Rauschendorfer, Theresa, et al. “Acute and Chronic Effects of a Light-Activated FGF Receptor in Keratinocytes in Vitro and in Mice.”10.26508/lsa.202101100__Life Science Alliance, vol. 4, no. 11, e202101100, Life Science Alliance, 2021, doi:10.26508/lsa.202101100.
LibreCat: https://research-explorer.ista.ac.at/record/10144
DOI: 10.26508/lsa.202101100
PMID: 34548382

Inglés Prieto, Álvaro, et al. “Optogenetic Delivery of Trophic Signals in a Genetic Model of Parkinson’s Disease.”10.1371/journal.pgen.1009479__PLoS Genetics, vol. 17, no. 4, Public Library of Science, 2021, p. e1009479, doi:10.1371/journal.pgen.1009479.
LibreCat: https://research-explorer.ista.ac.at/record/9363
DOI: 10.1371/journal.pgen.1009479
WoS: 000640606700001

Kainrath, Stephanie, and Harald L. Janovjak. “Design and Application of Light-Regulated Receptor Tyrosine Kinases.”10.1007/978-1-0716-0755-8_16__Photoswitching Proteins, edited by Dominik Niopek, vol. 2173, Springer Nature, 2020, pp. 233–46, doi:10.1007/978-1-0716-0755-8_16.
LibreCat: https://research-explorer.ista.ac.at/record/8173
DOI: 10.1007/978-1-0716-0755-8_16

Henneberger, Christian, et al. “LTP Induction Boosts Glutamate Spillover by Driving Withdrawal of Perisynaptic Astroglia.”10.1016/j.neuron.2020.08.030__Neuron, vol. 108, no. 5, Elsevier, 2020, p. 9–936., doi:10.1016/j.neuron.2020.08.030.
LibreCat: https://research-explorer.ista.ac.at/record/8674
DOI: 10.1016/j.neuron.2020.08.030
WoS: 000603428000010
PMID: 32976770

Capek, Daniel, et al. “Light-Activated Frizzled7 Reveals a Permissive Role of Non-Canonical Wnt Signaling in Mesendoderm Cell Migration.”10.7554/eLife.42093__ELife, vol. 8, e42093, eLife Sciences Publications, 2019, doi:10.7554/eLife.42093.
LibreCat: https://research-explorer.ista.ac.at/record/6025
DOI: 10.7554/eLife.42093
WoS: 000458025300001

Tichy, Alexandra-Madelaine, et al. “Engineering Strategy and Vector Library for the Rapid Generation of Modular Light-Controlled Protein–Protein Interactions.”10.1016/j.jmb.2019.05.033__Journal of Molecular Biology, vol. 431, no. 17, Elsevier, 2019, pp. 3046–55, doi:10.1016/j.jmb.2019.05.033.
LibreCat: https://research-explorer.ista.ac.at/record/6564
DOI: 10.1016/j.jmb.2019.05.033
WoS: 000482872100002

Mckenzie, Catherine, et al. “Isolation of Synaptic Vesicles from Genetically Engineered Cultured Neurons.”10.1016/j.jneumeth.2018.11.018__Journal of Neuroscience Methods, vol. 312, Elsevier, 2019, pp. 114–21, doi:10.1016/j.jneumeth.2018.11.018.
LibreCat: https://research-explorer.ista.ac.at/record/7406
DOI: 10.1016/j.jneumeth.2018.11.018
WoS: 000456220900013
PMID: 30496761

Zhang, William, et al. “Monitoring Hippocampal Glycine with the Computationally Designed Optical Sensor GlyFS.”10.1038/s41589-018-0108-2__Nature Chemical Biology, vol. 14, no. 9, Nature Publishing Group, 2018, pp. 861–69, doi:10.1038/s41589-018-0108-2.
LibreCat: https://research-explorer.ista.ac.at/record/137
DOI: 10.1038/s41589-018-0108-2
WoS: 000442174500013
PMID: 30061718 

