Zobrazeno 1 - 10
of 88
pro vyhledávání: '"Angelika Schierhorn"'
Autor:
Marius Kollmer, William Close, Leonie Funk, Jay Rasmussen, Aref Bsoul, Angelika Schierhorn, Matthias Schmidt, Christina J. Sigurdson, Mathias Jucker, Marcus Fändrich
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
Alzheimer’s disease is characterised by the deposition of Aβ amyloid fibrils and tau protein neurofibrillary tangles. Here the authors use cryo-EM to structurally characterise brain derived Aβ amyloid fibrils and find that they are polymorphic an
Externí odkaz:
https://doaj.org/article/bd15cbb55e35470c93b5f854aad34b44
Autor:
Falk Liberta, Sarah Loerch, Matthies Rennegarbe, Angelika Schierhorn, Per Westermark, Gunilla T. Westermark, Bouke P. C. Hazenberg, Nikolaus Grigorieff, Marcus Fändrich, Matthias Schmidt
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Systemic AA amyloidosis is caused by misfolding of the acute phase protein serum amyloid A1. Here the authors present the cryo-EM structures of murine and human AA amyloid fibrils that were isolated from tissue samples and describe how the fibrils di
Externí odkaz:
https://doaj.org/article/a47ab7cd22cf43a58ce79e21f975d4b7
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-8 (2017)
Abstract Amyloid A (AA) amyloidosis is a systemic protein misfolding disease affecting humans and other vertebrates. While the protein precursor in humans and mice is the acute-phase reactant serum amyloid A (SAA) 1.1, the deposited fibrils consist m
Externí odkaz:
https://doaj.org/article/b27108d49c674c0499766e0c7a5184f5
Autor:
Anna Katharina Weyrauch, Mario Jakob, Angelika Schierhorn, Ralf Bernd Klösgen, Dariush Hinderberger
Publikováno v:
PLoS ONE, Vol 12, Iss 9, p e0184968 (2017)
Histidine-Proline-rich Glycoprotein (HPRG) is a plasma protein of vertebrates and several marine bivalves. Due to its multidomain structure consisting of several regions HPRG can interact with a variety of ligands, however the exact physiological rol
Externí odkaz:
https://doaj.org/article/3f482dfe3d654a16a3e61ba040a84fda
Publikováno v:
International Journal of Molecular Sciences, Vol 17, Iss 10, p 1687 (2016)
Spider dragline is used by many members of the Araneae family not only as a proteinogenic safety thread but also for web construction. Spider dragline has been shown to possess high tensile strength in combination with elastic behavior. This high ten
Externí odkaz:
https://doaj.org/article/db24c1ba17364300a65be796d44e6d49
Autor:
Anna Schildbach, Markus Pietzsch, Udo Reichl, Angelika Schierhorn, Erdmann Rapp, Jan Klapproth, Reza Mahour, Thomas Rexer
Publikováno v:
Biotechnology and Bioengineering
Glycosylation of proteins is a key function of the biosynthetic‐secretory pathway in the endoplasmic reticulum (ER) and Golgi apparatus. Glycosylated proteins play a crucial role in cell trafficking and signaling, cell‐cell adhesion, blood‐grou
Autor:
Marie-Theres Vielberg, Karl-Heinz Gührs, Andreas Schmidt, Rolf Koehler, Stefan Schönland, Marcus Fändrich, Angelika Schierhorn, Matthias Schmidt, William Close, Hauke Lilie, Falk Liberta, Christian Haupt, Ute Hegenbart, Karthikeyan Annamalai, Michael Groll
Publikováno v:
Angewandte Chemie. 129:7618-7622
Systemic amyloidosis is caused by the misfolding of a circulating amyloid precursor protein and the deposition of amyloid fibrils in multiple organs. Chemical and biophysical analysis of amyloid fibrils from human AL and murine AA amyloidosis reveal
Autor:
Michael Spinka, Stephan König, Robert Pertermann, Tom Reichenbach, Elena Bergner, Anne-Kathrin Blume, Philipp Zimmermann, Christiane Ehrt, Sebastian Seiferheld, Angelika Schierhorn
Publikováno v:
Biochemistry. 56:1285-1298
The catalytic activity of the allosteric enzyme pyruvate decarboxylase from yeast is strictly controlled by its own substrate pyruvate via covalent binding at a separate regulatory site. Kinetic studies, chemical modifications, cross-linking, small-a
Autor:
Jay Rasmussen, Leonie Funk, Marcus Fändrich, Aref Bsoul, Christina J. Sigurdson, Mathias Jucker, Angelika Schierhorn, Marius Kollmer, Matthias Schmidt, William Close
Publikováno v:
Nature Communications
Nature Communications 10(1), 4760 (2019). doi:10.1038/s41467-019-12683-8
Nature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
Nature Communications 10(1), 4760 (2019). doi:10.1038/s41467-019-12683-8
Nature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
The formation of Aβ amyloid fibrils is a neuropathological hallmark of Alzheimer’s disease and cerebral amyloid angiopathy. However, the structure of Aβ amyloid fibrils from brain tissue is poorly understood. Here we report the purification of A
Arginine methylation enhances the RNA chaperone activity of the West Nile virus host factor AUF1 p45
Autor:
Uwe G. Liebert, Ralph Golbik, Susann Friedrich, Grit Szczepankiewicz, Sven-Erik Behrens, Tobias Schmidt, Angelika Schierhorn, Sandra Bergs, Hauke Lilie
Publikováno v:
RNA. 22:1574-1591
A prerequisite for the intracellular replication process of the Flavivirus West Nile virus (WNV) is the cyclization of the viral RNA genome, which enables the viral replicase to initiate RNA synthesis. Our earlier studies indicated that the p45 isofo