Cukkemane A, Becker N, Zielinski M, Frieg B, Lakomek NA, Heise H, SchröderGF, Willbold D, Weiergräber OH Conformational heterogeneity coupled with β-fibril formation of a scaffold protein involved in chronic mental illnesses Transl Psychiatry 11, 639 (2021) https://doi.org/10.1038/s41398-021-01765-1
König AS, Rösener NS, Gremer L, Tusche M, Flender D, Reinartz E, Hoyer W, Neudecker P, Willbold D, Heise H Structural details of amyloid β oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy J Biol Chem 296, 100499 (2021) https://doi.org/10.1016/j.jbc.2021.100499
Willbold D, Strodel B, Schröder GF, Hoyer W, Heise H Amyloid-type protein aggregation and prion-like properties of amyloids Chem Rev 121, 8285-8307 (2021) https://doi.org/10.1021/acs.chemrev.1c00196
Hasecke F, Miti T, Perez C, Barton J, Schölzel D, Gremer L, Grüning CSR, Matthews G, Meisl G, Knowles TPJ, Willbold D, Neudecker P, Heise H, Ullah G, Hoyer W, Muschol M Origin of metastable oligomers and their effects on amyloid fibril self-assembly Chem. Sci. 9, 5937-5948 (2018) https://doi.org/10.1039/c8sc01479e
Rösener NS, Gremer L, Reinartz E, König A, Brener O, Heise H, Hoyer W, Neudecker P, Willbold D A d-enantiomeric peptide interferes with heteroassociation of amyloid-β oligomers and prion protein J. Biol. Chem. 293, 15748-15764 (2018) https://doi.org/10.1074/jbc.RA118.003116
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, 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)
Weirich F, Gremer L, Mirecka EA, Schiefer S, Hoyer W, Heise H Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet Core PLOS One 11, e0161243 (2016) http://dx.doi.org/10.1371/journal.pone.0161243
Müller H, Brener O, Andreoletti O, Piechatzek T, Willbold D, Legname G, Heise H Progress toward structural understanding of infectious sheep PrP-amyloid Prion 8, 344-358 (2014)
Do H, Wittlich M, Glück JM, Möckel L, Willbold D, Koenig BW, Heise H Full-length Vpu and human CD4(372-433) in phospholipid bilayers as seen by magic angle spinning NMR. Biol. Chem. 394, 1453-1463 (2013)
Müller H, Etzkorn M, Heise H Solid-State NMR Spectroscopy of Proteins. Top. Curr. Chem. in press, (2013)
Kumar A, Heise H, Blommers MJJ, Krastel P, Schmitt E, Petersen F, Mandelkow EM, Carlomagno T, Griesinger C, Baldus M Interaction of Epothilone B (Patupilone) with Microtubules, as Detected by Solid-State NMR Spectroscopy Angew. Chem. Int. Ed. Engl. 49, 7504-7507 (2010)
Karpinar DP, Balija MBG, Kügler S, Opazo F, Rezaei-Ghaleh N, Bender N, Kim HY, Taschenberger G, Falkenburger BH, Heise H, Kumar A, Riedel D, Fichtner L, Voigt A, Braus GH, Giller K, Becker S, Herzig A, Baldus M, Jäckle H, Eimer S, Schulz JB, Griesinger C, Zweckstetter M Pre-fibrillar a-Synuclein Variants with Impaired beta-Structure Increase Neurotoxicity in Parkinson`s Disease Models EMBO J. 28, 3256-3268 (2009)
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
Gardiennet C, Loquet A, Etzkorn M, Heise H, Baldus M, Böckmann A Structural constraints for the Crh protein from solid-state NMR experiments. J. Biomol. NMR 40, 239-250. (2008)
Heise H Solid-State NMR Spectroscopy of Amyloid Proteins. ChemBioChem 9, 179-189 (2008)
Heise H, Celej MS, Becker S, Riedel D, Pelah A, Kumar A, Jovin TM, Baldus M Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein J. Mol. Biol. 380, 444-450 (2008)
Heise H, Hoyer W, Becker S, Anronesi OC, Riedel D, Baldus M Molecular secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR Proc. Natl. Acad. Sci. USA 102, 15871-15876 (2005)
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