Morri, Maurizio, et al. “Optical Functionalization of Human Class A Orphan G-Protein-Coupled Receptors.”10.1038/s41467-018-04342-1__Nature Communications, vol. 9, no. 1, 1950, Springer Nature, 2018, doi:10.1038/s41467-018-04342-1.
LibreCat: https://research-explorer.ista.ac.at/record/5984
DOI: 10.1038/s41467-018-04342-1
WoS: 000432280000006

Kainrath, Stephanie, et al. “Grünlicht-Induzierte Rezeptorinaktivierung Durch Cobalamin-Bindende Domänen.”10.1002/ange.201611998__Angewandte Chemie, vol. 129, no. 16, Wiley, 2017, pp. 4679–82, doi:10.1002/ange.201611998.
LibreCat: https://research-explorer.ista.ac.at/record/538
DOI: 10.1002/ange.201611998

Clifton, Ben, et al. “Ancestral Protein Reconstruction and Circular Permutation for Improving the Stability and Dynamic Range of FRET Sensors.”10.1007/978-1-4939-6940-1_5__Synthetic Protein Switches, edited by Viktor Stein, vol. 1596, Springer, 2017, pp. 71–87, doi:10.1007/978-1-4939-6940-1_5.
LibreCat: https://research-explorer.ista.ac.at/record/957
DOI: 10.1007/978-1-4939-6940-1_5

Mitchell, Joshua, et al. “Method for Developing Optical Sensors Using a Synthetic Dye Fluorescent Protein FRET Pair and Computational Modeling and Assessment.”10.1007/978-1-4939-6940-1_6__Synthetic Protein Switches, edited by Viktor Stein, vol. 1596, Springer, 2017, pp. 89–99, doi:10.1007/978-1-4939-6940-1_6.
LibreCat: https://research-explorer.ista.ac.at/record/958
DOI: 10.1007/978-1-4939-6940-1_6

Agus, Viviana, and Harald L. Janovjak. “Optogenetic Methods in Drug Screening: Technologies and Applications.”10.1016/j.copbio.2017.02.006__Current Opinion in Biotechnology, vol. 48, Elsevier, 2017, pp. 8–14, doi:10.1016/j.copbio.2017.02.006.
LibreCat: https://research-explorer.ista.ac.at/record/1026
DOI: 10.1016/j.copbio.2017.02.006
WoS: 000418313200003

Kainrath, Stephanie, et al. “Green-Light-Induced Inactivation of Receptor Signaling Using Cobalamin-Binding Domains.”10.1002/anie.201611998__Angewandte Chemie - International Edition, vol. 56, no. 16, Wiley-Blackwell, 2017, pp. 4608–11, doi:10.1002/anie.201611998.
LibreCat: https://research-explorer.ista.ac.at/record/1028
DOI: 10.1002/anie.201611998
WoS: 000398154000038

Janovjak, Harald L. “Light at the End of the Protein: Crystal Structure of a C-Terminal Light-Sensing Domain.”10.1016/j.str.2016.01.002__Structure, vol. 24, no. 2, Cell Press, 2016, pp. 213–15, doi:10.1016/j.str.2016.01.002.
LibreCat: https://research-explorer.ista.ac.at/record/1440
DOI: 10.1016/j.str.2016.01.002

Mitchell, Joshua, et al. “Rangefinder: A Semisynthetic FRET Sensor Design Algorithm.”10.1021/acssensors.6b00576__ACS SENSORS, vol. 1, no. 11, American Chemical Society, 2016, pp. 1286–90, doi:10.1021/acssensors.6b00576.
LibreCat: https://research-explorer.ista.ac.at/record/1101
DOI: 10.1021/acssensors.6b00576

Gschaider-Reichhart, Eva, et al. “A Phytochrome Sensory Domain Permits Receptor Activation by Red Light.”10.1002/anie.201601736__Angewandte Chemie - International Edition, vol. 55, no. 21, Wiley, 2016, pp. 6339–42, doi:10.1002/anie.201601736.
LibreCat: https://research-explorer.ista.ac.at/record/1441
DOI: 10.1002/anie.201601736

