Selected Publications

Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis Radamaker, L, Lin Y-H, Annamalai K, Huhn S, Hegenbart U, Schönland SO, Fritz G, Schmidt M, Fändrich M. Nature Comm. 10, 1103 (2019)

Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids Liberta F, Loerch S, Rennegarbe M, Schierhorn A, Westermark P, Westermark GT, Hazenberg BPC, Grigorieff N, Fändrich M, Schmid M. Nature Comm. 10, 1104 (2019)

Physical basis of amyloid fibril polymorphism. Close W, Neumann M, Schmidt A, Hora M, Annamalai K, Schmidt M, Reif B, Schmidt V, Grigorieff N, Fändrich M. Nature Comm. 9, 699 (2018)

Serum amyloid A forms stable oligomers that disrupt vesicles at lysosomal pH and contribute to the pathogenesis of reactive amyloidosis. Jayaraman S, Gantz, DL, Haupt C, Gursky O. Proc. Natl. Acad. Sci. U.S.A. 114, E6507-E6515 (2017)

Cellular mechanism of fibril formation from serum amyloid A1 protein. Claus S, Meinhardt K, Aumüller T, Puscalau-Girtu I, Linder J, Haupt C, Walther P, Syrovets T, Simmet T, Fändrich M. EMBO Rep. 18, 1352-1366 (2017)

Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo. Annamalai K, Liberta F, Vielberg M-T, Close W, Lilie H, Gührs K-H, Schierhorn A, Koehler R, Schmidt A, Haupt C, Hegenbart U, Schönland S, Schmidt M, Groll M, Fändrich M Angew Chem Int Ed 56, 7618–7622 (2017)

Hydrostatic pressure increases the catalytic activity of amyloid fibril enzymes. Luong TQ, Erwin N, Neumann M, Schmidt A, Loos C, Schmidt V, Fändrich M, Winter R Angewandte Chemie Int. Ed. 2016, 55, 12412–12416                                         

Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril. Schmidt A, Annamalai K, Schmidt M, Grigorieff N, Fändrich M Proc Natl Acad Sci U.S.A. 2016, 113, 6200-6205                                                      

Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits. Kollmer M, Meinhardt K, Haupt C, Liberta F, Wulff M, Linder J, Handl L, Heinrich L, Loos C, Schmidt M, Syrovets T, Simmet T, Westermark P, Westermark GT, Horn U,  Schmidt V, Walther P, Fändrich M. Proc Natl Acad Sci U.S.A. 2016, 113, 5604-5609

Enhanced Fibril Fragmentation of N-Terminally Truncated and Pyroglutamyl-Modified Aβ Peptide. Wulff M, Baumann M, Thümmler A, Yadav JK, Heinrich L, Knüpfer U, Schlenzig D, Schierhorn A,  Rahfeld JU, Horn U, Balbach J, Demuth HU, Fändrich M Angewandte Chemie Int. Ed. 2016, 55, 5081-5084                                                             

Polymorphism of amyloid fibrils in vivo. Annamalai K, Gührs KH, Koehler R, Schmidt M, Michel H, Loos C, Gaffney PM, Sigurdson CJ, Hegenbart U, Schönland S, Fändrich M Angewandte Chemie Int. Ed. 2016, 55, 4822–4825                                                           

Age-dependent defects of alpha-synuclein oligomer uptake in microglia and monocytes. Bliederhaeuser C, Grozdanov V, Speidel A, Zondler L, Ruf WP, Bayer H, Kiechle M, Feiler MS, Freischmidt A, Brenner D, Witting A, Hengerer B, Fändrich M, Ludolph AC, Weishaupt JH, Gillardon F, Danzer KM Acta Neuropathol. 2016, 131, 379-391

Peptide Dimer Structure in an Aß(1-42) Fibril Visualized with Cryo-EM. Schmidt M, Rohou A, Lasker K, Yadav JK, Schiene-Fischer C, Fändrich M, Grigorieff N Proc Natl Acad Sci U.S.A. 2015, 112, 11858-11863

AA Amyloidosis: Pathogenesis and Targeted Therapy. Westermark GT, Fändrich M, Westermark P Annu. Rev. Pathol. Mech. Dis. 2015, 10, 321–344

Protein aggregation in Alzheimer’s disease: Aß and τ and their potential roles in the pathogenesis of AD. Thal DR, Fändrich M Acta Neuropathol 2015, 129, 163–165

Neuropathology and biochemistry of Aß and its aggregates in Alzheimer’s disease. Thal DR, Walter J, Saido TC, Fändrich M Acta Neuropathol 2015, 129, 167–182

Structure and biomedical applications of amyloid oligomer nanoparticles. Kumar ST, Meinhardt J, Fuchs AK, Aumüller T, Leppert J, Büchele B, Knüpfer U, Ramachandran R, Yadav JK, Prell E, Morgado I, Ohlenschläger O, Horn U, Simmet T, Görlach M, Fändrich M ACS Nano 2014, 25, 8(11), 11042-52

Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen. Usmani S, Zirafi O, Müller J, Sandi-Monroy N, Yadav JK, Meier C, Weil T, Roan NR, Greene WC, Walther P, Nilsson KPR, Hammerström P, Wetzel R, Gagsteiger F, Fändrich M, Kirchhoff F, Münch J Nature Communications 2014, 5, Article number: 3508

Protein chemistry: Catalytic amyloid fibrils. Aumüller T, Marcus F Nature Chemistry 2014, 6, 273–274

Biotechnologically engineered protein binders for applications in amyloid diseases. Haupt C, Fändrich M Trends in Biotechnology 2014, 32, 513–520

Biochemical stages amyloid β-protein aggregation and accumulation in the human brain and its association with symptomatic and preclinical Alzheimer's disease. Upadhaya AR, Kosterin I, Kumar S, von Arnim CAF, Yamaguchi H, Fändrich M, Walter J, Thal DR Brain 2014, 137, 887-903

Molecular Basis of β-Amyloid Oligomer Binding and Inhibition with a Conformation-Specific Antibody Fragment. Morgado I, Wieligmann K, Bereza M, Rönicke R, Meinhardt K, Wacker J, Hortschansky P, Malešević M, Parthier C, Schiene-Fischer C, Reymann KG, Stubbs MT, Görlach M, Horn U, Fändrich M, Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 12503–12508

An asymmetric dimer is the basic subunit in Alzheimer's disease β-amyloid fibrils. Lopez del Amo JM, Schmidt M, Fink U, Muralidar Dasari M, Fändrich M, Reif B Angewandte Chemie Int. Edt. 2012, 51, 6136-6139

Structural basis of Aβ-dependent synaptic dysfunctions. Christian Haupt C, Leppert J, Rönicke R, Meinhardt J, Yadav JK, Ramachandran R, Ohlenschläger O, Reymann KG, Görlach M, Fändrich M Angewandte Chemie Int. Edt. 2012, 51, 1576-1579

An orcein-related small molecule promotes the conversion of toxic oligomersto non-toxic, beta-sheet-rich amyloid fibrils. Bieschke J, Herbst M, Wiglenda T, Friedrich RP, Boeddrich A, Schiele F, Kleckers D, Lopez de Vega JM, Grüning B, Wang Q, Schmidt MR, Lurz R, Anwyl R, Schnoegl S, Fändrich M, Frank RF, Reif B, Günther S, Walsh DM, Wanker EE Nature Chem. Biol. 2012, 8, 93–101

Solid-State NMR of Aβ Protofibrils Implies a β-Sheet Remodelling upon Maturation into Terminal Amyloid Fibrils. Scheidt HA, Morgado I, Rothemund S, Huster D, Fändrich M. Angewandte Chemie Int. Edt. 2011, 50, 2837 –2840

Recent progress in understanding Alzheimer’s β-amyloid structures (Review). Fändrich M, Schmidt M, Grigorieff N Trends in Biochem. Scie., 2011, 36, 338-345

Assembly of Alzheimer's Aβ peptide into nanostructured amyloid fibrils (Review). Morgado I, Fändrich M Current Opinion in Colloid and Interface Science, 2011, 16, 508–514

Nanoscale flexibility parameters of Alzheimer amyloid fibrils determined using electron cryo-microscopy. Sachse C, Grigorieff N, Fändrich M Angewandte Chemie Int. Edt. 2010, 49, 1321 –1323

Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity. Friedrich RP, Tepper K, Rönicke R, Westermann M, Reymann K, Kaether C, Fändrich M Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 1942–1947

Comparison between Alzheimer's Ab(1-40) and Ab(1-42) amyloid fibrils reveals similar protofilament structures. Schmidt M, Sachse C, Richer W, Xu C, Fändrich M, Grigorieff N Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 19813–19818

Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy. Sachse C, Fändrich M, Grigorieff N Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 7462–7466

Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Ab protofibrils. Habicht G, Haupt C, Friedrich RP, Hortschansky P, Sachse C, Meinhardt J, Wieligmann K, Gellermann GP, Brodhun M, Götz J, Halbhuber KJ, Röcken C, Horn U, Fändrich M Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 19232–19237

Review: On the structural definition of amyloid fibrils and other polypeptide aggregates. Fändrich M Cell. Mol. Life Sci. 2007, 64, 2066-2078

Raft lipids as common components of human extracellular amyloid fibrils. Gellermann GP Appel TR, Tannert A, Radestock A, Hortschansky  P, Schroeckh V, Leisner C Lütkepohl T, Shtrasburg S, Röcken C, Pras M, Linke RP, Diekmann S, Fändrich M Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 6297–6302