Publications of the Schuler Group

ZORA Publication List

Publications

• 2015

  • Benke, S., Roderer, D., Wunderlich, B., Nettels, D., Glockshuber, R., & Schuler, B. (2015). The assembly dynamics of the cytolytic pore toxin ClyA Nature Communications, 6, 6198. https://doi.org/10.1038/ncomms7198
  • Borgia, A., Kemplen, K. R., Borgia, M. B., Soranno, A., Shammas, S., Wunderlich, B., Nettels, D., Best, R. B., Clarke, J., & Schuler, B. (2015). Transient misfolding dominates multidomain protein folding Nature Communications, 6, online. https://doi.org/10.1038/ncomms9861

• 2014

  • Hofmann, H., Hillger, F., Delley, C., Hoffmann, A., Pfeil, S. H., Nettels, D., Lipman, E. A., & Schuler, B. (2014). Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy Biophysical Journal, 107, 2882–2893. https://doi.org/10.1016/j.bpj.2014.11.002
  • Roderer, D., Benke, S., Müller, M., Fäh-Rechsteiner, H., Ban, N., Schuler, B., & Glockshuber, R. (2014). Characterization of variants of the pore-forming toxin ClyA from Escherichia coli controlled by a redox switch Biochemistry, 53, 6357–6369. https://doi.org/10.1021/bi5007578
  • Brucale, M., Schuler, B., & Samorì, B. (2014). Single-molecule studies of intrinsically disordered proteins Chemical Reviews, 114, 3281–3317. https://doi.org/10.1021/cr400297g
  • Kellner, R., Hofmann, H., Barducci, A., Wunderlich, B., Nettels, D., & Schuler, B. (2014). Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein Proceedings of the National Academy of Sciences of the United States of America, 111, 13355–13360. https://doi.org/10.1073/pnas.1407086111
  • Weisenburger, S., Jing, B., Hänni, D., Reymond, L., Schuler, B., Renn, A., & Sandoghdar, V. (2014). Cryogenic colocalization microscopy for nanometer-distance measurements ChemPhysChem, 15, 763–770. https://doi.org/10.1002/cphc.201301080
  • Soranno, A., Koenig, I., Borgia, M. B., Hofmann, H., Zosel, F., Nettels, D., & Schuler, B. (2014). Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments Proceedings of the National Academy of Sciences of the United States of America, 111, 4874–4879. https://doi.org/10.1073/pnas.1322611111
  • Wuttke, R., Hofmann, H., Nettels, D., Borgia, M. B., Mittal, J., Best, R. B., & Schuler, B. (2014). Temperature-dependent solvation modulates the dimensions of disordered proteins Proceedings of the National Academy of Sciences of the United States of America, 111, 5213–5218. https://doi.org/10.1073/pnas.1313006111
  • Pochorovski, I., Knehans, T., Nettels, D., Müller, A. M., Schweizer, W. B., Caflisch, A., Schuler, B., & Diederich, F. (2014). Experimental and computational study of BODIPY dye-labeled cavitand dynamics Journal of the American Chemical Society, 136, 2441–2449. https://doi.org/10.1021/ja4104292

• 2013

  • Schuler, B., & Clarke, J. (2013). Biophysics: Rough passage across a barrier Nature, 502, 632–633. https://doi.org/10.1038/nature12697
  • Schuler, B., & Hofmann, H. (2013). Single-molecule spectroscopy of protein folding dynamics - expanding scope and timescales Current Opinion in Structural Biology, 23, 36–47. https://doi.org/10.1016/j.sbi.2012.10.008
  • Hofmann, H., Nettels, D., & Schuler, B. (2013). Single-molecule spectroscopy of the unexpected collapse of an unfolded protein at low pH Journal of Chemical Physics, 139, 121930. https://doi.org/10.1063/1.4820490
  • Haenni, D., Zosel, F., Reymond, L., Nettels, D., & Schuler, B. (2013). Intramolecular distances and dynamics from the combined Photon statistics of single-molecule FRET and photoinduced electron transfer Journal of Physical Chemistry B, 117, 13015–13028. https://doi.org/10.1021/jp402352s
  • Aznauryan, M., Nettels, D., Holla, A., Hofmann, H., & Schuler, B. (2013). Single-molecule spectroscopy of cold denaturation and the temperature-induced collapse of unfolded proteins Journal of the American Chemical Society, 135, 14040–14043. https://doi.org/10.1021/ja407009w
  • Wunderlich, B., Nettels, D., Benke, S., Clark, J., Weidner, S., Hofmann, H., Pfeil, S. H., & Schuler, B. (2013). Microfluidic mixer designed for performing single-molecule kinetics with confocal detection on timescales from milliseconds to minutes Nature Protocols, 8, 1459–1474. https://doi.org/10.1038/nprot.2013.082

• 2012

  • Nettels, D., Hoffmann, A., & Schuler, B. (2012). Correction to “Unfolded Protein and Peptide Dynamics Investigated with Single-Molecule FRET and Correlation Spectroscopy from Picoseconds to Seconds.” Journal of Physical Chemistry B, 112, 6137–6146. https://doi.org/10.1021/jp303954v
  • Schuler, B., Müller-Späth, S., Soranno, A., & Nettels, D. (2012). Application of confocal single-molecule FRET to intrinsically disordered proteins Methods in Molecular Biology, 896, 21–45. https://doi.org/10.1007/978-1-4614-3704-8_2
  • Hofmann, H., Soranno, A., Borgia, A., Gast, K., Nettels, D., & Schuler, B. (2012). Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy Proceedings of the National Academy of Sciences of the United States of America, 109, 16155–16160. https://doi.org/10.1073/pnas.1207719109
  • Borgia, A., Wensley, B. G., Soranno, A., Nettels, D., Borgia, M. B., Hoffmann, A., Pfeil, S. H., Lipman, E. A., Clarke, J., & Schuler, B. (2012). Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy Nature Communications, 3, 1195. https://doi.org/10.1038/ncomms2204

Pagination