49 Publications

Mark all

[49]
2019 | Journal Article | IST-REx-ID: 6025   OA
Capek, D., Smutny, M., Tichy, A. M., Morri, M., Janovjak, H. L., & Heisenberg, C.-P. J. (2019). Light-activated Frizzled7 reveals a permissive role of non-canonical wnt signaling in mesendoderm cell migration. ELife, 8. https://doi.org/10.7554/eLife.42093
View | Files available | DOI
 
[48]
2019 | Journal Article | IST-REx-ID: 6564   OA
Tichy, A.-M., Gerrard, E. J., Legrand, J. M. D., Hobbs, R. M., & Janovjak, H. L. (2019). Engineering strategy and vector library for the rapid generation of modular light-controlled protein–protein interactions. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2019.05.033
View | DOI | Download (ext.)
 
[47]
2018 | Journal Article | IST-REx-ID: 137   OA
Zhang, W., Herde, M., Mitchell, J., Whitfield, J., Wulff, A., Vongsouthi, V., … Henneberger, C. (2018). Monitoring hippocampal glycine with the computationally designed optical sensor GlyFS. Nature Chemical Biology, 14(9), 861–869. https://doi.org/10.1038/s41589-018-0108-2
View | DOI | Download (ext.) | PubMed | Europe PMC
 
[46]
2018 | Journal Article | IST-REx-ID: 5984   OA
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. Nature Communications, 9(1). https://doi.org/10.1038/s41467-018-04342-1
View | Files available | DOI
 
[45]
2017 | Book Chapter | IST-REx-ID: 958
Mitchell, J., Zhang, W., Herde, M., Henneberger, C., Janovjak, H. L., O’Mara, M., & Jackson, C. (2017). Method for developing optical sensors using a synthetic dye fluorescent protein FRET pair and computational modeling and assessment. In V. Stein (Ed.), Synthetic Protein Switches (Vol. 1596, pp. 89–99). Springer. https://doi.org/10.1007/978-1-4939-6940-1_6
View | DOI
 
[44]
2017 | Journal Article | IST-REx-ID: 1028   OA
Kainrath, S., Stadler, M., Gschaider-Reichhart, E., Distel, M., & Janovjak, H. L. (2017). Green-light-induced inactivation of receptor signaling using cobalamin-binding domains. Angewandte Chemie - International Edition, 56(16), 4608–4611. https://doi.org/10.1002/anie.201611998
View | Files available | DOI
 
[43]
2017 | Journal Article | IST-REx-ID: 538   OA
Kainrath, S., Stadler, M., Gschaider-Reichhart, E., Distel, M., & Janovjak, H. L. (2017). Grünlicht-induzierte Rezeptorinaktivierung durch Cobalamin-bindende Domänen. Angewandte Chemie, 129(16), 4679–4682. https://doi.org/10.1002/ange.201611998
View | Files available | DOI
 
[42]
2017 | Journal Article | IST-REx-ID: 1026
Agus, V., & Janovjak, H. L. (2017). Optogenetic methods in drug screening: Technologies and applications. Current Opinion in Biotechnology, 48, 8–14. https://doi.org/10.1016/j.copbio.2017.02.006
View | DOI
 
[41]
2017 | Book Chapter | IST-REx-ID: 957
Clifton, B., Whitfield, J., Sanchez Romero, I., Herde, M., Henneberger, C., Janovjak, H. L., & Jackson, C. (2017). Ancestral protein reconstruction and circular permutation for improving the stability and dynamic range of FRET sensors. In V. Stein (Ed.), Synthetic Protein Switches (Vol. 1596, pp. 71–87). Springer. https://doi.org/10.1007/978-1-4939-6940-1_5
View | DOI
 
[40]
2016 | Journal Article | IST-REx-ID: 1440
Janovjak, H. L. (2016). Light at the end of the protein: Crystal structure of a C-terminal light-sensing domain. Structure, 24(2), 213–215. https://doi.org/10.1016/j.str.2016.01.002
View | DOI
 
[39]
2016 | Journal Article | IST-REx-ID: 1441
Gschaider-Reichhart, E., Inglés Prieto, Á., Tichy, A.-M., Mckenzie, C., & Janovjak, H. L. (2016). A phytochrome sensory domain permits receptor activation by red light. Angewandte Chemie - International Edition, 55(21), 6339–6342. https://doi.org/10.1002/anie.201601736
View | Files available | DOI
 
