ICS Key Visual

Navigation und Service


  • Rosenbach H, Borggräfe J, Victor J, Wuebben C, Schiemann O, Hoyer W, Steger G, Etzkorn M, Span I  
    Influence of monovalent metal ions on metal binding and catalytic activity of the 10–23 DNAzyme 
    Biological Chemistry , (2020) 
    https://doi.org/10.1515/hsz-2020-0207  
  • Rosenbach H, Victor J, Borggräfe J, Biehl R, Steger G, Etzkorn M, Span I. 
    Expanding crystallization tools for nucleic acid complexes using U1A protein variants 
    Journal of Structural Biology 210, 107480 (2020) 
    https://doi.org/10.1016/j.jsb.2020.107480  
  • Rosenbach H, Victor J, Etzkorn M, Steger G, Riesner D, Span I 
    Molecular Features and Metal Ions that Influence 10-23 DNAzyme Activity 
    Molecules 25, 3100 (2020) 
    https://doi.org/10.3390/molecules25133100  
    Special Issue "Advances in Catalytic DNA" 
  • Viegas A, Dollinger P, Verma N, Kubiak J, Viennet T, Seidel CAM, Gohlke H, Etzkorn M, Kovacic F, Jaeger KE 
    Structural and dynamic insights revealing how lipase binding domain MD1 of Pseudomonas aeruginosa foldase affects lipase activation  
    Sci Rep 10, 3578 (2020) 
    https://doi.org/10.1038/s41598-020-60093-4  
  • Viegas A, Yin DM, Borggräfe J, Viennet T, Falke M, Schmitz A, Famulok M, Etzkorn M 
    Molecular Architecture of a Network of Potential Intracellular EGFR Modulators: ARNO, CaM, Phospholipids, and the Juxtamembrane Segment 
    Structure 28, 1-9 (2020) 
    https://doi.org/10.1016/j.str.2019.11.001  
  • Falke M, Victor J, Wördehoff MM, Peduzzo A, Zhang T, Schröder GF, Buell AK, Hoyer W, Etzkorn M 
    α-Synuclein-derived lipoparticles in the study of α-synuclein amyloid fibril formation 
    Chem Phys Lipids 220, 57-65 (2019) 
    https://doi.org/10.1016/j.chemphyslip.2019.02.009  
  • Porta N, Zaschke-Kriesche J, Frieg J, Gopalswamy M, Zivkovic A, Etzkorn M, Stark H, Smits S, Gohlke H 
    Small-molecule inhibitors of nisin resistance protein NSR from the human pathogen Streptococcus agalactiae  
    Bioorg Med Chem 27, 115079 (2019) 
    https://doi.org/10.1016/j.bmc.2019.115079  
  • Viennet T, Bungert-Pümke S, Elter S, Viegas A, Fahlke C, Etzkorn M 
    Reconstitution and NMR characterization of the ion-channel accessory subunit barttin in detergents and lipid-bilayer nanodiscs 
    Frontiers in Molecular Biosciences 6, 13 (2019) 
    https://doi.org/10.3389/fmolb.2019.00013  
  • Uluca B, Viennet T, Petrovic D, Shaykhalishahi H, Weirich F, Gönülalan A, Strodel B, Etzkorn M, Hoyer W, Heise H 
    DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of α-Synuclein in Different States 
    Biophys. J. 114, 1614-1623 (2018) 
    https://doi.org/10.1016/j.bpj.2018.02.011  
  • Viennet T, Wördehoff MW, Uluca B, Poojari C, Shaykhalishahi H, Willbold D, Strodel B, Heise H, Buell AK, Hoyer W, Etzkorn M: 
    Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation 
    Commun. Biol. 1, 44 (2018) 
    https://doi.org/10.1038/s42003-018-0049-z  
  • Bronder AM, Bieker A, Elter S, Etzkorn M, Haeussinger D, Oesterhelt F 
    Oriented membrane protein reconstitution into tethered lipid membranes for AFM Force Spectroscopy 
    Biophys. J. 111, 1925-1934 (2016) 
    http://dx.doi.org/10.1016/j.bpj.2016.08.051  
  • Viegas A, Viennet T, Etzkorn M 
    The power, pitfalls and potential of the nanodisc system for NMR-based studies  
    Biol. Chem. 397, 1335–1354 (2016) 
    https://doi.org/10.1515/hsz-2016-0224  
  • Viegas A, Viennet T, Yu TY, Schumann F, Bermel W, Wagner G, Etzkorn M 
    UTOPIA NMR: activating unexploited magnetization using interleaved low-gamma detection. 
