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  • Altendorf T, Gering I, Santiago-Schübel B, Aghabashlou Saisan S, Tamgüney G, Tusche M, Honold D, Schemmert S, Hoyer W, Mohrlüder J, Willbold D 
    Stabilization of monomeric Tau protein by all D-enantiomeric peptide ligands as therapeutic strategy for Alzheimer's disease and other tauopathies 
    Int J Mol Sci 24, 2161 (2023) 
  • Gomes CM, Hoyer W, Luo J 
    Editorial: The biochemistry of amyloids in neurodegenerative diseases, volume II 
    Front Neurosci 17, 1236518 (2023) 
  • Heid LF, Kupreichyk T, Schützmann MP, Schneider W, Stoldt M, Hoyer W 
    Nucleation of α-Synuclein Amyloid Fibrils Induced by Cross-Interaction with β-Hairpin Peptides Derived from Immunoglobulin Light Chains 
    Int J Mol Sci 24, 16132 (2023) 
  • Muschol M, Hoyer W 
    Amyloid oligomers as on-pathway precursors or off-pathway competitors of fibrils 
    Front Mol Biosci 10, 1120416 (2023) 
  • Pils M, Dybala A, Rehn F, Blömeke L, Bujnicki T, Kraemer-Schulien V, Hoyer W, Riesner D, Willbold D, Bannach O 
    Development and implementation of an internal quality control sample to standardize oligomer-based diagnostics of Alzheimer's disease 
    Diagnostics 13, 1702 (2023) 
  • Schulz CM, Pfitzer A, Hoyer W 
    Fibril core regions in engineered α-synuclein dimer are crucial for blocking of fibril elongation 
    BBA Adv 4, 100110 (2023) 
  • Braczynski AK, Sevenich M, Gering I, Kupreichyk T, Agerschou ED, Kronimus Y, Habib P, Stoldt M, Willbold D, Schulz JB, Bach JP, Falkenburger BH, Hoyer W 
    Alpha-synuclein-specific naturally occurring antibodies inhibit aggregation in vitro and in vivo 
    Biomolecules 12, 469 (2022) 
  • Maity D, Oh Y, Gremer L, Hoyer W, Magzoub M, Hamilton AD 
    Cucurbit[7]uril inhibits islet amyloid polypeptide aggregation by targeting N terminus hot segments and attenuates cytotoxicity 
    Chemistry , e202200456 (2022) 
  • Törner R, Kupreichyk T, Gremer L, Debled EC, Fenel D, Schemmert S, Gans P, Willbold D, Schoehn G, Hoyer W, Boisbouvier J 
    Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin 
    Nat Commun 13, 2363 (2022) 
  • Törner R, Kupreichyk T, Hoyer W, Boisbouvier J 
    The role of heat shock proteins in preventing amyloid toxicity 
    Front Mol Biosci 9, 1045616 (2022) 
  • Agerschou ED, Schützmann MP, Reppert N, Wördehoff MM, Shaykhalishahi H, Buell AK, Hoyer W 
    β-Turn exchanges in the α-synuclein segment 44-TKEG-47 reveal high sequence fidelity requirements of amyloid fibril elongation 
    Biophys. Chem. 269, 106519 (2021) 
  • Gomes CM, Hoyer W, Luo J 
    Editorial: The Biochemistry of Amyloids in Neurodegenerative Diseases, Volume I 
    Front Neurosci 15, 819481 (2021) 
  • Hasecke F, Niyangoda C, Borjas G, Pan J, Matthews G, Muschol M, Hoyer W 
    Protofibril‐fibril interactions inhibit amyloid fibril assembly by obstructing secondary nucleation 
    Angew. Chem. Int. Ed. 60, 3016-3021 (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) 
  • Rosenbach H, Borggräfe J, Victor J, Wuebben C, Schiemann O, Hoyer W, Steger G, Etzkorn M, Span I 
    Influence of monovalent metal ions on metal binding and catalytic activity of the 10–23 DNAzyme 
    Biological Chemistry 402, 99-111 (2021) 
  • Schützmann MP, Hasecke F, Bachmann S, Zielinski M, Hänsch S, Schröder GF, Zempel H, Hoyer W 
    Endo-lysosomal Aβ concentration and pH trigger formation of Aβ oligomers that potently induce Tau missorting 
    Nat Commun 12, 4634 (2021) 
  • Szegő EM, Boß F, Komnig D, Gärtner C, Höfs L, Shaykhalishahi H, Wördehoff MM, Saridaki T, Schulz JB, Hoyer W, Falkenburger BH 
    A β-wrapin targeting the N-terminus of α-synuclein monomers reduces fibril-induced aggregation in neurons 
    Front Neurosci 15, 696440 (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) 
  • Agerschou ED, Borgmann V, Wördehoff MM, Hoyer W 
    Inhibitor and substrate cooperate to inhibit amyloid fibril elongation of α-synuclein 
    Chem. Sci. 11, 11331-11337 (2020) 
  • Maity D, Kumar S, AlHussein R, Gremer L, Howarth M, Karpauskaite L, Hoyer W, Magzoubd M, Hamilton AD 
