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Your search keyword '"Bayer, Thomas"' showing total 11 results
Start Over Author "Bayer, Thomas" Journal journal of biological chemistry
11 results on '"Bayer, Thomas"'

4. Identification of Low Molecular Weight Pyroglutamate Aβ Oligomers in Alzheimer Disease

Author

Wirths, Oliver, primary, Erck, Christian, additional, Martens, Henrik, additional, Harmeier, Anja, additional, Geumann, Constanze, additional, Jawhar, Sadim, additional, Kumar, Sathish, additional, Multhaup, Gerd, additional, Walter, Jochen, additional, Ingelsson, Martin, additional, Degerman-Gunnarsson, Malin, additional, Kalimo, Hannu, additional, Huitinga, Inge, additional, Lannfelt, Lars, additional, and Bayer, Thomas A., additional

Published
2010
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6. Sortilin-related Receptor with A-type Repeats (SORLA) Affects the Amyloid Precursor Protein-dependent Stimulation of ERK Signaling and Adult Neurogenesis

Author

Rohe, Michael, primary, Carlo, Anne-Sophie, additional, Breyhan, Henning, additional, Sporbert, Anje, additional, Militz, Daniel, additional, Schmidt, Vanessa, additional, Wozny, Christian, additional, Harmeier, Anja, additional, Erdmann, Bettina, additional, Bales, Kelly R., additional, Wolf, Susanne, additional, Kempermann, Gerd, additional, Paul, Steven M., additional, Schmitz, Dietmar, additional, Bayer, Thomas A., additional, Willnow, Thomas E., additional, and Andersen, Olav M., additional

Published
2008
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11. Alzheimer beta-amyloid homodimers facilitate A beta fibrillization and the generation of conformational antibodies.

Author

Schmechel A, Zentgraf H, Scheuermann S, Fritz G, Pipkorn R, Reed J, Beyreuther K, Bayer TA, and Multhaup G

Subjects
Amyloid beta-Peptides genetics, Amyloid beta-Peptides ultrastructure, Circular Dichroism, Dimerization, Humans, Microscopy, Electron, Neurofibrillary Tangles pathology, Neurofibrillary Tangles ultrastructure, Peptide Fragments chemistry, Peptide Fragments ultrastructure, Protein Structure, Secondary, Amyloid beta-Peptides chemistry
Abstract

We reported previously that stabilized beta-amyloid peptide dimers were derived from mutant amyloid precursor protein with a single cysteine in the ectodomain juxtamembrane position. In vivo studies revealed that two forms of SDS-stable A beta homodimers exist, species ending at A beta 40 and A beta 42. The phenomenon of the transformation of the initially deposited 42-residue beta-amyloid peptide into the amyloid fibrils of Alzheimer's disease plaques remains to be explained in physical terms, i.e. energetically and structurally. We therefore performed spectroscopic analyses revealing that engineered dimeric peptides ending at residue 42 displayed a much more pronounced beta-structural transition than corresponding monomers. Specifically, the single chemically induced dimerization of A beta peptides significantly increased the beta-sheet content by a factor of 2. The C-terminal residues Ile-41 and Ala-42 of dimeric forms further increased the beta-sheet content by roughly one-third. In contrast to A beta 42, the beta-sheet content of the alpha- and gamma-secretase-generated p3 fragments did not necessarily correlate with the tendency to form fibrils, although p3/17-42 had a pronounced thread forming character with fibril lengths of up to 2.5 microM. Electron microscopic images show that forms of p3/17-42 generated smaller granular particles than forms ending at residue 40. We discuss these findings in terms of A beta 1-42 dimers representing paranuclei, which self-aggregate into ribbon-like ordered fibrils by elongation. Based on A beta 42 dimer-specific titers of a polyclonal antiserum we propose that the A beta homodimer represents a nidus for plaque formation and a well defined novel therapeutic target.

Published
2003
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