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Coauthors
Michael Wördehoff Physikalische Biologie, Heinrich-Heine-Universität, Germany, Germany,
1 protocol

Wolfgang Hoyer
  • Institut für Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf, Germany, Germany,
  • 1 Author merit

Education

PhD, Max Planck Institute for Biophysical Chemistry, Germany, 2004

Current position

Group Leader, Physical Biology, Heinrich Heine University Düsseldorf, Germany

Publications

  1. Hasecke, F., Miti, T., Perez, C., Barton, J., Schölzel, D., Gremer, L., Grüning, C. S., Matthews, G., Meisl, G., Knowles, T. P., Willbold, D., Neudecker, P., Heise, H., Ullah, G., Hoyer, W. and Muschol, M. (2018) Origin of metastable oligomers and their effects on amyloid fibril self-assembly. Chem Sci
  2. Uluca, B., Viennet, T., Petrovic, D., Shaykhalishahi, H., Weirich, F., Gonulalan, A., Strodel, B., Etzkorn, M., Hoyer, W. and Heise, H. (2018). DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of alpha-Synuclein in Different States. Biophys J 114(7): 1614-1623.
  3. Viennet, T., Wördehoff, M. M., Uluca, B., Poojari, C., Shaykhalishahi, H., Willbold, D., Strodel, B., Heise, H., Buell, A. K., Hoyer, W. and Etzkorn, M. (2018) Structural insights from lipid-bilayer nanodiscs link α-synuclein membrane-binding modes to amyloid fibril formation. Communications Biology
  4. Orr, A. A., Shaykhalishahi, H., Mirecka, E. A., Jonnalagadda, S. V., Hoyer, W. and Tamamis, P. (2018) Elucidating the multi-targeted anti-amyloid activity and enhanced islet amyloid polypeptide binding of β-wrapins. Comput Chem Eng
  5. Gremer, L., Scholzel, D., Schenk, C., Reinartz, E., Labahn, J., Ravelli, R. B. G., Tusche, M., Lopez-Iglesias, C., Hoyer, W., Heise, H., Willbold, D. and Schroder, G. F. (2017). Fibril structure of amyloid-beta(1-42) by cryo-electron microscopy. Science 358(6359): 116-119.
  6. Wordehoff, M. M., Shaykhalishahi, H., Gross, L., Gremer, L., Stoldt, M., Buell, A. K., Willbold, D. and Hoyer, W. (2017). Opposed Effects of Dityrosine Formation in Soluble and Aggregated alpha-Synuclein on Fibril Growth. J Mol Biol 429(20): 3018-3030.
  7. Mirecka, E. A., Feuerstein, S., Gremer, L., Schroder, G. F., Stoldt, M., Willbold, D. and Hoyer, W. (2016). beta-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor. Sci Rep 6: 33474.
  8. Orr, A. A., Wordehoff, M. M., Hoyer, W. and Tamamis, P. (2016). Uncovering the Binding and Specificity of beta-Wrapins for Amyloid-beta and alpha-Synuclein. J Phys Chem B 120(50): 12781-12794.
  9. Weirich, F., Gremer, L., Mirecka, E. A., Schiefer, S., Hoyer, W. and Heise, H. (2016). Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the beta-Sheet Core. PLoS One 11(9): e0161243.
  10. Brener, O., Dunkelmann, T., Gremer, L., van Groen, T., Mirecka, E. A., Kadish, I., Willuweit, A., Kutzsche, J., Jurgens, D., Rudolph, S., Tusche, M., Bongen, P., Pietruszka, J., Oesterhelt, F., Langen, K. J., Demuth, H. U., Janssen, A., Hoyer, W., Funke, S. A., Nagel-Steger, L. and Willbold, D. (2015). QIAD assay for quantitating a compound's efficacy in elimination of toxic Abeta oligomers. Sci Rep 5: 13222.