    Sub-stoichiometric inhibition of IAPP aggregation: a peptidomimetic approach to antiamyloid agents 
    RSC Chem. Biol. 1, 225-232 (2020) 
  • Röder C, Kupreichyk T, Gremer L, Schäfer LU, Pothula KR, Ravelli RBG, Willbold D, Hoyer W, Schröder GF 
    Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils 
    Nat. Struct. Mol. Biol. 27, 660-667 (2020) 
  • Rösener NS, Gremer L, Wördehoff MM, Kupreichyk T, Etzkorn M, Neudecker P, Hoyer W 
    Clustering of human prion protein and α-synuclein oligomers requires the prion protein Nterminus 
    Commun. Biol. 3, 365 (2020) 
  • Agerschou ED, Flagmeier P, Saridaki T, Galvagnion C, Komnig D, Heid L, Prasad V, Shaykhalishahi H, Willbold D, Dobson CM, Voigt A, Falkenburger B, Hoyer W, Buell AK 
    An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils 
    eLife 8, e46112 (2019) 
  • Falke M, Victor J, Wördehoff MM, Peduzzo A, Zhang T, Schröder GF, Buell AK, Hoyer W, Etzkorn M 
    α-Synuclein-derived lipoparticles in the study of α-synuclein amyloid fibril formation 
    Chem Phys Lipids 220, 57-65 (2019) 
  • Perez C, Miti T, Hasecke F, Meisl G, Hoyer W, Muschol M, Ullah G 
    Mechanism of fibril and soluble oligomer formation in amyloid β and hen egg white lysozyme proteins 
    J. Phys. Chem. B 123, 5678-5689 (2019) 
  • Röder C, Vettore N, Mangels LN, Gremer L, Ravelli RBG, Willbold D, Hoyer W, Buell AK, Schröder GF 
    Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy 
    Nat. Commun. 10, 3754 (2019) 
  • Duggimpudi S, Kloetgen A, Maney SK, Münch PC, Hezaveh K, Shaykhalishahi H, Hoyer W, McHardy AC, Lang PA, Borkhardt A, Hoell JI 
    Transcriptome-wide analysis uncovers the targets of the RNA-binding protein MSI2 and effects of MSI2's RNA-binding activity on IL-6 signaling 
    J. Biol. Chem. 293, 15359-15369 (2018) 
  • 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) 
  • Orr AA, Shaykhalishahi H, Mirecka EA, Jonnalagadda SVR, Hoyer W, Tamamis P 
    Elucidating the multi-targeted anti-amyloid activity and enhanced islet amyloid polypeptide binding of β-wrapins 
    Comput. Chem. Eng. 116, 322-332 (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) 
  • Wördehoff M, Hoyer W 
    α-Synuclein aggregation monitored by Thioflavin T fluorescence assay 
    Bio Protoc. 8, e2941 (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) 
  • Wördehoff M, Shaykhalishahi H, Groß L, Gremer L, Stoldt M, Buell AK, Willbold D, Hoyer W 
    Opposed effects of dityrosine formation in soluble and aggregated α-synuclein on fibril growth 
    J. Mol. Biol. 429, 3018-3030 (2017) 
  • Mirecka EA, Feuerstein S, Gremer L, Schröder GF, Stoldt M, Willbold D, Hoyer W. 
    β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor 
    Sci. Rep. 6, 33474 (2016) 
  • Orr AA, Wördehoff MM, Hoyer W, Tamamis P 
    Uncovering the binding and specificity of β-wrapins for amyloid-β and α-synuclein 
    J. Phys. Chem. B 120, 12781-12794 (2016) 
  • 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) 
  • Brener O, Dunkelmann T, Gremer L, van Groen T, Mirecka EA, Kadish I, Willuweit A, Kutzsche J, Jürgens D, Rudolph S, Tusche M, Bongen P, Pietruszka J, Oesterhelt F, Langen K-J, Demuth H-U, Janssen A, Hoyer W, Funke SA, Nagel-Steger L, Willbold D 
    QIAD assay for quantitating a compound's efficacy in elimination of toxic Aβ oligomers. 
    Sci Rep 5, 13222 (2015) 
  • Shaykhalishahi H, Gauhar A, Wördehoff MM, Grüning CS, Klein A, Bannach O, Stoldt M, Willbold D, Härd T, Hoyer W 
    Contact between the beta1 and beta2 segments of alpha-synuclein that inhibits amyloid formation 
    Angew. Chem. Int. Ed. 54, 8837-8840 (2015) 
  • Shaykhalishahi H, Mirecka EA, Gauhar A, Grüning CSR, Willbold D, Härd T, Stoldt M, Hoyer W 
    A beta-hairpin-binding protein for three different disease-related amyloidogenic proteins 
    ChemBioChem 16, 411-414 (2015) 
  • Wördehoff MM, Bannach O, Shaykhalishahi H, Kulawik A, Schiefer S, Willbold D, Hoyer W, Birkmann E 
    Single fibril growth kinetics of alpha-synuclein. 
