- 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
- 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)
http://onlinelibrary.wiley.com/doi/10.1002/1873-3468.12983/abstract
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- 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, 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
- 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)
http://dx.doi.org/10.1126/science.aao2825
http://science.sciencemag.org/content/early/2017/09/06/science.aao2825
- 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
- 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)
http://dx.doi.org/10.1371/journal.pone.0102425
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0102425
- 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
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