Zobrazeno 1 - 6
of 6
pro vyhledávání: '"physiology [Amyloid beta-Protein Precursor]"'
Autor:
Alfredo Cáceres, Alfredo Lorenzo, Mariana Oksdath, Sebastian Dupraz, Santiago Quiroga, Lucas J. Sosa
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Journal of neurochemistry 143(1), 11-29 (2017). doi:10.1111/jnc.14122
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Journal of neurochemistry 143(1), 11-29 (2017). doi:10.1111/jnc.14122
The amyloid precursor protein (APP) is a type I transmembrane glycoprotein better known for its participation in the physiopathology of Alzheimer disease as the source of the beta amyloid fragment. However, the physiological functions of the full len
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::896ff31cec0fbc31ea05c790ee709a59
Wiley Online Library
Wiley Online Library
Autor:
Matthew E. Kennedy, Peer-Hendrik Kuhn, Stefan F. Lichtenthaler, Philip C. Wong, Robert Vassar, Lawrence Rajendran, Christian Haass
Publikováno v:
Journal of neurochemistry 130(1), 4-28 (2014). doi:10.1111/jnc.12715
Journal of Neurochemistry
Journal of Neurochemistry
The β-site APP cleaving enzymes 1 and 2 (BACE1 and BACE2) were initially identified as transmembrane aspartyl proteases cleaving the amyloid precursor protein (APP). BACE1 is a major drug target for Alzheimer's disease because BACE1-mediated cleavag
Publikováno v:
PLoS ONE
PLOS ONE 10(3), e0119768 (2015). doi:10.1371/journal.pone.0119768
PLoS ONE, Vol 10, Iss 3, p e0119768 (2015)
PLOS ONE 10(3), e0119768 (2015). doi:10.1371/journal.pone.0119768
PLoS ONE, Vol 10, Iss 3, p e0119768 (2015)
In Alzheimer's disease (AD), hallmark β-amyloid deposits are characterized by the presence of activated microglia around them. Despite an extensive characterization of the relation of amyloid plaques with microglia, little is known about the initiat
Autor:
Christian K.E. Jung, Jochen Herms
Publikováno v:
Experimental brain research 217(3-4), 463-470 (2011). doi:10.1007/s00221-011-2939-x
The amyloid precursor protein (APP) is transported in high amounts to the presynaptic endings where its function is still unknown. Several studies indicate that lack of APP or its overexpression affects the number of dendritic spines, the postsynapti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02550205364dc201122124ba90642327
Autor:
Richard M. Page, Harald Steiner, Christian Haass, Edith Winkler, Amelie Gutsmiedl, Akio Fukumori
Publikováno v:
The journal of biological chemistry 285(23), 17798-17810 (2010). doi:10.1074/jbc.M110.103283
Pathogenic generation of the 42-amino acid variant of the amyloid beta-peptide (Abeta) by beta- and gamma-secretase cleavage of the beta-amyloid precursor protein (APP) is believed to be causative for Alzheimer disease (AD). Lowering of Abeta(42) pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a16d16ae5dbab15510628cded650e667
Autor:
Steffen Burgold, Tobias Bittner, Harald Steiner, Gerda Mitteregger, Christian Haass, Christiane Volbracht, Hans A. Kretzschmar, Christian K.E. Jung, Jochen Herms, Martin Fuhrmann
Publikováno v:
Journal of Neuroscience; Vol 29
The journal of neuroscience 29(33), 10405-10409 (2009). doi:10.1523/JNEUROSCI.2288-09.2009
The journal of neuroscience 29(33), 10405-10409 (2009). doi:10.1523/JNEUROSCI.2288-09.2009
Alzheimer's disease (AD) represents the most common age-related neurodegenerative disorder. It is characterized by the invariant accumulation of the β-amyloid peptide (Aβ), which mediates synapse loss and cognitive impairment in AD. Current therape