Sako, Keisuke, et al. “Optogenetic Control of Nodal Signaling Reveals a Temporal Pattern of Nodal Signaling Regulating Cell Fate Specification during Gastrulation.”10.1016/j.celrep.2016.06.036__Cell Reports, vol. 16, no. 3, Cell Press, 2016, pp. 866–77, doi:10.1016/j.celrep.2016.06.036.
LibreCat: https://research-explorer.ista.ac.at/record/1100
DOI: 10.1016/j.celrep.2016.06.036

Mckenzie, Catherine, et al. “Flipping the Photoswitch: Ion Channels under Light Control.”10.1007/978-1-4939-2845-3_6__Novel Chemical Tools to Study Ion Channel Biology, vol. 869, Springer, 2015, pp. 101–17, doi:10.1007/978-1-4939-2845-3_6.
LibreCat: https://research-explorer.ista.ac.at/record/1549
DOI: 10.1007/978-1-4939-2845-3_6

Whitfield, Jason, et al. “Construction of a Robust and Sensitive Arginine Biosensor through Ancestral Protein Reconstruction.”10.1002/pro.2721__Protein Science, vol. 24, no. 9, Wiley, 2015, pp. 1412–22, doi:10.1002/pro.2721.
LibreCat: https://research-explorer.ista.ac.at/record/1611
DOI: 10.1002/pro.2721
PMID: 26061224

Hühner, Jens, et al. “Quantification of Riboflavin, Flavin Mononucleotide, and Flavin Adenine Dinucleotide in Mammalian Model Cells by CE with LED-Induced Fluorescence Detection.”10.1002/elps.201400451__Electrophoresis, vol. 36, no. 4, Wiley, 2015, pp. 518–25, doi:10.1002/elps.201400451.
LibreCat: https://research-explorer.ista.ac.at/record/1867
DOI: 10.1002/elps.201400451

Inglés Prieto, Álvaro, et al. “Light-Assisted Small-Molecule Screening against Protein Kinases.”10.1038/nchembio.1933__Nature Chemical Biology, vol. 11, no. 12, Nature Publishing Group, 2015, pp. 952–54, doi:10.1038/nchembio.1933.
LibreCat: https://research-explorer.ista.ac.at/record/1678
DOI: 10.1038/nchembio.1933

Inglés Prieto, Álvaro, et al. “The Optogenetic Promise for Oncology: Episode I.”10.4161/23723548.2014.964045__Molecular and Cellular Oncology, vol. 1, no. 4, e964045, Taylor &; Francis, 2014, doi:10.4161/23723548.2014.964045.
LibreCat: https://research-explorer.ista.ac.at/record/2032
DOI: 10.4161/23723548.2014.964045

Grusch, Michael, et al. “Spatio-Temporally Precise Activation of Engineered Receptor Tyrosine Kinases by Light.”10.15252/embj.201387695__EMBO Journal, vol. 33, no. 15, Wiley-Blackwell, 2014, pp. 1713–26, doi:10.15252/embj.201387695.
LibreCat: https://research-explorer.ista.ac.at/record/2084
DOI: 10.15252/embj.201387695

Szobota, Stephanie, et al. “Optical Control of Ligand-Gated Ion Channels.”10.1007/978-1-62703-351-0_32__Methods in Molecular Biology, vol. 998, Springer, 2013, pp. 417–35, doi:10.1007/978-1-62703-351-0_32.
LibreCat: https://research-explorer.ista.ac.at/record/2857
DOI: 10.1007/978-1-62703-351-0_32

Levitz, Joshua, et al. “Optical Control of Metabotropic Glutamate Receptors.”10.1038/nn.3346__Nature Neuroscience, vol. 16, Nature Publishing Group, 2013, pp. 507–16, doi:10.1038/nn.3346.
LibreCat: https://research-explorer.ista.ac.at/record/2856
DOI: 10.1038/nn.3346
PMID: 23455609

