Several funded PhD positions are available or will become available at our institute in 2019. Please send an application consisting of cover letter, c.v. and certificates, preferably combined into one PDF document to the following email address bewerbung-pbc(at)uni-ulm.de. The position will initially be filled for 2 years with a possibility for an extension. Incoming mails will be viewed from 1 March 2019 onwards. Positions will be filled as soon as possible. Applications for self-funded projects are also welcome.
Cryo-EM structure of an amyloid fibril from systemic amyloidosis. Falk Liberta, Sarah Loerch, Matthies Rennegarbe, Angelika Schierhorn, Per Westermark, Gunilla T Westermark, Nikolaus Grigorieff, Marcus Fandrich, Matthias Schmidt, BioRxiv https://www.biorxiv.org/content/10.1101/357129v1
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)
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)
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
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