[38]
2016 | Journal Article | IST-REx-ID: 1100
Sako, K., Pradhan, S., Barone, V., Inglés Prieto, Á., Mueller, P., Ruprecht, V., … Heisenberg, C.-P. J. (2016). Optogenetic control of nodal signaling reveals a temporal pattern of nodal signaling regulating cell fate specification during gastrulation. Cell Reports, 16(3), 866–877. https://doi.org/10.1016/j.celrep.2016.06.036
View | Files available | DOI
 
[37]
2016 | Journal Article | IST-REx-ID: 1101
Mitchell, J., Whitfield, J., Zhang, W., Henneberger, C., Janovjak, H. L., O’Mara, M., & Jackson, C. (2016). Rangefinder: A semisynthetic FRET sensor design algorithm. ACS SENSORS, 1(11), 1286–1290. https://doi.org/10.1021/acssensors.6b00576
View | DOI
 
[36]
2015 | Journal Article | IST-REx-ID: 1611   OA
Whitfield, J., Zhang, W., Herde, M., Clifton, B., Radziejewski, J., Janovjak, H. L., … Jackson, C. (2015). Construction of a robust and sensitive arginine biosensor through ancestral protein reconstruction. Protein Science, 24(9), 1412–1422. https://doi.org/10.1002/pro.2721
View | DOI | Download (ext.) | PubMed | Europe PMC
 
[35]
2015 | Journal Article | IST-REx-ID: 1678
Inglés Prieto, Á., Gschaider-Reichhart, E., Muellner, M., Nowak, M., Nijman, S., Grusch, M., & Janovjak, H. L. (2015). Light-assisted small-molecule screening against protein kinases. Nature Chemical Biology, 11(12), 952–954. https://doi.org/10.1038/nchembio.1933
View | Files available | DOI
 
[34]
2015 | Book Chapter | IST-REx-ID: 1549   OA
Mckenzie, C., Sanchez Romero, I., & Janovjak, H. L. (2015). Flipping the photoswitch: Ion channels under light control. In Novel chemical tools to study ion channel biology (Vol. 869, pp. 101–117). Springer. https://doi.org/10.1007/978-1-4939-2845-3_6
View | Files available | DOI
 
[33]
2015 | Journal Article | IST-REx-ID: 1867
Hühner, J., Inglés Prieto, Á., Neusüß, C., Lämmerhofer, M., & Janovjak, H. L. (2015). Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence detection. Electrophoresis, 36(4), 518–525. https://doi.org/10.1002/elps.201400451
View | DOI
 
[32]
2014 | Journal Article | IST-REx-ID: 2032   OA
Inglés Prieto, Á., Gschaider-Reichhart, E., Schelch, K., Janovjak, H. L., & Grusch, M. (2014). The optogenetic promise for oncology: Episode I. Molecular and Cellular Oncology, 1(4), e964045. https://doi.org/10.4161/23723548.2014.964045
View | Files available | DOI
 
[31]
2014 | Journal Article | IST-REx-ID: 2084
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, 33(15), 1713–1726. https://doi.org/10.15252/embj.201387695
View | Files available | DOI | Download (ext.)
 
[30]
2013 | Journal Article | IST-REx-ID: 2856   OA
Levitz, J., Pantoja, C., Gaub, B., Janovjak, H. L., Reiner, A., Hoagland, A., … Isacoff, E. (2013). Optical control of metabotropic glutamate receptors. Nature Neuroscience, 16, 507–516. https://doi.org/10.1038/nn.3346
View | DOI | Download (ext.) | PubMed | Europe PMC
 
[29]
2013 | Journal Article | IST-REx-ID: 2857   OA
Szobota, S., Mckenzie, C., & Janovjak, H. L. (2013). Optical control of ligand-gated ion channels. Methods in Molecular Biology, 998, 417–435. https://doi.org/10.1007/978-1-62703-351-0_32
View | Files available | DOI
 
[28]
2011 | Journal Article | IST-REx-ID: 3405   OA
Janovjak, H. L., Sandoz, G., & Isacoff, E. (2011). Modern ionotropic glutamate receptor with a K+ selectivity signature sequence. Nature Communications, 2(232), 1–6. https://doi.org/10.1038/ncomms1231
View | Files available | DOI
 
[27]
2011 | Book Chapter | IST-REx-ID: 3724
Janovjak, H. L., & Isacoff, E. (2011). Structure-based design of light-controlled proteins. In Photosensitive Molecules for the Control of Biological Function (Vol. 55, pp. 233–266). Springer. https://doi.org/10.1007/978-1-61779-031-7_13
View | DOI
 
[26]
2010 | Book Review | IST-REx-ID: 3406
Stawski, P., Janovjak, H. L., & Trauner, D. (2010). Pharmacology of ionotropic glutamate receptors: a structural perspective. Bioorganic and Medicinal Chemistry. Elsevier. https://doi.org/10.1016/j.bmc.2010.09.012
View | DOI
 
