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) https://doi.org/10.3390/ijms24032161
Gomes CM, Hoyer W, Luo J Editorial: The biochemistry of amyloids in neurodegenerative diseases, volume II Front Neurosci 17, 1236518 (2023) https://doi.org/10.3389/fnins.2023.1236518
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) https://doi.org/10.3390/ijms242216132
Muschol M, Hoyer W Amyloid oligomers as on-pathway precursors or off-pathway competitors of fibrils Front Mol Biosci 10, 1120416 (2023) https://doi.org/10.3389/fmolb.2023.1120416
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) https://doi.org/10.3390/diagnostics13101702
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) https://doi.org/10.1016/j.bbadva.2023.100110
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) https://doi.org/10.3390/biom12030469
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) https://doi.org/10.1002/chem.202200456
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) https://doi.org/10.1038/s41467-022-30042-y
Törner R, Kupreichyk T, Hoyer W, Boisbouvier J The role of heat shock proteins in preventing amyloid toxicity Front Mol Biosci 9, 1045616 (2022) https://doi.org/10.3389/fmolb.2022.1045616
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) https://doi.org/10.1016/j.bpc.2020.106519
Gomes CM, Hoyer W, Luo J Editorial: The Biochemistry of Amyloids in Neurodegenerative Diseases, Volume I Front Neurosci 15, 819481 (2021) https://doi.org/10.3389/fnins.2021.819481
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) https://doi.org/10.1002/anie.202010098
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
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) https://doi.org/10.1515/hsz-2020-0207
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) https://doi.org/10.1038/s41467-021-24900-4
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) https://doi.org/10.3389/fnins.2021.696440
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
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) https://doi.org/10.1039/D0SC04051G
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) https://doi.org/10.1039/D0CB00086H
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) https://doi.org/10.1038/s42003-020-1085-z
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) https://doi.org/10.7554/eLife.46112
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) https://doi.org/10.1016/j.chemphyslip.2019.02.009
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) https://doi.org/10.1021/acs.jpcb.9b02338
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) https://doi.org/10.1074/jbc.RA118.002243
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
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) https://doi.org/10.1016/j.compchemeng.2018.02.013
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
Wördehoff M, Hoyer W α-Synuclein aggregation monitored by Thioflavin T fluorescence assay Bio Protoc. 8, e2941 (2018) https://doi.org/10.21769/BioProtoc.2941
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) https://dx.doi.org/10.1021/acs.jpcb.6b08485
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
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) http://dx.doi.org/10.1038/srep13222
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) http://dx.doi.org/10.1002/anie.201503018
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) http://dx.doi.org/10.1002/cbic.201402552
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) http://dx.doi.org/10.1093/protein/gzu047
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) http://dx.doi.org/10.1074/jbc.M114.560920
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) http://dx.doi.org/10.1016/j.jbiotec.2014.06.006
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) http://dx.doi.org/10.1074/jbc.M113.513432
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)