Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Martina Radli"'
Publikováno v:
PLoS ONE, Vol 12, Iss 6, p e0180047 (2017)
The molecular chaperone Hsp90 is an essential member of the cellular proteostasis system. It plays an important role in the stabilisation and activation of a large number of client proteins and is involved in fatal disease processes, e.g. Alzheimer d
Externí odkaz:
https://doaj.org/article/7c4440e1eb984fe2a62dd6edc3b580f7
Publikováno v:
PLoS ONE, Vol 8, Iss 10, p e77257 (2013)
Mutations in the central region of the signalling hub Adenomatous Polyposis Coli (APC) cause colorectal tumourigenesis. The structure of this region remained unknown. Here, we characterise the Mutation Cluster Region in APC (APC-MCR) as intrinsically
Externí odkaz:
https://doaj.org/article/5cd39db0b268435caffa635467081b0a
The formation of fibrillar tangles of the Tau protein is crucial in the development of Alzheimer’s disease. Biophysical methods based on labelling of the cysteines of Tau with fluorescence dyes would allow to study fibril formation with an ‘inter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cf9a4eb2168faac446e8e027a285230
https://doi.org/10.1101/211904
https://doi.org/10.1101/211904
Autor:
Eckhard Mandelkow, Markus Zweckstetter, Afonso M.S. Duarte, Tatiana Didenko, Tania Morán Luengo, Stefan G.D. Rüdiger, G. Elif Karagöz, Tobias Madl, Chad A. Dickey, Hans Ippel, Bryce A. Nordhues, Jacek Biernat, Rolf Boelens, Elias Akoury, Martina Radli, Dmitry B. Veprintsev
Publikováno v:
Cell
Cell, 156(5), 963-974. Cell Press
Europe PubMed Central
Cell 156(5), 963-974 (2014). doi:10.1016/j.cell.2014.01.037
Cell 156, 963-974 (2014)
Cell, 156(5), 963. Cell Press
Cell, 156(5), 963-974. Cell Press
Europe PubMed Central
Cell 156(5), 963-974 (2014). doi:10.1016/j.cell.2014.01.037
Cell 156, 963-974 (2014)
Cell, 156(5), 963. Cell Press
Protein folding in the cell relies on the orchestrated action of conserved families of molecular chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding path, yet the molecular basis of this timing is enigmatic, mainly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c71a1240dfd843ee70b399e9af2ba17a
https://doi.org/10.1016/j.cell.2014.01.037
https://doi.org/10.1016/j.cell.2014.01.037