Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Hanna Willander"'
Publikováno v:
Prion. 6:498-509
The cellular prion protein (PrP (C) ) is attached to the cell membrane via its glycosylphosphatidylinositol (GPI)-anchor and is constitutively shed into the extracellular space. Here, three different mechanisms are presented that concurrently shed Pr
Autor:
Jan-Bernd Stukenborg, Michael Landreh, Olle Söder, Hanna Willander, Jan Johansson, Hans Jörnvall
Publikováno v:
Biochemical and Biophysical Research Communications. 418:489-493
Insulin aggregation can prevent rapid insulin uptake and cause localized amyloidosis in the treatment of type-1 diabetes. In this study, we investigated the effect of C-peptide, the 31-residue peptide cleaved from proinsulin, on insulin fibrillation
Publikováno v:
FEBS Journal. 278:3893-3904
The BRICHOS domain was initially defined from sequence alignments of the Bri protein associated with familial dementia, chondromodulin associated with chondrosarcoma and surfactant protein C precursor (proSP-C) associated with respiratory distress sy
Publikováno v:
Biochemical and Biophysical Research Communications. 402:515-518
Amyloid consists of β-sheet polymers and is associated with disease and with functional assemblies. Amyloid-forming proteins differ widely in native structures and sequences. We describe here how conformational preferences of non-polar amino acid re
Autor:
Hanna Willander, Michael Landreh, Jan-Bernd Stukenborg, Hans Jörnvall, Gunvor Alvelius, Jan Johansson, Olle Söder
Publikováno v:
The FEBS journal. 279(24)
Proinsulin processing into insulin and C-peptide in the secretory granules of the pancreatic β-cells occurs under mildly acidic conditions and at high peptide concentrations (> 10 mm). Mature insulin has reduced solubility and a propensity to adopt
Autor:
Stefan D. Knight, Glareh Askarieh, Jenny Presto, Henrik Biverstål, Jan Johansson, Hanna Willander, Sara Linse, Birgitta Frohm
Publikováno v:
The Journal of biological chemistry. 287(37)
Amyloid diseases such as Alzheimer, Parkinson, and prion diseases are associated with a specific form of protein misfolding and aggregation into oligomers and fibrils rich in β-sheet structure. The BRICHOS domain consisting of ∼100 residues is fou
Publikováno v:
Alzheimer's & Dementia. 8
Autor:
Hanna Willander, Per Westermark, Michael Landreh, Aaron Hamvas, Jenny Presto, Johan Åqvist, Hans Jörnvall, Henrik Keränen, Glareh Askarieh, Tomas Bergman, Helena Berglund, Lawrence M. Nogee, Stefan D. Knight, Jan Johansson, Cristina Casals, Alejandra Sáenz, Erik Hermansson, Kerstin Nordling
BRICHOS domains are encoded in > 30 human genes, which are associated with cancer, neurodegeneration, and interstitial lung disease (ILD). The BRICHOS domain from lung surfactant protein C proprotein (proSP-C) is required for membrane insertion of SP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b9bea3053a271a05660e6acf4869cef
https://europepmc.org/articles/PMC3289314/
https://europepmc.org/articles/PMC3289314/
Autor:
Jenny Presto, Erik Hermansson, Sara Linse, Stefan D. Knight, G. Askarieh, Hanna Willander, Jan Johansson
Publikováno v:
Alzheimer's & Dementia. 7
Publikováno v:
The FEBS journal. 278(20)
The BRICHOS domain was initially defined from sequence alignments of the Bri protein associated with familial dementia, chondromodulin associated with chondrosarcoma and surfactant protein C precursor (proSP-C) associated with respiratory distress sy