Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Philip J B Koeck"'
Autor:
Gefei Chen, Axel Abelein, Harriet E. Nilsson, Axel Leppert, Yuniesky Andrade-Talavera, Simone Tambaro, Lovisa Hemmingsson, Firoz Roshan, Michael Landreh, Henrik Biverstål, Philip J. B. Koeck, Jenny Presto, Hans Hebert, André Fisahn, Jan Johansson
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
The BRICHOS domain is a chaperone that can act against amyloid-β peptide fibril formation and non-fibrillar protein aggregation. Here the authors use a multidisciplinary approach and show that the Bri2 BRICHOS domain has qualitatively different chap
Externí odkaz:
https://doaj.org/article/54f4eca3feec44a6b3d1e292c044e1a5
Autor:
Xueying Zhong, Rakesh Kumar, Yu Wang, Henrik Biverstål, Caroline Ingeborg Jegerschöld, Philip J B Koeck, Jan Johansson, Axel Abelein, Gefei Chen
Publikováno v:
ACS Chemical Biology. 17:2201-2211
Amyloid-β peptide (Aβ) aggregation is one of the hallmarks of Alzheimer's disease (AD). Mutations in Aβ are associated with early onset familial AD, and the Arctic mutant E22G (Aβ
Autor:
Gefei, Chen, Yuniesky, Andrade-Talavera, Xueying, Zhong, Sameer, Hassan, Henrik, Biverstål, Helen, Poska, Axel, Abelein, Axel, Leppert, Nina, Kronqvist, Anna, Rising, Hans, Hebert, Philip J B, Koeck, André, Fisahn, Jan, Johansson
Publikováno v:
RSC chemical biology. 3(11)
Proteins can self-assemble into amyloid fibrils or amorphous aggregates and thereby cause disease. Molecular chaperones can prevent both these types of protein aggregation, but to what extent the respective mechanisms are overlapping is not fully und
Autor:
Sergio, Trillo-Muyo, Harriet E, Nilsson, Christian V, Recktenwald, Anna, Ermund, Caroline, Ridley, Lauren N, Meiss, Andrea, Bähr, Nikolai, Klymiuk, Jeffrey J, Wine, Philip J B, Koeck, David J, Thornton, Hans, Hebert, Gunnar C, Hansson
Publikováno v:
The Journal of Biological Chemistry
Most MUC5B mucin polymers in the upper airways of humans and pigs are produced by submucosal glands. MUC5B forms N-terminal covalent dimers that are further packed into larger assemblies because of low pH and high Ca2+ in the secretory granule of the