Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Christian Barucker"'
Autor:
Georg Beckmann, Peter St George-Hyslop, Oliver Peters, Lili-Naz Hazrati, Veit Althoff, Murat Eravci, Anette Sommer, Thomas Dyrks, Gerhard Multhaup, John C.S. Breitner, Damian Brockschnieder, Carola G. Schipke, Christian Barucker, Paul E. Fraser, Anja Harmeier
Publikováno v:
Journal of Alzheimer's Disease. 44:613-624
The pathogenesis of Alzheimer's disease (AD) is characterized by the aggregation of amyloid-{beta} (A{beta}) peptides leading to deposition of senile plaques and a progressive decline of cognitive functions, which currently remains the main criterion
Publikováno v:
ChemBioChem. 13:2657-2660
Aggregation of amyloid β (Aβ(1-42)), causing toxicity, is a critical step in Alzheimer's disease (AD). AD studies are difficult to compare because Aβ(1-42) aggregation is poorly controllable under physiological conditions. To control aggregation a
Autor:
Mark A. Hancock, Francois Charron, Dietmar Schmitz, Paul Dembny, Shireen Hossain, Peter W. Hildebrand, Yong Rao, Jürgen P. Rabe, Philip K.-Y. Chang, Heiko J. Bittner, Gerhard Multhaup, Rudi Lurz, Christian Barucker, Hunter Shaw, Wei Zhuang, Manuel Gensler, R. Anne McKinney, Anja Harmeier, Filip Liebsch, Scott A. Cameron
Publikováno v:
Scientific reports 5(1), 15410 (2015). doi:10.1038/srep15410
Scientific Reports
Scientific Reports
The amyloid-β42 (Aβ42) peptide is believed to be the main culprit in the pathogenesis of Alzheimer disease (AD), impairing synaptic function and initiating neuronal degeneration. Soluble Aβ42 oligomers are highly toxic and contribute to progressiv
Publikováno v:
The FASEB Journal. 29
Objectives: The transmembrane sequence (TMS) of APP (Aβ residues 29 to 49) is a key determinant of Aβ42 oligomerization and toxicity, with G33 being the critical residue (Harmeier et al., 2009). A ...
Autor:
Beatrix Fauler, Rudi Lurz, Kai Frederik Albring, Joerg Weiske, Peter W. Hildebrand, Stefan Prokop, Gerhard Multhaup, Christian Barucker, Frank L. Heppner, Otmar Huber, Anja Harmeier
Publikováno v:
The Journal of Biological Chemistry
Although soluble species of the amyloid-β peptide Aβ42 correlate with disease symptoms in Alzheimer disease, little is known about the biological activities of amyloid-β (Aβ). Here, we show that Aβ peptides varying in lengths from 38 to 43 amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d8bcdf01803608e7d3f94f8e945a66a
https://hdl.handle.net/11858/00-001M-0000-0029-CB57-811858/00-001M-0000-0029-CB55-C
https://hdl.handle.net/11858/00-001M-0000-0029-CB57-811858/00-001M-0000-0029-CB55-C
Autor:
Michael Schaefer, Linda Schauenburg, Daniela Kaden, Manuel E. Than, Gerhard Multhaup, Dirk Roeser, Christian Barucker, Magnus C. Mayer, Philipp Voigt, Mark A. Hancock
Publikováno v:
The Journal of biological chemistry. 289(27)
The amyloid precursor protein (APP) and the APP-like proteins 1 and 2 (APLP1 and APLP2) are a family of multidomain transmembrane proteins possessing homo- and heterotypic contact sites in their ectodomains. We previously reported that divalent metal
Autor:
Gerd Multhaup, Wei Zhuang, Manuel Gensler, Rudi Lurz, Benjamin R. Rost, Christian Barucker, Peter W. Hildebrand, Dietmar Schmitz, Anja Harmeier, Jürgen P. Rabe, Michael Beyermann
Publikováno v:
Alzheimer's & Dementia. 7
Autor:
Joerg Weiske, Kai Frederik Albring, Christian Barucker, Anja Harmeier, Gerd Multhaup, Otmar Huber
Publikováno v:
Alzheimer's & Dementia. 6