[25]
2010 | Journal Article | IST-REx-ID: 3407
Janovjak, H. L., Szobota, S., Wyart, C., Trauner, D., & Isacoff, E. (2010). A light-gated, potassium-selective glutamate receptor for the optical inhibition of neuronal firing. Nature Neuroscience, 13, 1027–1032. https://doi.org/10.1038/nn.2589
View | DOI
 
[24]
2009 | Journal Article | IST-REx-ID: 3408
Szymczak, P., & Janovjak, H. L. (2009). Periodic forces trigger a complex mechanical response in ubiquitin. Journal of Molecular Biology, 390(3), 443–456. https://doi.org/10.1016/j.jmb.2009.04.071
View | DOI
 
[23]
2008 | Book Review | IST-REx-ID: 3410
Janovjak, H. L., Sapra, T., Kedrov, A., & Mueller, D. (2008). From valleys to ridges: Exploring the energy landscape of single membrane proteins. ChemPhysChem. Wiley-Blackwell. https://doi.org/10.1002/cphc.200700662
View | DOI
 
[22]
2008 | Book Chapter | IST-REx-ID: 3726
Engel, A., Janovjak, H. L., Fotiadis, D., Kedrov, A., Cisneros, D., & Mueller, D. (2008). Single-molecule microscopy and force spectroscopy of membrane proteins. In Single Molecules and Nanotechnology (Vol. 12, pp. 279–311). Springer. https://doi.org/10.1007/978-3-540-73924-1_11
View | DOI
 
[21]
2008 | Journal Article | IST-REx-ID: 3409
Struckmeier, J., Wahl, R., Leuschner, M., Nunes, J., Janovjak, H. L., Geisler, U., … Mueller, D. (2008). Fully automated single-molecule force spectroscopy for screening applications. Nanotechnology, 19(38). https://doi.org/10.1088/0957-4484/19/38/384020
View | DOI
 
[20]
2007 | Journal Article | IST-REx-ID: 3411   OA
Preiner, J., Janovjak, H. L., Rankl, C., Knaus, H., Cisneros, D., Kedrov, A., … Hinterdorfer, P. (2007). Free energy of membrane protein unfolding derived from single-molecule force measurements. Biophysical Journal, 93(3), 930–937. https://doi.org/10.1529/biophysj.106.096982
View | DOI | Download (ext.)
 
[19]
2007 | Book Review | IST-REx-ID: 3412
Kedrov, A., Janovjak, H. L., Sapra, T., & Mueller, D. (2007). Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy. Annual Review of Biophysics. Annual Reviews. https://doi.org/10.1146/annurev.biophys.36.040306.132640
View | DOI
 
[18]
2007 | Journal Article | IST-REx-ID: 3727
Bippes, C., Janovjak, H. L., Kedrov, A., & Mueller, D. (2007). Digital force-feedback for protein unfolding experiments using atomic force microscopy. Nanotechnology, 18(4). https://doi.org/10.1088/0957-4484/18/4/044022
View | DOI
 
[17]
2007 | Journal Article | IST-REx-ID: 3723
Janovjak, H. L., Knaus, H., & Mueller, D. (2007). Transmembrane helices have rough energy surfaces. Journal of the American Chemical Society, 129(2), 246–247. https://doi.org/10.1021/ja065684a
View | DOI
 
[16]
2006 | Book Review | IST-REx-ID: 3415
Janovjak, H. L., Kedrov, A., Cisneros, D., Sapra, T., Struckmeier, J., & Mueller, D. (2006). Imaging and detecting molecular interactions of single membrane proteins. Neurobiology of Aging. Elsevier. https://doi.org/10.1016/j.neurobiolaging.2005.03.031
View | DOI
 
[15]
2006 | Book Chapter | IST-REx-ID: 3404
Janovjak, H. L., Sawhney, R., Stark, M., & Mueller, D. (2006). Atomic force microscopy. In Techniques in Microscopy for Biomedical Applications (Vol. 2, pp. 213–284). World Scientific Publishing.
View
 
[14]
2006 | Book Chapter | IST-REx-ID: 3722
Janovjak, H. L., & Mueller, D. (2006). Rastersondenmikroskopie. In Bioanalytik. Spektrum Akademischer Verlag.
View
 
[13]
2006 | Journal Article | IST-REx-ID: 3728
Cieplak, M., Filipek, S., Janovjak, H. L., & Krzysko, K. (2006). Pulling single bacteriorhodopsin out of a membrane: Comparison of simulation and experiment. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1758(4), 537–544. https://doi.org/10.1016/j.bbamem.2006.03.028
View | DOI
 
