Fändrich, Marcus, Tito, Mark A., Leroux, Michel R., Rostom, Adam A., Hartl, F. Ulrich, Dobson, Christopher M., ...
We have analyzed a newly described archaeal GimC/prefoldin homologue, termed MtGimC, by using nanoflow electrospray coupled with time-of-flight MS. The molecular weight of the complex from...
The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
Fändrich, Marcus, Dobson, Christopher M.
Amyloid fibrils and prions are proteinaceous aggregates that are based on a unique form of polypeptide configuration, termed cross-β structure. Using a group of chemically distinct polyamino acids,...
Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments
Fändrich, Marcus, Forge, Vincent, Buder, Katrin, Kittler, Marlis, Dobson, Christopher M., Diekmann, Stephan
Observations that β-sheet proteins form amyloid fibrils under at least partially denaturing conditions has raised questions as to whether these fibrils assemble by docking of preformed β-structure...
Raft lipids as common components of human extracellular amyloid fibrils
Gellermann, Gerald P., Appel, Thomas R., Tannert, Astrid, Radestock, Anja, Hortschansky, Peter, Schroeckh, Volker, ...
Amyloid fibrils are fibrillar polypeptide aggregates from several degenerative human conditions, including Alzheimer's and Creutzfeldt-Jakob diseases. Analysis of amyloid fibrils derived from various...
Fändrich, Marcus, Tito, Mark A., Leroux, Michel R., Rostom, Adam A., Hartl, F. Ulrich, Dobson, Christopher M., ...
We have analyzed a newly described archaeal GimC/prefoldin homologue, termed MtGimC, by using nanoflow electrospray coupled with time-of-flight MS. The molecular weight of the complex from...
The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
Fändrich, Marcus, Dobson, Christopher M.
Amyloid fibrils and prions are proteinaceous aggregates that are based on a unique form of polypeptide configuration, termed cross-β structure. Using a group of chemically distinct polyamino acids,...
Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments
Fändrich, Marcus, Forge, Vincent, Buder, Katrin, Kittler, Marlis, Dobson, Christopher M., Diekmann, Stephan
Observations that β-sheet proteins form amyloid fibrils under at least partially denaturing conditions has raised questions as to whether these fibrils assemble by docking of preformed β-structure...
Raft lipids as common components of human extracellular amyloid fibrils
Gellermann, Gerald P., Appel, Thomas R., Tannert, Astrid, Radestock, Anja, Hortschansky, Peter, Schroeckh, Volker, ...
Amyloid fibrils are fibrillar polypeptide aggregates from several degenerative human conditions, including Alzheimer's and Creutzfeldt-Jakob diseases. Analysis of amyloid fibrils derived from various...
Peim, Alexander, Hortschansky, Peter, Christopeit, Tony, Schroeckh, Volker, Richter, Walter, Fändrich, Marcus
Amyloid formation is a nucleation-dependent process that is accelerated dramatically in vivo and in vitro upon addition of appropriate fibril seeds. A potent species barrier can be effective in this...
Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer’s β-amyloid variants
Hortschansky, Peter, Christopeit, Tony, Schroeckh, Volker, Fändrich, Marcus
We have determined the critical concentrations of a set of 18 variants of Alzheimer’s Aβ(1–40) peptide, each carrying a different residue at position 18. We find that the critical concentrations...
The aggregation kinetics of Alzheimer’s β-amyloid peptide is controlled by stochastic nucleation
Hortschansky, Peter, Schroeckh, Volker, Christopeit, Tony, Zandomeneghi, Giorgia, Fändrich, Marcus
We report here a recombinant expression system that allows production of large quantities of Alzheimer’s Aβ(1–40) peptide. The material is competent to dissolve in water solutions with...
Mutagenic analysis of the nucleation propensity of oxidized Alzheimer’s β-amyloid peptide
Christopeit, Tony, Hortschansky, Peter, Schroeckh, Volker, Gührs, Karlheinz, Zandomeneghi, Giorgia, Fändrich, Marcus
The formation of polypeptide aggregates represents a nucleated polymerization reaction in which an initial nucleation event (lag phase) is followed by the extension of newly formed nuclei into larger...
FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils
Zandomeneghi, Giorgia, Krebs, Mark R.H., McCammon, Margaret G., Fändrich, Marcus
The presence of β-sheets in the core of amyloid fibrils raised questions as to whether or not β-sheet-containing proteins, such as transthyretin, are predisposed to form such fibrils. However, we...
Similarities in the thermodynamics and kinetics of aggregation of disease-related Aβ(1–40) peptides
Meinhardt, Jessica, Tartaglia, Gian Gaetano, Pawar, Amol, Christopeit, Tony, Hortschansky, Peter, Schroeckh, Volker, ...
Increasing evidence indicates that polypeptide aggregation often involves a nucleation and a growth phase, although the relationship between the factors that determine these two phases has not yet...
Habicht, Gernot, Haupt, Christian, Friedrich, Ralf P., Hortschansky, Peter, Sachse, Carsten, Meinhardt, Jessica, ...
The formation of amyloid fibrils is a common biochemical characteristic that occurs in Alzheimer's disease and several other amyloidoses. The unifying structural feature of amyloid fibrils is their...
Aβ Mediated Diminution of MTT Reduction—An Artefact of Single Cell Culture?
Rönicke, Raik, Klemm, Anja, Meinhardt, Jessica, Schröder, Ulrich H., Fändrich, Marcus, Reymann, Klaus G.
The 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-tetrazoliumbromide (MTT) reduction assay is a frequently used and easily reproducible method to measure beta-amyloid (Aβ) toxicity in different types of...
Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy
Sachse, Carsten, Fändrich, Marcus, Grigorieff, Nikolaus
Alzheimer's disease is a neurodegenerative disorder that is characterized by the cerebral deposition of amyloid fibrils formed by Aβ peptide. Despite their prevalence in Alzheimer's and other...