Janovjak, Harald L., et al. “Modern Ionotropic Glutamate Receptor with a K+ Selectivity Signature Sequence.”10.1038/ncomms1231__Nature Communications, vol. 2, no. 232, Nature Publishing Group, 2011, pp. 1–6, doi:10.1038/ncomms1231.
LibreCat: https://research-explorer.ista.ac.at/record/3405
DOI: 10.1038/ncomms1231

Janovjak, Harald L., and Ehud Isacoff. “Structure-Based Design of Light-Controlled Proteins.”10.1007/978-1-61779-031-7_13__Photosensitive Molecules for the Control of Biological Function, vol. 55, Springer, 2011, pp. 233–66, doi:10.1007/978-1-61779-031-7_13.
LibreCat: https://research-explorer.ista.ac.at/record/3724
DOI: 10.1007/978-1-61779-031-7_13

Janovjak, Harald L., et al. “A Light-Gated, Potassium-Selective Glutamate Receptor for the Optical Inhibition of Neuronal Firing.”10.1038/nn.2589__Nature Neuroscience, vol. 13, Nature Publishing Group, 2010, pp. 1027–32, doi:10.1038/nn.2589.
LibreCat: https://research-explorer.ista.ac.at/record/3407
DOI: 10.1038/nn.2589

Stawski, Philipp, et al. “Pharmacology of Ionotropic Glutamate Receptors: A Structural Perspective.”10.1016/j.bmc.2010.09.012__Bioorganic and Medicinal Chemistry, vol. 18, no. 22, Elsevier, 2010, pp. 7759–72, doi:10.1016/j.bmc.2010.09.012.
LibreCat: https://research-explorer.ista.ac.at/record/3406
DOI: 10.1016/j.bmc.2010.09.012

Szymczak, Piotr, and Harald L. Janovjak. “Periodic Forces Trigger a Complex Mechanical Response in Ubiquitin.”10.1016/j.jmb.2009.04.071__Journal of Molecular Biology, vol. 390, no. 3, Elsevier, 2009, pp. 443–56, doi:10.1016/j.jmb.2009.04.071.
LibreCat: https://research-explorer.ista.ac.at/record/3408
DOI: 10.1016/j.jmb.2009.04.071

Janovjak, Harald L., et al. “From Valleys to Ridges: Exploring the Energy Landscape of Single Membrane Proteins.”10.1002/cphc.200700662__ChemPhysChem, vol. 9, no. 7, Wiley-Blackwell, 2008, pp. 954–66, doi:10.1002/cphc.200700662.
LibreCat: https://research-explorer.ista.ac.at/record/3410
DOI: 10.1002/cphc.200700662

Struckmeier, Jens, et al. “Fully Automated Single-Molecule Force Spectroscopy for Screening Applications.”10.1088/0957-4484/19/38/384020__Nanotechnology, vol. 19, no. 38, IOP Publishing Ltd., 2008, doi:10.1088/0957-4484/19/38/384020.
LibreCat: https://research-explorer.ista.ac.at/record/3409
DOI: 10.1088/0957-4484/19/38/384020

Engel, Andreas, et al. “Single-Molecule Microscopy and Force Spectroscopy of Membrane Proteins.”10.1007/978-3-540-73924-1_11__Single Molecules and Nanotechnology, vol. 12, Springer, 2008, pp. 279–311, doi:10.1007/978-3-540-73924-1_11.
LibreCat: https://research-explorer.ista.ac.at/record/3726
DOI: 10.1007/978-3-540-73924-1_11

Preiner, Johannes, et al. “Free Energy of Membrane Protein Unfolding Derived from Single-Molecule Force Measurements.”10.1529/biophysj.106.096982__Biophysical Journal, vol. 93, no. 3, Biophysical Society, 2007, pp. 930–37, doi:10.1529/biophysj.106.096982.
LibreCat: https://research-explorer.ista.ac.at/record/3411
DOI: 10.1529/biophysj.106.096982