[12]
2006 | Journal Article | IST-REx-ID: 3413
Kessler, M., Gottschalk, K., Janovjak, H. L., Mueller, D., & Gaub, H. (2006). Bacteriorhodopsin folds into the membrane against an external force. Journal of Molecular Biology, 357(2), 644–654. https://doi.org/10.1016/j.jmb.2005.12.065
View | DOI
 
[11]
2006 | Journal Article | IST-REx-ID: 3414
Kedrov, A., Janovjak, H. L., Ziegler, C., Kühlbrandt, W., & Mueller, D. (2006). Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli. Journal of Molecular Biology, 355(1), 2–8. https://doi.org/10.1016/j.jmb.2005.10.028
View | DOI
 
[10]
2006 | Journal Article | IST-REx-ID: 3729
Bippes, C., Humphris, A., Stark, M., Mueller, D., & Janovjak, H. L. (2006). Direct measurement of single-molecule visco-elasticity in atomic force microscope force-extension experiments. European Biophysics Journal, 35(3), 287–292. https://doi.org/10.1007/s00249-005-0023-9
View | DOI
 
[9]
2005 | Journal Article | IST-REx-ID: 3721   OA
Janovjak, H. L., Mueller, D., & Humphris, A. (2005). Molecular force modulation spectroscopy revealing the dynamic response of single bacteriorhodopsins. Biophysical Journal, 88(2), 1423–1431. https://doi.org/10.1529/biophysj.104.052746
View | DOI | Download (ext.)
 
[8]
2005 | Journal Article | IST-REx-ID: 3416   OA
Janovjak, H. L., Sapra, T., & Mueller, D. (2005). Complex stability of single proteins explored by forced unfolding experiments. Biophysical Journal, 88(5), 37–39. https://doi.org/10.1529/biophysj.105.059774
View | DOI | Download (ext.)
 
[7]
2005 | Journal Article | IST-REx-ID: 3417
Kuhn, M., Janovjak, H. L., Hubain, M., & Mueller, D. (2005). Automated alignment and pattern recognition of single-molecule force spectroscopy data. Journal of Microscopy, 218(2), 125–132. https://doi.org/10.1111/j.1365-2818.2005.01478.x
View | DOI
 
[6]
2005 | Journal Article | IST-REx-ID: 3418
Janovjak, H. L., Struckmeier, J., & Mueller, D. (2005). Hydrodynamic effects in fast AFM single molecule force measurements. European Biophysics Journal, 34(1), 91–96. https://doi.org/10.1007/s00249-004-0430-3
View | DOI
 
[5]
2004 | Journal Article | IST-REx-ID: 3420
Kedrov, A., Ziegler, C., Janovjak, H. L., Kühlbrandt, W., & Mueller, D. (2004). Controlled unfolding and refolding of a single sodium/proton antiporter using atomic force microscopy. Journal of Molecular Biology, 340(5), 1143–1152. https://doi.org/10.1016/j.jmb.2004.05.026
View | DOI
 
[4]
2004 | Journal Article | IST-REx-ID: 3419
Janovjak, H. L., Struckmeier, J., Hubain, M., Kessler, M., Kedrov, A., & Mueller, D. (2004). Probing the energy landscape of the membrane protein bacteriorhodopsin. Structure, 12(5), 871–879. https://doi.org/10.1016/j.str.2004.03.016
View | DOI
 
[3]
2003 | Journal Article | IST-REx-ID: 3725   OA
Janovjak, H. L., Kessler, M., Oesterhelt, D., Gaub, H., & Mueller, D. (2003). Unfolding pathways of native bacteriorhodopsin depend on temperature. EMBO Journal, 22(19), 5220–5229. https://doi.org/10.1093/emboj/cdg509
View | DOI | Download (ext.)
 