    J. Biomol. NMR 64, 9-15 (2016) 
    http://dx.doi.org/10.1007/s10858-015-0008-7  
  • Viennet T, Viegas A, Kuepper A, Arens S, Gelev V, Petrov O, Grossmann TN, Heise H, Etzkorn M 
    Selective Protein Hyperpolarization in Cell Lysates Using Targeted Dynamic Nuclear Polarization 
    Angew. Chem. Int. Ed. 55, 10746–10750 (2016) 
    http://dx.doi.org/10.1002/anie.201603205  
    (selected as inside cover article)  
  • Elter S, Raschle T, Arens S, Viegas A, Gelev V, Etzkorn M, Wagner G 
    The use of amphipols for NMR structural characterization of 7-TM proteins 
    J. Membr. Biol. 247, 957-964 (2014) 
    http://dx.doi.org/10.1007/s00232-014-9669-5  
  • Etzkorn M, Zoonens M, Catoire LJ, Popot JL, Hiller S 
    How Amphipols Embed Membrane Proteins: Global Solvent Accessibility and Interaction with a Flexible Protein Terminus 
    J. Membr. Biol. 247, 965-970 (2014) 
    http://dx.doi.org/10.1007/s00232-014-9657-9  
  • Yi T, Zhai B, Yu Y, Kiyotsugu Y, Raschle T, Etzkorn M, Seo HC, Nagiec M, Luna RE, Reinherz EL, Blenis J, Gygi SP, Wagner G 
    Quantitative phosphoproteomic analysis reveals system-wide signaling pathways downstream of SDF-1/CXCR4 in breast cancer stem cells 
    PNAS 111(21), E2182-E2190 (2014) 
    http://dx.doi.org/10.1073/pnas.1404943111  
    http://dx.doi.org/10.1073/pnas.1405991111  
    See also PNAS highlight commentary (follow second link) 
  • Etzkorn M, Raschle T, Hagn F, Gelev V, Rice A, Walz T, Wagner G 
    Cell-Free Expressed Bacteriorhodopsin in Different Soluble Membrane Mimetics: Biophysical Properties and NMR Accessibility. 
    Structure 21, 394-401 (2013) 
    http://dx.doi.org/10.1016/j.str.2013.01.005  
  • Hagn F, Etzkorn M, Raschle T, Wagner G 
    Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins 
    J. Am. Chem. Soc 135, 1919-1925 (2013) 
    http://dx.doi.org/10.1021/ja310901f  
    (See also Science Editor's Choice: http://dx.doi.org/10.1126/science.339.6123.1013-a ) 
  • Müller H, Etzkorn M, Heise H 
    Solid-State NMR Spectroscopy of Proteins. 
    Top. Curr. Chem. in press, (2013) 
  • Etzkorn M, Böckmann A, Baldus M 
    Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR 
    J. biomol. NMR 49, 121-129 (2011) 
    http://dx.doi.org/10.1007/s10858-011-9468-6  
  • Bardiaux B, Favier A, Etzkorn M, Baldus M, Böckmann A, Nilges M, Malliavin T: 
    Simultaneous use of solution, solid-state NMR and X-ray crystallography to study the conformational landscape of the Crh protein during oligomerization and crystallization. 
    Adv. Appl. Bioinf. Chem. 3, 25-38 (2010) 
  • Etzkorn M, Seidel K, Li L, Martell S, Engelhard M, Baldus M 
    Complex Formation and Light Activation in Membrane Embedded Sensory Rhodopsin II as Seen by Solid-State NMR Spectroscopy. 
    Structure 10, 293-300 (2010) 
    http://dx.doi.org/10.1016/j.str.2010.01.011  
  • Kneuper H, Scheu PD, Etzkorn M, Sevvana M, Dünnwald P, Becker S, Baldus M, Griesinger C, Unden G 
    Sensing Ligands by Periplasmic Sensing Histidine Kinases with Sensory PAS Domains. 
    Sensory Mechanisms in Bacteria; Caister Academic Press, (2010) 
  • Raschle T, Hiller S, Etzkorn M, Wagner G 
    Non-micellar systems for solution NMR spectroscopy of membrane proteins. 
