Zobrazeno 1 - 10
of 161
pro vyhledávání: '"WESTLIND DANIELSSON, A"'
Autor:
Nilsberth, Camilla, Westlind-Danielsson, Anita, Eckman, Christopher B., Condron, Margaret M., Axelman, Karin, Forsell, Charlotte, Stenh, Charlotte, Luthman, Johan, Teplow, David B., Younkin, Steven G., Näslund, Jan, Lannfelt, Lars
Publikováno v:
Nature Neuroscience. Sep2001, Vol. 4 Issue 9, p887. 7p.
Publikováno v:
Scandinavian Journal of Clinical and Laboratory Investigation. 67:179-190
There are an increasing number of genetic and neuropathological observations to suggest that cystatin C, an extracellular protein produced by all nucleated cells, might play a role in the pathophysiology of sporadic Alzheimer's disease (AD). Recent o
Autor:
Maj-Linda Bardyl Selenica, Anita Westlind-Danielsson, Marianne Schultzberg, Catharina Lindberg
Publikováno v:
Journal of Molecular Neuroscience. 27:001-012
Activated microglia represent a major source of inflammatory factors in Alzheimer's disease and a possible source of cytotoxic factors. beta-Amyloid (Abeta) peptide, the predominant component in amyloid plaques, has been shown to activate microglia a
Publikováno v:
Journal of Molecular Biology. 339:145-159
A new early-onset form of Alzheimer's disease (AD) was described recently where a point mutation was discovered in codon 693 of the beta-amyloid (Abeta) precursor protein gene, the Arctic mutation. The mutation translates into a single amino acid sub
Autor:
Jan Näslund, Charlotte Stenh, Karin Axelman, Anita Westlind-Danielsson, Steven G. Younkin, Margaret M. Condron, Charlotte Forsell, Lars Lannfelt, David B. Teplow, Camilla Nilsberth, Christopher B. Eckman, Johan Luthman
Publikováno v:
Nature Neuroscience. 4:887-893
Several pathogenic Alzheimer's disease (AD) mutations have been described, all of which cause increased amyloid beta-protein (Abeta) levels. Here we present studies of a pathogenic amyloid precursor protein (APP) mutation, located within the Abeta se
Publikováno v:
Analytical Chemistry. 73:2625-2631
A novel method for the determination of the enantiomeric composition of peptides is presented. In this paper, the focus has been on beta-amyloid peptides from deceased Alzheimer's disease patients. The peptides are hydrolyzed using mineral acid. The