[2]
2002 | Journal Article | IST-REx-ID: 3422
Müller, P., Janovjak, H. L., Miserez, A., & Dobbie, Z. (2002). Processing of gene expression data generated by quantitative real-time RT-PCR. Biotechniques, 32(6), 1372–1379.
View
 
[1]
2002 | Book Review | IST-REx-ID: 3421
Mueller, D., Janovjak, H. L., Lehto, T., Kuerschner, L., & Anderson, K. (2002). Observing structure, function and assembly of single proteins by AFM. Progress in Biophysics and Molecular Biology. Elsevier. https://doi.org/10.1016/S0079-6107(02)00009-3
View | DOI
 

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49 Publications

Mark all

[49]
2019 | Journal Article | IST-REx-ID: 6025   OA
Capek, D., Smutny, M., Tichy, A. M., Morri, M., Janovjak, H. L., & Heisenberg, C.-P. J. (2019). Light-activated Frizzled7 reveals a permissive role of non-canonical wnt signaling in mesendoderm cell migration. ELife, 8. https://doi.org/10.7554/eLife.42093
View | Files available | DOI
 
[48]
2019 | Journal Article | IST-REx-ID: 6564   OA
Tichy, A.-M., Gerrard, E. J., Legrand, J. M. D., Hobbs, R. M., & Janovjak, H. L. (2019). Engineering strategy and vector library for the rapid generation of modular light-controlled protein–protein interactions. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2019.05.033
View | DOI | Download (ext.)
 
[47]
2018 | Journal Article | IST-REx-ID: 137   OA
Zhang, W., Herde, M., Mitchell, J., Whitfield, J., Wulff, A., Vongsouthi, V., … Henneberger, C. (2018). Monitoring hippocampal glycine with the computationally designed optical sensor GlyFS. Nature Chemical Biology, 14(9), 861–869. https://doi.org/10.1038/s41589-018-0108-2
View | DOI | Download (ext.) | PubMed | Europe PMC
 
[46]
2018 | Journal Article | IST-REx-ID: 5984   OA
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. Nature Communications, 9(1). https://doi.org/10.1038/s41467-018-04342-1
View | Files available | DOI
 
[45]
2017 | Book Chapter | IST-REx-ID: 958
Mitchell, J., Zhang, W., Herde, M., Henneberger, C., Janovjak, H. L., O’Mara, M., & Jackson, C. (2017). Method for developing optical sensors using a synthetic dye fluorescent protein FRET pair and computational modeling and assessment. In V. Stein (Ed.), Synthetic Protein Switches (Vol. 1596, pp. 89–99). Springer. https://doi.org/10.1007/978-1-4939-6940-1_6
View | DOI
 
[44]
2017 | Journal Article | IST-REx-ID: 1028   OA
Kainrath, S., Stadler, M., Gschaider-Reichhart, E., Distel, M., & Janovjak, H. L. (2017). Green-light-induced inactivation of receptor signaling using cobalamin-binding domains. Angewandte Chemie - International Edition, 56(16), 4608–4611. https://doi.org/10.1002/anie.201611998
View | Files available | DOI
 
[43]
2017 | Journal Article | IST-REx-ID: 538   OA
Kainrath, S., Stadler, M., Gschaider-Reichhart, E., Distel, M., & Janovjak, H. L. (2017). Grünlicht-induzierte Rezeptorinaktivierung durch Cobalamin-bindende Domänen. Angewandte Chemie, 129(16), 4679–4682. https://doi.org/10.1002/ange.201611998
View | Files available | DOI
 
[42]
2017 | Journal Article | IST-REx-ID: 1026
Agus, V., & Janovjak, H. L. (2017). Optogenetic methods in drug screening: Technologies and applications. Current Opinion in Biotechnology, 48, 8–14. https://doi.org/10.1016/j.copbio.2017.02.006
View | DOI
 
[41]
2017 | Book Chapter | IST-REx-ID: 957
Clifton, B., Whitfield, J., Sanchez Romero, I., Herde, M., Henneberger, C., Janovjak, H. L., & Jackson, C. (2017). Ancestral protein reconstruction and circular permutation for improving the stability and dynamic range of FRET sensors. In V. Stein (Ed.), Synthetic Protein Switches (Vol. 1596, pp. 71–87). Springer. https://doi.org/10.1007/978-1-4939-6940-1_5
View | DOI
 
[40]
2016 | Journal Article | IST-REx-ID: 1440
Janovjak, H. L. (2016). Light at the end of the protein: Crystal structure of a C-terminal light-sensing domain. Structure, 24(2), 213–215. https://doi.org/10.1016/j.str.2016.01.002
View | DOI
 
[39]
2016 | Journal Article | IST-REx-ID: 1441
Gschaider-Reichhart, E., Inglés Prieto, Á., Tichy, A.-M., Mckenzie, C., & Janovjak, H. L. (2016). A phytochrome sensory domain permits receptor activation by red light. Angewandte Chemie - International Edition, 55(21), 6339–6342. https://doi.org/10.1002/anie.201601736
View | Files available | DOI
 