Kedrov, Alexej, et al. “Deciphering Molecular Interactions of Native Membrane Proteins by Single-Molecule Force Spectroscopy.”10.1146/annurev.biophys.36.040306.132640__Annual Review of Biophysics, vol. 36, Annual Reviews, 2007, pp. 233–60, doi:10.1146/annurev.biophys.36.040306.132640.
LibreCat: https://research-explorer.ista.ac.at/record/3412
DOI: 10.1146/annurev.biophys.36.040306.132640

Bippes, Christian, et al. “Digital Force-Feedback for Protein Unfolding Experiments Using Atomic Force Microscopy.”10.1088/0957-4484/18/4/044022__Nanotechnology, vol. 18, no. 4, IOP Publishing Ltd., 2007, doi:10.1088/0957-4484/18/4/044022.
LibreCat: https://research-explorer.ista.ac.at/record/3727
DOI: 10.1088/0957-4484/18/4/044022

Janovjak, Harald L., et al. “Transmembrane Helices Have Rough Energy Surfaces.”10.1021/ja065684a__Journal of the American Chemical Society, vol. 129, no. 2, ACS, 2007, pp. 246–47, doi:10.1021/ja065684a.
LibreCat: https://research-explorer.ista.ac.at/record/3723
DOI: 10.1021/ja065684a

Janovjak, Harald L., et al. “Atomic Force Microscopy.” Techniques in Microscopy for Biomedical Applications, vol. 2, World Scientific Publishing, 2006, pp. 213–84.
LibreCat: https://research-explorer.ista.ac.at/record/3404

Kessler, Max, et al. “Bacteriorhodopsin Folds into the Membrane against an External Force.”10.1016/j.jmb.2005.12.065__Journal of Molecular Biology, vol. 357, no. 2, Elsevier, 2006, pp. 644–54, doi:10.1016/j.jmb.2005.12.065.
LibreCat: https://research-explorer.ista.ac.at/record/3413
DOI: 10.1016/j.jmb.2005.12.065

Kedrov, Alexej, et al. “Observing Folding Pathways and Kinetics of a Single Sodium-Proton Antiporter from Escherichia Coli.”10.1016/j.jmb.2005.10.028__Journal of Molecular Biology, vol. 355, no. 1, Elsevier, 2006, pp. 2–8, doi:10.1016/j.jmb.2005.10.028.
LibreCat: https://research-explorer.ista.ac.at/record/3414
DOI: 10.1016/j.jmb.2005.10.028

Janovjak, Harald L., et al. “Imaging and Detecting Molecular Interactions of Single Membrane Proteins.”10.1016/j.neurobiolaging.2005.03.031__Neurobiology of Aging, vol. 27, Elsevier, 2006, pp. 546–61, doi:10.1016/j.neurobiolaging.2005.03.031.
LibreCat: https://research-explorer.ista.ac.at/record/3415
DOI: 10.1016/j.neurobiolaging.2005.03.031

Bippes, Christian, et al. “Direct Measurement of Single-Molecule Visco-Elasticity in Atomic Force Microscope Force-Extension Experiments.”10.1007/s00249-005-0023-9__European Biophysics Journal, vol. 35, no. 3, Springer, 2006, pp. 287–92, doi:10.1007/s00249-005-0023-9.
LibreCat: https://research-explorer.ista.ac.at/record/3729
DOI: 10.1007/s00249-005-0023-9

Cieplak, Marek, et al. “Pulling Single Bacteriorhodopsin out of a Membrane: Comparison of Simulation and Experiment.”10.1016/j.bbamem.2006.03.028__Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 1758, no. 4, Elsevier, 2006, pp. 537–44, doi:10.1016/j.bbamem.2006.03.028.
LibreCat: https://research-explorer.ista.ac.at/record/3728
DOI: 10.1016/j.bbamem.2006.03.028

Janovjak, Harald L., and Daniel Mueller. “Rastersondenmikroskopie.” Bioanalytik, Spektrum Akademischer Verlag, 2006.
LibreCat: https://research-explorer.ista.ac.at/record/3722

