Affiliation: Institute of Molecular Biotechnology
- The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleationPeter Hortschansky
Institut für Molekulare Biotechnologie IMB, Jena, Germany
Protein Sci 14:1753-9. 2005..These data imply that the nucleation event is under influence of a stochastic factor that can manifest itself in profound macroscopic differences in the aggregation kinetics of otherwise indistinguishable samples...
- The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formationMarcus Fändrich
Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, South Parks Road, UK
EMBO J 21:5682-90. 2002....
- Apomyoglobin reveals a random-nucleation mechanism in amyloid protofibril formationMarcus Fändrich
Institut für Molekulare Biotechnologie IMB, Beutenbergstrasse 11, Postfach 100 813, D 07708 Jena, Germany
Acta Histochem 108:215-9. 2006..Once the appropriate structural characteristics are acquired, PFs are formed by addition of further polypeptide chains...
- Myoglobin forms amyloid fibrils by association of unfolded polypeptide segmentsMarcus Fändrich
Institut fur Molekulare Biotechnologie, Beutenbergstrasse 11, D 07745 Jena, Germany
Proc Natl Acad Sci U S A 100:15463-8. 2003..However, it is inevitable that such conditions often stabilize protein folding intermediates...
- Structure and formation of amyloid fibrilsMarcus Fändrich
Institute of Molecular Biotechnology, Jena, Germany
Acta Histochem 105:379. 2003
- Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptidesJessica Meinhardt
Leibniz Institut für Altersforschung, Fritz Lipmann Institut, D 07745 Jena, Germany
Protein Sci 16:1214-22. 2007....
- Mutagenic exploration of the cross-seeding and fibrillation propensity of Alzheimer's beta-amyloid peptide variantsAlexander Peim
Leibniz Institut für Altersforschung, Jena, Germany
Protein Sci 15:1801-5. 2006..Hence, the nucleus acts in this case as a catalyst that promotes the fibrillation of different polypeptide chains according to their intrinsic structural predilection...
- Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer's beta-amyloid variantsPeter Hortschansky
Leibniz Institut für Naturstoff Forschung une Infektionsbiologie, Hans Knöll Institut, D 07745 Jena, Germany
Protein Sci 14:2915-8. 2005....
- Alzheimer-like plaque formation by human macrophages is reduced by fibrillation inhibitors and lovastatinGerald P Gellermann
Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstrasse 11, D 07745 Jena, Germany
J Mol Biol 360:251-7. 2006....
- Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's abeta(1-40) amyloid fibrilsKarolin Klement
Leibniz Institut für Altersforschung, Beutenbergstrasse 11, D 07745 Jena, Germany
J Mol Biol 373:1321-33. 2007..These observations are important for understanding and predicting aggregation on the basis of simple physico-chemical properties...
- FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrilsGiorgia Zandomeneghi
Institut für Molekulare Biotechnologie IMB, D 07745 Jena, Germany
Protein Sci 13:3314-21. 2004..These data imply that amyloid fibril formation from native beta-sheet proteins can involve a substantial structural reorganization...
- Absolute correlation between lag time and growth rate in the spontaneous formation of several amyloid-like aggregates and fibrilsMarcus Fändrich
Leibniz Institut für Altersforschung, Fritz Lipmann Institut, Beutenbergstrasse 11, D 07745 Jena, Germany
J Mol Biol 365:1266-70. 2007..These data suggest mechanistic similarities in the nucleation behaviour of different amyloid-like fibrils and aggregates...
- Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrilsJessica Meinhardt
Leibniz Institut für Altersforschung Fritz Lipmann Institut, Beutenbergstrabetae 11, D 07745 Jena, Germany
J Mol Biol 386:869-77. 2009..This property differs significantly from native, monomeric protein folding reactions that produce, for one protein sequence, only one ordered conformation and only one set of inter-residue interactions...
- Raft lipids as common components of human extracellular amyloid fibrilsGerald P Gellermann
Institut fur Molekulare Biotechnologie, Beutenbergstrasse 11, 07745 Jena, Germany
Proc Natl Acad Sci U S A 102:6297-302. 2005..These data suggest the existence of common cellular mechanisms in the generation of different types of clinical amyloid deposits...
- Identification of molecular compounds critical to Alzheimer's-like plaque formationGerald P Gellermann
Leibniz Institute for Age Research, Fritz Lipmann Institut, Jena, Germany
J Neurosci Res 85:2037-44. 2007..Altogether, our data demonstrate the utility of this cell model for investigating pathways and molecular interactions critical to amyloidogenesis...
- Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's beta-amyloid peptideTony Christopeit
Institut fur Molekulare Biotechnologie, D 07745 Jena, Germany
Protein Sci 14:2125-31. 2005..These data imply that the two reactions, nucleation and polymerization, are governed by very similar physicochemical principles and that they involve the formation of the same types of noncovalent interactions...