[38]
2016 | Journal Article | IST-REx-ID: 1100
Sako, K., Pradhan, S., Barone, V., Inglés Prieto, Á., Mueller, P., Ruprecht, V., … Heisenberg, C.-P. J. (2016). Optogenetic control of nodal signaling reveals a temporal pattern of nodal signaling regulating cell fate specification during gastrulation. Cell Reports, 16(3), 866–877. https://doi.org/10.1016/j.celrep.2016.06.036
View | Files available | DOI
 
[37]
2016 | Journal Article | IST-REx-ID: 1101
Mitchell, J., Whitfield, J., Zhang, W., Henneberger, C., Janovjak, H. L., O’Mara, M., & Jackson, C. (2016). Rangefinder: A semisynthetic FRET sensor design algorithm. ACS SENSORS, 1(11), 1286–1290. https://doi.org/10.1021/acssensors.6b00576
View | DOI
 
[36]
2015 | Journal Article | IST-REx-ID: 1611   OA
Whitfield, J., Zhang, W., Herde, M., Clifton, B., Radziejewski, J., Janovjak, H. L., … Jackson, C. (2015). Construction of a robust and sensitive arginine biosensor through ancestral protein reconstruction. Protein Science, 24(9), 1412–1422. https://doi.org/10.1002/pro.2721
View | DOI | Download (ext.) | PubMed | Europe PMC
 
[35]
2015 | Journal Article | IST-REx-ID: 1678
Inglés Prieto, Á., Gschaider-Reichhart, E., Muellner, M., Nowak, M., Nijman, S., Grusch, M., & Janovjak, H. L. (2015). Light-assisted small-molecule screening against protein kinases. Nature Chemical Biology, 11(12), 952–954. https://doi.org/10.1038/nchembio.1933
View | Files available | DOI
 
[34]
2015 | Book Chapter | IST-REx-ID: 1549   OA
Mckenzie, C., Sanchez Romero, I., & Janovjak, H. L. (2015). Flipping the photoswitch: Ion channels under light control. In Novel chemical tools to study ion channel biology (Vol. 869, pp. 101–117). Springer. https://doi.org/10.1007/978-1-4939-2845-3_6
View | Files available | DOI
 
[33]
2015 | Journal Article | IST-REx-ID: 1867
Hühner, J., Inglés Prieto, Á., Neusüß, C., Lämmerhofer, M., & Janovjak, H. L. (2015). Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence detection. Electrophoresis, 36(4), 518–525. https://doi.org/10.1002/elps.201400451
View | DOI
 
[32]
2014 | Journal Article | IST-REx-ID: 2032   OA
Inglés Prieto, Á., Gschaider-Reichhart, E., Schelch, K., Janovjak, H. L., & Grusch, M. (2014). The optogenetic promise for oncology: Episode I. Molecular and Cellular Oncology, 1(4), e964045. https://doi.org/10.4161/23723548.2014.964045
View | Files available | DOI
 
[31]
2014 | Journal Article | IST-REx-ID: 2084
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, 33(15), 1713–1726. https://doi.org/10.15252/embj.201387695
View | Files available | DOI | Download (ext.)
 
[30]
2013 | Journal Article | IST-REx-ID: 2856   OA
Levitz, J., Pantoja, C., Gaub, B., Janovjak, H. L., Reiner, A., Hoagland, A., … Isacoff, E. (2013). Optical control of metabotropic glutamate receptors. Nature Neuroscience, 16, 507–516. https://doi.org/10.1038/nn.3346
View | DOI | Download (ext.) | PubMed | Europe PMC
 
[29]
2013 | Journal Article | IST-REx-ID: 2857   OA
Szobota, S., Mckenzie, C., & Janovjak, H. L. (2013). Optical control of ligand-gated ion channels. Methods in Molecular Biology, 998, 417–435. https://doi.org/10.1007/978-1-62703-351-0_32
View | Files available | DOI
 
[28]
2011 | Journal Article | IST-REx-ID: 3405   OA
Janovjak, H. L., Sandoz, G., & Isacoff, E. (2011). Modern ionotropic glutamate receptor with a K+ selectivity signature sequence. Nature Communications, 2(232), 1–6. https://doi.org/10.1038/ncomms1231
View | Files available | DOI
 
[27]
2011 | Book Chapter | IST-REx-ID: 3724
Janovjak, H. L., & Isacoff, E. (2011). Structure-based design of light-controlled proteins. In Photosensitive Molecules for the Control of Biological Function (Vol. 55, pp. 233–266). Springer. https://doi.org/10.1007/978-1-61779-031-7_13
View | DOI
 
[26]
2010 | Book Review | IST-REx-ID: 3406
Stawski, P., Janovjak, H. L., & Trauner, D. (2010). Pharmacology of ionotropic glutamate receptors: a structural perspective. Bioorganic and Medicinal Chemistry. Elsevier. https://doi.org/10.1016/j.bmc.2010.09.012
View | DOI
 