    Curr. Opin. Struct. Biol. 20, 471-479 (2010) 
    http://dx.doi.org/10.1016/j.sbi.2010.05.006  
  • Schneider R, Etzkorn M, Giller K, Daebel V, Eisfeld J, Zweckstetter M, Griesinger C, Becker S, Lange A 
    The Native Conformation of the Human VDAC1 N Terminus 
    Angew. Chem. Int. Ed. 49, 1882-1885 (2010) 
    http://dx.doi.org/10.1002/anie.200906241  
  • Schneider R, Seidel K, Etzkorn M, Lange A, Becker S, Baldus M 
    Probing molecular motion by double-quantum (13C,13C) solid-state NMR spectroscopy: application to ubiquitin. 
    J. Am. Chem. Soc 132, 223-233 (2010) 
    http://dx.doi.org/10.1021/ja906283h  
  • Ader C, Schneider R, Seidel K, Etzkorn M, Becker S, Baldus M 
    Structural rearrangements of membrane proteins probed by water-edited solid-state NMR spectroscopy. 
    J. Am. Chem. Soc 131, 170-176 (2009) 
    http://dx.doi.org/10.1021/ja806306e  
  • Seidel K, Etzkorn M, Schneider R, Ader C, Baldus M 
    Comparative Analysis of NMR Chemical Shift Predictions for Proteins in the Solid Phase. 
    Solid State Nucl. Magn. Res. 35, 235-242 (2009) 
    http://dx.doi.org/10.1016/j.ssnmr.2008.12.008  
  • Etzkorn M, Kneuper H, Dünnwald P, Vijaian V, Griesinger C, Becker S, Unden G, Baldus M 
    Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS. 
    Nat. Struct. Mol. Biol. 15, 1031-1039 (2008) 
    http://dx.doi.org/10.1038/nsmb.1493  
    (selected as "Article of the month") 
  • Gardiennet C, Loquet A, Etzkorn M, Heise H, Baldus M, Böckmann A 
    Structural constraints for the Crh protein from solid-state NMR. 
    J. biomol. NMR 4035, 239-250 (2008) 
    http://dx.doi.org/10.1007/s10858-008-9229-3  
  • Ader C, Schneider R, Seidel K, Etzkorn M, Baldus, M 
    Magic-angle-spinning NMR spectroscopy applied to small molecules and peptides in lipid bilayers. 
    Biochem. Soc. Trans. 35, 991-995 (2007) 
    http://dx.doi.org/10.1042/BST0350991  
  • Etzkorn M, Böckmann A, Penin F, Riedel D, Baldus M 
    Characterization of folding intermediates of a domain-swapped protein by solid-state NMR spectroscopy. 
    J. Am. Chem. Soc 129, 169-175 (2007) 
    http://dx.doi.org/10.1021/ja066469x  
  • Etzkorn M, Martell S, Andronesi OC, Seidel K, Engelhard M, Baldus M 
    Secondary structure and topology of a seven-helix receptor in native membranes studied by solid-state NMR. 
    Angew. Chem. Int. Ed. 46, 459-462 (2007) 
    http://dx.doi.org/10.1002/anie.200602139  
    (selected as "Cover article") 
  • Heise H, Seidel K, Etzkorn M, Becker S, Baldus M 
    3D MAS Solid-state NMR spectroscopy for resonance assignment and structure elucidation of proteins. Novel pulse schemes and sensitivity considerations. 
    J. Magn. Res. 173, 65-74 (2005) 
    http://dx.doi.org/10.1016/j.jmr.2004.11.020  
  • Seidel K, Etzkorn M, Heise H, Becker S, Baldus M 
    High-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin. 
    ChemBioChem 6, 1638-1647 (2005) 
    http://dx.doi.org/10.1002/cbic.200500085  
  • Seidel K, Etzkorn M, Sonnenberg L, Griesinger C, Sebald A, Baldus M 
    Studying 3D structure and dynamics by high resolution solid-state NMR: Application to L-Tyrosine-Ethylester. 
    J. Phys. Chem. A 109, 2436-2442 (2005) 
    http://dx.doi.org/10.1021/jp045605m  
  • Etzkorn M, Böckmann A, Lange A, Baldus M 
    Probing molecular interfaces using 2D magic-angle-spinning NMR on protein mixtures with di¬fferent uniform labeling. 
    J. Am. Chem. Soc 126, 14746-14751 (2004) 
    http://dx.doi.org/10.1021/ja0479181  

Servicemenü

Homepage