_identifier":{"isbn":["9781461439028"],"eisbn":["9781461439035"]},"article_processing_charge":"No","scopus_import":"1"},{"date_published":"2011-03-08T00:00:00Z","publication":"Nature Communications","citation":{"ama":"Janovjak HL, Sandoz G, Isacoff E. Modern ionotropic glutamate receptor with a K+ selectivity signature sequence. Nature Communications. 2011;2(232):1-6. doi:10.1038/ncomms1231","ista":"Janovjak HL, Sandoz G, Isacoff E. 2011. Modern ionotropic glutamate receptor with a K+ selectivity signature sequence. Nature Communications. 2(232), 1–6.","ieee":"H. L. Janovjak, G. Sandoz, and E. Isacoff, “Modern ionotropic glutamate receptor with a K+ selectivity signature sequence,” Nature Communications, vol. 2, no. 232. Nature Publishing Group, pp. 1–6, 2011.","apa":"Janovjak, H. L., Sandoz, G., & Isacoff, E. (2011). Modern ionotropic glutamate receptor with a K+ selectivity signature sequence. Nature Communications. Nature Publishing Group. https://doi.org/10.1038/ncomms1231","mla":"Janovjak, Harald L., et al. “Modern Ionotropic Glutamate Receptor with a K+ Selectivity Signature Sequence.” Nature Communications, vol. 2, no. 232, Nature Publishing Group, 2011, pp. 1–6, doi:10.1038/ncomms1231.","short":"H.L. Janovjak, G. Sandoz, E. Isacoff, Nature Communications 2 (2011) 1–6.","chicago":"Janovjak, Harald L, Guillaume Sandoz, and Ehud Isacoff. “Modern Ionotropic Glutamate Receptor with a K+ Selectivity Signature Sequence.” Nature Communications. Nature Publishing Group, 2011. https://doi.org/10.1038/ncomms1231."},"page":"1 - 6","day":"08","has_accepted_license":"1","scopus_import":1,"pubrep_id":"832","file":[{"content_type":"application/pdf","file_size":387654,"creator":"system","access_level":"open_access","file_name":"IST-2017-832-v1+1_janovjak.pdf","checksum":"6b68d65aadd97c18d663eb117a0a9d35","date_created":"2018-12-12T10:11:36Z","date_updated":"2020-07-14T12:46:12Z","relation":"main_file","file_id":"4891"}],"oa_version":"Submitted Version","user_id":"4435EBFC-F248-11E8-B48F-1D18A9856A87","_id":"3405","ddc":["570","571"],"status":"public","title":"Modern ionotropic glutamate receptor with a K+ selectivity signature sequence","intvolume":" 2","abstract":[{"lang":"eng","text":"Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system and gates non-selective cation channels. The origins of glutamate receptors are not well understood as they differ structurally and functionally from simple bacterial ligand-gated ion channels. Here we report the discovery of an ionotropic glutamate receptor that combines the typical eukaryotic domain architecture with the 'TXVGYG' signature sequence of the selectivity filter found in K+ channels. This receptor exhibits functional properties intermediate between bacterial and eukaryotic glutamate-gated ion channels, suggesting a link in the evolution of ionotropic glutamate receptors."}],"issue":"232","type":"journal_article","doi":"10.1038/ncomms1231","language":[{"iso":"eng"}],"oa":1,"quality_controlled":"1","month":"03","author":[{"orcid":"0000-0002-8023-9315","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","last_name":"Janovjak","first_name":"Harald L","full_name":"Janovjak, Harald L"},{"last_name":"Sandoz","first_name":"Guillaume","full_name":"Sandoz, Guillaume"},{"first_name":"Ehud","last_name":"Isacoff","full_name":"Isacoff, Ehud"}],"date_created":"2018-12-11T12:03:09Z","date_updated":"2021-01-12T07:43:15Z","volume":2,"year":"2011","publication_status":"published","department":[{"_id":"HaJa"}],"publisher":"Nature Publishing Group","file_date_updated":"2020-07-14T12:46:12Z","publist_id":"2997"}]