[25]
2010 | Journal Article | IST-REx-ID: 3407
Janovjak, H. L., Szobota, S., Wyart, C., Trauner, D., & Isacoff, E. (2010). A light-gated, potassium-selective glutamate receptor for the optical inhibition of neuronal firing. Nature Neuroscience, 13, 1027–1032. https://doi.org/10.1038/nn.2589
View | DOI
 
[24]
2009 | Journal Article | IST-REx-ID: 3408
Szymczak, P., & Janovjak, H. L. (2009). Periodic forces trigger a complex mechanical response in ubiquitin. Journal of Molecular Biology, 390(3), 443–456. https://doi.org/10.1016/j.jmb.2009.04.071
View | DOI
 
[23]
2008 | Book Review | IST-REx-ID: 3410
Janovjak, H. L., Sapra, T., Kedrov, A., & Mueller, D. (2008). From valleys to ridges: Exploring the energy landscape of single membrane proteins. ChemPhysChem. Wiley-Blackwell. https://doi.org/10.1002/cphc.200700662
View | DOI
 
[22]
2008 | Book Chapter | IST-REx-ID: 3726
Engel, A., Janovjak, H. L., Fotiadis, D., Kedrov, A., Cisneros, D., & Mueller, D. (2008). Single-molecule microscopy and force spectroscopy of membrane proteins. In Single Molecules and Nanotechnology (Vol. 12, pp. 279–311). Springer. https://doi.org/10.1007/978-3-540-73924-1_11
View | DOI
 
[21]
2008 | Journal Article | IST-REx-ID: 3409
Struckmeier, J., Wahl, R., Leuschner, M., Nunes, J., Janovjak, H. L., Geisler, U., … Mueller, D. (2008). Fully automated single-molecule force spectroscopy for screening applications. Nanotechnology, 19(38). https://doi.org/10.1088/0957-4484/19/38/384020
View | DOI
 
[20]
2007 | Journal Article | IST-REx-ID: 3411   OA
Preiner, J., Janovjak, H. L., Rankl, C., Knaus, H., Cisneros, D., Kedrov, A., … Hinterdorfer, P. (2007). Free energy of membrane protein unfolding derived from single-molecule force measurements. Biophysical Journal, 93(3), 930–937. https://doi.org/10.1529/biophysj.106.096982
View | DOI | Download (ext.)
 
[19]
2007 | Book Review | IST-REx-ID: 3412
Kedrov, A., Janovjak, H. L., Sapra, T., & Mueller, D. (2007). Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy. Annual Review of Biophysics. Annual Reviews. https://doi.org/10.1146/annurev.biophys.36.040306.132640
View | DOI
 
[18]
2007 | Journal Article | IST-REx-ID: 3727
Bippes, C., Janovjak, H. L., Kedrov, A., & Mueller, D. (2007). Digital force-feedback for protein unfolding experiments using atomic force microscopy. Nanotechnology, 18(4). https://doi.org/10.1088/0957-4484/18/4/044022
View | DOI
 
[17]
2007 | Journal Article | IST-REx-ID: 3723
Janovjak, H. L., Knaus, H., & Mueller, D. (2007). Transmembrane helices have rough energy surfaces. Journal of the American Chemical Society, 129(2), 246–247. https://doi.org/10.1021/ja065684a
View | DOI
 
[16]
2006 | Book Review | IST-REx-ID: 3415
Janovjak, H. L., Kedrov, A., Cisneros, D., Sapra, T., Struckmeier, J., & Mueller, D. (2006). Imaging and detecting molecular interactions of single membrane proteins. Neurobiology of Aging. Elsevier. https://doi.org/10.1016/j.neurobiolaging.2005.03.031
View | DOI
 
[15]
2006 | Book Chapter | IST-REx-ID: 3404
Janovjak, H. L., Sawhney, R., Stark, M., & Mueller, D. (2006). Atomic force microscopy. In Techniques in Microscopy for Biomedical Applications (Vol. 2, pp. 213–284). World Scientific Publishing.
View
 
[14]
2006 | Book Chapter | IST-REx-ID: 3722
Janovjak, H. L., & Mueller, D. (2006). Rastersondenmikroskopie. In Bioanalytik. Spektrum Akademischer Verlag.
View
 
[13]
2006 | Journal Article | IST-REx-ID: 3728
Cieplak, M., Filipek, S., Janovjak, H. L., & Krzysko, K. (2006). Pulling single bacteriorhodopsin out of a membrane: Comparison of simulation and experiment. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1758(4), 537–544. https://doi.org/10.1016/j.bbamem.2006.03.028
View | DOI
 
