Zobrazeno 1 - 3
of 3
pro vyhledávání: '"ultrastructure [Neurofibrillary Tangles]"'
Autor:
Michel, C. H., Kumar, S., Pinotsi, D., Tunnacliffe, A., St. George-Hyslop, P., Mandelkow, E., Mandelkow, E.-M., Kaminski, C. F., Kaminski Schierle, G. S.
Publikováno v:
The Journal of Biological Chemistry
Journal of Biological Chemistry
The journal of biological chemistry 289(2), 956-967 (2013). doi:10.1074/jbc.M113.515445
Journal of Biological Chemistry
The journal of biological chemistry 289(2), 956-967 (2013). doi:10.1074/jbc.M113.515445
Background: The aggregation and stereotypic spreading of Tau protein is associated with Alzheimer disease. Results: Monomeric Tau enters neurons and nucleates and engages endogenous Tau to aggregate. Conclusion: Endocytosis of soluble Tau triggers ag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::f0fdf02f62a1c6798f3141c249adb75f
https://pubmed.ncbi.nlm.nih.gov/24235150
https://pubmed.ncbi.nlm.nih.gov/24235150
Autor:
Adam Lange, Christian Griesinger, Venita Daebel, Antoine Loquet, Birgit Habenstein, Vinesh Vijayan, Markus Zweckstetter, Eckhard Mandelkow, Martin Schwalbe, Henrik Müller, Subashchandrabose Chinnathambi, Elias Akoury, Jacek Biernat, Katharina Tepper, Marc Baldus
Publikováno v:
Journal of the American Chemical Society 134(34), 13982-13989 (2012). doi:10.1021/ja305470p
Journal of the American Chemical Society
Journal of the American Chemical Society
One of the hallmarks of Alzheimer's disease is the self-assembly of the microtubule-associated protein tau into fibers termed "paired helical filaments" (PHFs). However, the structural basis of PHF assembly at atomic detail is largely unknown. Here,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::687614ad6618c210c7fb21ce69d0dd98
https://pub.dzne.de/record/136609
https://pub.dzne.de/record/136609
Autor:
Mitsuru Kawai, George Perry, Sandra L. Siedlak, Patrick Cras, Jennifer Vande Weghe, Massimo Tabaton, Barry D. Greenberg
The neurotrophic activity of beta-amyloid protein (beta-AP) has been suggested to be responsible for the dystrophic neurites that surround beta-AP deposits in senile plaques of Alzheimer disease. The recent finding that neurofibrillary tangles (NFT)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7fe81992dcfa6c6d50e15751b70fbff
http://hdl.handle.net/11567/301693
http://hdl.handle.net/11567/301693