  11. Shaykhalishahi, H., Gauhar, A., Wordehoff, M. M., Gruning, C. S., Klein, A. N., Bannach, O., Stoldt, M., Willbold, D., Hard, T. and Hoyer, W. (2015). Contact between the beta1 and beta2 Segments of alpha-Synuclein that Inhibits Amyloid Formation. Angew Chem Int Ed Engl 54(30): 8837-8840.
  12. Wordehoff, M. M., Bannach, O., Shaykhalishahi, H., Kulawik, A., Schiefer, S., Willbold, D., Hoyer, W. and Birkmann, E. (2015). Single fibril growth kinetics of alpha-synuclein. J Mol Biol 427(6 Pt B): 1428-1435.
  13. Shaykhalishahi, H., Mirecka, E. A., Gauhar, A., Gruning, C. S., Willbold, D., Hard, T., Stoldt, M. and Hoyer, W. (2015). A beta-hairpin-binding protein for three different disease-related amyloidogenic proteins. Chembiochem 16(3): 411-414.
  14. Gauhar, A., Shaykhalishahi, H., Gremer, L., Mirecka, E. A. and Hoyer, W. (2014). Impact of subunit linkages in an engineered homodimeric binding protein to alpha-synuclein. Protein Eng Des Sel 27(12): 473-479.
  15. Gruning, C. S., Mirecka, E. A., Klein, A. N., Mandelkow, E., Willbold, D., Marino, S. F., Stoldt, M. and Hoyer, W. (2014). Alternative conformations of the Tau repeat domain in complex with an engineered binding protein. J Biol Chem 289(33): 23209-23218.
  16. Mirecka, E. A., Gremer, L., Schiefer, S., Oesterhelt, F., Stoldt, M., Willbold, D. and Hoyer, W. (2014). Engineered aggregation inhibitor fusion for production of highly amyloidogenic human islet amyloid polypeptide. J Biotechnol 191: 221-227.
  17. Mirecka, E. A., Shaykhalishahi, H., Gauhar, A., Akgul, S., Lecher, J., Willbold, D., Stoldt, M. and Hoyer, W. (2014). Sequestration of a beta-hairpin for control of alpha-synuclein aggregation. Angew Chem Int Ed Engl 53(16): 4227-4230.
  18. Gruning, C. S., Klinker, S., Wolff, M., Schneider, M., Toksoz, K., Klein, A. N., Nagel-Steger, L., Willbold, D. and Hoyer, W. (2013). The off-rate of monomers dissociating from amyloid-beta protofibrils. J Biol Chem 288(52): 37104-37111.
  19. Luheshi, L. M., Hoyer, W., de Barros, T. P., van Dijk Hard, I., Brorsson, A. C., Macao, B., Persson, C., Crowther, D. C., Lomas, D. A., Stahl, S., Dobson, C. M. and Hard, T. (2010). Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo. PLoS Biol 8(3): e1000334.
  20. Macao, B., Hoyer, W., Sandberg, A., Brorsson, A. C., Dobson, C. M. and Hard, T. (2008). Recombinant amyloid beta-peptide production by coexpression with an affibody ligand. BMC Biotechnol 8: 82.
  21. Hoyer, W. and Hard, T. (2008). Interaction of Alzheimer's A beta peptide with an engineered binding protein--thermodynamics and kinetics of coupled folding-binding. J Mol Biol 378(2): 398-411.
  22. Hoyer, W., Gronwall, C., Jonsson, A., Stahl, S. and Hard, T. (2008). Stabilization of a beta-hairpin in monomeric Alzheimer's amyloid-beta peptide inhibits amyloid formation. Proc Natl Acad Sci U S A 105(13): 5099-5104
1 Protocol published
α-Synuclein Aggregation Monitored by Thioflavin T Fluorescence Assay
Authors:  Michael M. Wördehoff and Wolfgang Hoyer, date: 07/20/2018, view: 34, Q&A: 0
Studying the aggregation of amyloid proteins like α-synuclein in vitro is a convenient and popular tool to gain kinetic insights into aggregation as well as to study factors (e.g., aggregation inhibitors) that influence it. These ...