Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Birgitta Frohm"'
Publikováno v:
PLoS ONE, Vol 7, Iss 2, p e32254 (2012)
Nano-sized (10(-9)-10(-7) m) particles offer many technical and biomedical advances over the bulk material. The use of nanoparticles in cosmetics, detergents, food and other commercial products is rapidly increasing despite little knowledge of their
Externí odkaz:
https://doaj.org/article/f33dbfe8e2fa43ff86d3b62194b2f6eb
Autor:
Tanja Weiffert, Christopher J.R. Dunning, Kaj Blennow, David Klenerman, Tuomas P. J. Knowles, Henrik Zetterberg, Erik Portelius, Georg Meisl, Suman De, Sara Linse, Birgitta Frohm, Patrick Flagmeier, Christopher M. Dobson
Publikováno v:
ACS Chemical Neuroscience. 10:2374-2384
Aggregation of the amyloid-β (Aβ) peptide into plaques is believed to play a crucial role in Alzheimer's disease. Amyloid plaques consist of fibrils of full length Aβ peptides as well as N-terminally truncated species. β-Site amyloid precursor pr
Autor:
Tuomas P. J. Knowles, Ulyana Shimanovich, Aviad Levin, Sara Linse, Zenon Toprakcioglu, Karin S. Åkerfeldt, Thomas C. T. Michaels, Birgitta Frohm, Dror Eliaz, Erwin De Genst
Publikováno v:
Small (Weinheim an der Bergstrasse, Germany). 17(26)
Peptides and proteins have evolved to self-assemble into supramolecular entities through a set of non-covalent interactions. Such structures and materials provide the functional basis of life. Crucially, biomolecular assembly processes can be highly
Autor:
Dev, Thacker, Kalyani, Sanagavarapu, Birgitta, Frohm, Georg, Meisl, Tuomas P J, Knowles, Sara, Linse
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Alzheimer’s disease affects a rapidly growing number of individuals worldwide. Key unresolved questions relate to the onset and propagation of the disease, linked to the self-assembly of amyloid β peptide into fibrillar and smaller ag
Autor:
Tuomas P. J. Knowles, Henrik Zetterberg, Tommy Cedervall, Sara Linse, Mattias Törnquist, Thom Leiding, Kaj Blennow, Oskar Hansson, Rebecca Frankel, Ulf Andreasson, Georg Meisl, Birgitta Frohm
Publikováno v:
Communications Biology, Vol 2, Iss 1, Pp 1-11 (2019)
Communications Biology
Communications Biology
Funder: Knut och Alice Wallenbergs Stiftelse (Knut and Alice Wallenberg Foundation); doi: https://doi.org/10.13039/501100004063
Funder: Alzheimerfonden; doi: https://doi.org/10.13039/501100008599
Alzheimer’s disease is linked to amyloid
Funder: Alzheimerfonden; doi: https://doi.org/10.13039/501100008599
Alzheimer’s disease is linked to amyloid
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance The aggregation of the amyloid-β (Aβ) peptide into amyloid fibrils is associated with Alzheimer’s disease, and several point mutations leading to early-onset disease have been identified in Aβ. By studying the aggregation of five di
Autor:
Birgitta Frohm, Yongchao Su, Michael T. Colvin, Robert G. Griffin, Sara Linse, Robert Silvers
Publikováno v:
Journal of the American Chemical Society
The presence of amyloid plaques composed of amyloid beta (Aβ) fibrils is a hallmark of Alzheimer's disease (AD). The Aβ peptide is present as several length variants with two common alloforms consisting of 40 and 42 amino acids, denoted Aβ1-40 and
Autor:
Johan Malm, Ulf Olsson, Karin S. Åkerfeldt, Sara Linse, Birgitta Frohm, J E DeNizio, Luigi Gentile, David Lee
Publikováno v:
Soft Matter. 11:414-421
The peptide GSFSIQYTYHV derived from human semenogelin I forms a transparent hydrogel through spontaneous self-assembly in water at neutral pH. Linear rheology measurements demonstrate that the gel shows a dominating elastic response over a large fre
Autor:
Tuomas P. J. Knowles, Katja Bernfur, Risto Cukalevski, Birgitta Frohm, Georg Meisl, Ulrich Weininger, Sara Linse, Xiaoting Yang
Publikováno v:
Chemical Science. 6:4215-4233
The assembly of proteins into amyloid fibrils, a phenomenon central to several currently incurable human diseases, is a process of high specificity that commonly tolerates only a low level of sequence mismatch in the component polypeptides. However,
Autor:
Tuomas P. J. Knowles, Samuel I. A. Cohen, Birgitta Frohm, Christopher M. Dobson, Georg Meisl, Erik Hellstrand, Xiaoting Yang, Sara Linse, Julius B. Kirkegaard
Publikováno v:
Proceedings of the National Academy of Sciences. 111:9384-9389
The two major forms of the amyloid-beta (Aβ) peptide found in plaques in patients suffering from Alzheimer's disease, Aβ40 and Aβ42, only differ by two amino acids in the C-terminal region, yet they display markedly different aggregation behavior.