[12]
2006 | Journal Article | IST-REx-ID: 3413
Kessler, M., Gottschalk, K., Janovjak, H. L., Mueller, D., & Gaub, H. (2006). Bacteriorhodopsin folds into the membrane against an external force. Journal of Molecular Biology, 357(2), 644–654. https://doi.org/10.1016/j.jmb.2005.12.065
View | DOI
 
[11]
2006 | Journal Article | IST-REx-ID: 3414
Kedrov, A., Janovjak, H. L., Ziegler, C., Kühlbrandt, W., & Mueller, D. (2006). Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli. Journal of Molecular Biology, 355(1), 2–8. https://doi.org/10.1016/j.jmb.2005.10.028
View | DOI
 
[10]
2006 | Journal Article | IST-REx-ID: 3729
Bippes, C., Humphris, A., Stark, M., Mueller, D., & Janovjak, H. L. (2006). Direct measurement of single-molecule visco-elasticity in atomic force microscope force-extension experiments. European Biophysics Journal, 35(3), 287–292. https://doi.org/10.1007/s00249-005-0023-9
View | DOI
 
[9]
2005 | Journal Article | IST-REx-ID: 3721   OA
Janovjak, H. L., Mueller, D., & Humphris, A. (2005). Molecular force modulation spectroscopy revealing the dynamic response of single bacteriorhodopsins. Biophysical Journal, 88(2), 1423–1431. https://doi.org/10.1529/biophysj.104.052746
View | DOI | Download (ext.)
 
[8]
2005 | Journal Article | IST-REx-ID: 3416   OA
Janovjak, H. L., Sapra, T., & Mueller, D. (2005). Complex stability of single proteins explored by forced unfolding experiments. Biophysical Journal, 88(5), 37–39. https://doi.org/10.1529/biophysj.105.059774
View | DOI | Download (ext.)
 
[7]
2005 | Journal Article | IST-REx-ID: 3417
Kuhn, M., Janovjak, H. L., Hubain, M., & Mueller, D. (2005). Automated alignment and pattern recognition of single-molecule force spectroscopy data. Journal of Microscopy, 218(2), 125–132. https://doi.org/10.1111/j.1365-2818.2005.01478.x
View | DOI
 
[6]
2005 | Journal Article | IST-REx-ID: 3418
Janovjak, H. L., Struckmeier, J., & Mueller, D. (2005). Hydrodynamic effects in fast AFM single molecule force measurements. European Biophysics Journal, 34(1), 91–96. https://doi.org/10.1007/s00249-004-0430-3
View | DOI
 
[5]
2004 | Journal Article | IST-REx-ID: 3420
Kedrov, A., Ziegler, C., Janovjak, H. L., Kühlbrandt, W., & Mueller, D. (2004). Controlled unfolding and refolding of a single sodium/proton antiporter using atomic force microscopy. Journal of Molecular Biology, 340(5), 1143–1152. https://doi.org/10.1016/j.jmb.2004.05.026
View | DOI
 
[4]
2004 | Journal Article | IST-REx-ID: 3419
Janovjak, H. L., Struckmeier, J., Hubain, M., Kessler, M., Kedrov, A., & Mueller, D. (2004). Probing the energy landscape of the membrane protein bacteriorhodopsin. Structure, 12(5), 871–879. https://doi.org/10.1016/j.str.2004.03.016
View | DOI
 
[3]
2003 | Journal Article | IST-REx-ID: 3725   OA
Janovjak, H. L., Kessler, M., Oesterhelt, D., Gaub, H., & Mueller, D. (2003). Unfolding pathways of native bacteriorhodopsin depend on temperature. EMBO Journal, 22(19), 5220–5229. https://doi.org/10.1093/emboj/cdg509
View | DOI | Download (ext.)
 
[2]
2002 | Journal Article | IST-REx-ID: 3422
Müller, P., Janovjak, H. L., Miserez, A., & Dobbie, Z. (2002). Processing of gene expression data generated by quantitative real-time RT-PCR. Biotechniques, 32(6), 1372–1379.
View
 
[1]
2002 | Book Review | IST-REx-ID: 3421
Mueller, D., Janovjak, H. L., Lehto, T., Kuerschner, L., & Anderson, K. (2002). Observing structure, function and assembly of single proteins by AFM. Progress in Biophysics and Molecular Biology. Elsevier. https://doi.org/10.1016/S0079-6107(02)00009-3
View | DOI
 

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