Kuhn, Michael, et al. “Automated Alignment and Pattern Recognition of Single-Molecule Force Spectroscopy Data.”10.1111/j.1365-2818.2005.01478.x__Journal of Microscopy, vol. 218, no. 2, Wiley-Blackwell, 2005, pp. 125–32, doi:10.1111/j.1365-2818.2005.01478.x.
LibreCat: https://research-explorer.ista.ac.at/record/3417
DOI: 10.1111/j.1365-2818.2005.01478.x

Janovjak, Harald L., et al. “Complex Stability of Single Proteins Explored by Forced Unfolding Experiments.”10.1529/biophysj.105.059774__Biophysical Journal, vol. 88, no. 5, Biophysical Society, 2005, pp. 37–39, doi:10.1529/biophysj.105.059774.
LibreCat: https://research-explorer.ista.ac.at/record/3416
DOI: 10.1529/biophysj.105.059774

Janovjak, Harald L., et al. “Hydrodynamic Effects in Fast AFM Single Molecule Force Measurements.”10.1007/s00249-004-0430-3__European Biophysics Journal, vol. 34, no. 1, Springer, 2005, pp. 91–96, doi:10.1007/s00249-004-0430-3.
LibreCat: https://research-explorer.ista.ac.at/record/3418
DOI: 10.1007/s00249-004-0430-3

Janovjak, Harald L., et al. “Molecular Force Modulation Spectroscopy Revealing the Dynamic Response of Single Bacteriorhodopsins.”10.1529/biophysj.104.052746__Biophysical Journal, vol. 88, no. 2, Biophysical Society, 2005, pp. 1423–31, doi:10.1529/biophysj.104.052746.
LibreCat: https://research-explorer.ista.ac.at/record/3721
DOI: 10.1529/biophysj.104.052746

Kedrov, Alexej, et al. “Controlled Unfolding and Refolding of a Single Sodium/Proton Antiporter Using Atomic Force Microscopy.”10.1016/j.jmb.2004.05.026__Journal of Molecular Biology, vol. 340, no. 5, Elsevier, 2004, pp. 1143–52, doi:10.1016/j.jmb.2004.05.026.
LibreCat: https://research-explorer.ista.ac.at/record/3420
DOI: 10.1016/j.jmb.2004.05.026

Janovjak, Harald L., et al. “Probing the Energy Landscape of the Membrane Protein Bacteriorhodopsin.”10.1016/j.str.2004.03.016__Structure, vol. 12, no. 5, Cell Press, 2004, pp. 871–79, doi:10.1016/j.str.2004.03.016.
LibreCat: https://research-explorer.ista.ac.at/record/3419
DOI: 10.1016/j.str.2004.03.016

Janovjak, Harald L., et al. “Unfolding Pathways of Native Bacteriorhodopsin Depend on Temperature.”10.1093/emboj/cdg509__EMBO Journal, vol. 22, no. 19, Wiley-Blackwell, 2003, pp. 5220–29, doi:10.1093/emboj/cdg509.
LibreCat: https://research-explorer.ista.ac.at/record/3725
DOI: 10.1093/emboj/cdg509

Mueller, Daniel, et al. “Observing Structure, Function and Assembly of Single Proteins by AFM.”10.1016/S0079-6107(02)00009-3__Progress in Biophysics and Molecular Biology, vol. 79, no. 1–3, Elsevier, 2002, pp. 1–43, doi:10.1016/S0079-6107(02)00009-3.
LibreCat: https://research-explorer.ista.ac.at/record/3421
DOI: 10.1016/S0079-6107(02)00009-3
PMID: 12225775

Müller, Patrick, et al. “Processing of Gene Expression Data Generated by Quantitative Real-Time RT-PCR.” Biotechniques, vol. 32, no. 6, Informa Healthcare, 2002, pp. 1372–79.
LibreCat: https://research-explorer.ista.ac.at/record/3422
PMID: 12074169