    J. Mol. Biol. 427, 1428-1435 (2015) 
  • Gauhar A, Shaykhalishahi H, Gremer L, Mirecka EA, Hoyer W 
    Impact of subunit linkages in an engineered homodimeric binding protein to alpha-synuclein 
    Protein Eng. Des. Sel. 27, 473-479 (2014) 
  • Grüning CS, Mirecka EA, Klein AN, Mandelkow E, Willbold D, Marino SF, Stoldt M, Hoyer W 
    Alternative conformations of the tau repeat domain in complex with an engineered binding protein 
    J. Biol. Chem. 289, 23209-23218 (2014) 
  • Mirecka EA, Gremer L, Schiefer S, Oesterhelt F, Stoldt M, Willbold D, Hoyer W 
    Engineered aggregation inhibitor fusion for production of highly amyloidogenic human islet amyloid polypeptide 
    J. Biotechnol. 191, 221-227 (2014) 
  • Mirecka EA, Shaykhalishahi H, Gauhar A, Akgül S, Lecher J, Willbold D, Stoldt M, Hoyer W 
    Sequestration of a beta-hairpin for control of alpha-synuclein aggregation 
    Angew. Chem. Int. Ed. 53, 4227-4230 (2014) 
  • Grüning CS, Klinker S, Wolff M, Schneider M, Toksöz K, Klein AN, Nagel-Steger L, Willbold D, Hoyer W 
    The off-rate of monomers dissociating from amyloid-beta protofibrils 
    J. Biol. Chem. 288, 37104-37111 (2013) 
  • Luheshi LM, Hoyer W, de Barros TP, van Dijk-Härd I, Brorsson AC, Macao B, Persson C, Crowther DC, Lomas DA, Ståhl S, Dobson CM, Härd T 
    Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo 
    PLoS Biol. 8, e1000334 (2010) 
  • Hoyer W, Grönwall C, Jonsson A, Ståhl S, Härd T 
    Stabilization of a beta-hairpin in monomeric Alzheimer’s amyloid-beta peptide inhibits amyloid formation 
    Proc. Natl. Acad. Sci. USA 105, 5099-5104 (2008) 
  • Hoyer W, Härd T 
    Interaction of Alzheimer’s Abeta peptide with an engineered binding protein - Thermodynamics and kinetics of coupled folding-binding 
    J. Mol. Biol. 378, 398-411 (2008) 
  • Macao B, Hoyer W, Sandberg A, Brorsson AC, Dobson CM, Härd T 
    Recombinant amyloid beta-peptide production by coexpression with an affibody ligand 
    BMC Biotechnol. 8, 82 (2008) 
  • Bertoncini CW, Jung YS, Fernández CO, Hoyer W, Griesinger C, Jovin TM, Zweckstetter M 
    Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein 
    Proc. Natl. Acad. Sci. USA 102, 1430-1435 (2005) 
  • 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) 
  • Rasia RM, Bertoncini CW, Marsh D, Hoyer W, Cherny D, Zweckstetter M, Griesinger C, Jovin TM, Fernández, CO 
    Structural characterization of copper (II) binding to alpha-synuclein: New insights into the bioinorganic chemistry of Parkinson’s disease 
    Proc. Natl. Acad. Sci. USA 102, 4294-4299 (2005) 
  • Cherny D, Hoyer W, Subramaniam V, Jovin TM 
    Double-stranded DNA stimulates the fibrillation of alpha-synuclein in vitro and is associated with the mature fibrils. An electron microscopy study 
    J. Mol. Biol. 344, 929-938 (2004) 
  • Fernández CO, Hoyer W, Zweckstetter M, Jares-Erijman EA, Subramaniam V, Griesinger C, Jovin TM 
    NMR of alpha-synuclein complexes with polyamines elucidates the mechanism and kinetics of induced aggregation 
    EMBO J. 23, 2039-2046 (2004) 
  • Hoyer W, Cherny D, Subramaniam V, Jovin TM 
    Impact of the acidic C-terminal region aa109-140 on alpha-synuclein aggregation in vitro 
    Biochemistry 43, 16233-16242 (2004) 
  • Hoyer W, Cherny D, Subramaniam V, Jovin TM 
    Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy 
    J. Mol. Biol. 340, 127-139 (2004) 
  • Masarik M, Stobiecka A, Kizek R, Jelen F, Pechan Z, Hoyer W, Jovin TM, Subramaniam V, Palecek E 
    Sensitive electrochemical detection of native and aggregated alpha-synuclein protein involved in Parkinson's disease 
    Electroanalysis 16, 1172-1181 (2004) 
  • Antony T, Hoyer W, Cherny D, Heim G, Jovin TM, Subramaniam V 
    Cellular polyamines promote the aggregation of alpha-synuclein 
    J. Biol. Chem. 278, 3235-3240 (2003) 
  • Hoyer W, Antony T, Cherny D, Heim G, Jovin TM, Subramaniam V 
    Dependence of alpha-synuclein aggregate morphology on solution conditions 
    J. Mol. Biol. 322, 383-393 (2002) 
  • Hoyer W, Ramm K, Plückthun, A 
    A kinetic trap is an intrinsic feature in the folding pathway of single-chain Fv fragments 
    Biophys. Chem. 96, 273-284 (2002) 
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