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  • 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) 
  • 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) 
  • 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) 
  • 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) 
  • Kulawik A,Heise H,Zafiu C,Willbold D,Bannach O. 
    Advancements of the sFIDA method for oligomer-based diagnostics of neurodegenerative diseases 
    FEBS Letters , (2018) 
  • 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) 
  • 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) 
  • 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) 
  • Gremer L, Schölzel D, Schenk C, Reinartz E, Labahn J, Ravelli RB, Tusche M, Lopez-Iglesias C, Hoyer W, Heise H, Willbold D, Schröder GF 
    Fibril structure of amyloid-ß(1-42) by cryoelectron microscopy 
    Science 358, 116-119 (2017) 
  • 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) 
    (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) 
  • Zhang SC, Gremer L, Heise H, Janning P, Shymanets A, Cirstea IC, Krause E,Nürnberg B, Ahmadian MR 
    Liposome reconstitution and modulation of recombinant prenylated human Rac1 by GEFs, GDI1 and Pak1 
    PLoS One 9(7), (2016) 
  • 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) 
  • 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) 
  • 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)