The amyloid-β degradation intermediate Aβ34 is pericyte-associated and reduced in brain capillaries of patients with Alzheimer’s disease

Autor: Tunahan Kirabali, Serena Rigotti, Alessandro Siccoli, Filip Liebsch, Adeola Shobo, Christoph Hock, Roger M. Nitsch, Gerhard Multhaup, Luka Kulic

Publikováno v: Acta Neuropathologica Communications, Vol 7, Iss 1, Pp 1-14 (2019)

Abstract An impairment of amyloid β-peptide (Aβ) clearance is suggested to play a key role in the pathogenesis of sporadic Alzheimer’s disease (AD). Amyloid degradation is mediated by various mechanisms including fragmentation by enzymes like nep

Externí odkaz: https://doaj.org/article/47910761693948dea8c5d3ea5f4deee8

Biallelic gephyrin variants lead to impaired GABAergic inhibition in a patient with developmental and epileptic encephalopathy

Autor: Arthur Macha, Florian Hetsch, Patrick Van Bogaert, Borislav Dejanovic, Steffen Fricke, Franziska Neuser, Jose Angel Santamaria-Araujo, Vanessa Kress, Filip Liebsch, Lena Johannes, Alec Aeby, Catheline Vilain, Sarah Weckhuysen, Guenter Schwarz, Tania Djémié, Jochen C. Meier

Publikováno v: Human molecular genetics

Synaptic inhibition is essential for shaping the dynamics of neuronal networks, and aberrant inhibition is linked to epilepsy. Gephyrin (Geph) is the principal scaffolding protein at inhibitory synapses and is essential for postsynaptic clustering of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::180886e444ed6f6878cab9428fe64b24
https://doi.org/10.1093/hmg/ddab298

Aβ34 is a BACE1-derived degradation intermediate associated with amyloid clearance and Alzheimer’s disease progression

Autor: Paul Saftig, Peter Kunach, Randall J. Bateman, Wiesje M. van der Flier, Philip Scheltens, Judes Poirier, John C.S. Breitner, Pedro Rosa-Neto, Mark A. Hancock, Christoph Hock, Vivienne Engelschalt, Filip Liebsch, Adeola Shobo, Charlotte E. Teunissen, Irem Ulku, Gerhard Multhaup, Luka Kulic

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
Nature Communications, 10(1):2240. Nature Publishing Group
Nature Communications
Liebsch, F, Kulic, L, Teunissen, C, Shobo, A, Ulku, I, Engelschalt, V, Hancock, M A, van der Flier, W M, Kunach, P, Rosa-Neto, P, Scheltens, P, Poirier, J, Saftig, P, Bateman, R J, Breitner, J, Hock, C & Multhaup, G 2019, ' Aβ34 is a BACE1-derived degradation intermediate associated with amyloid clearance and Alzheimer’s disease progression ', Nature Communications, vol. 10, no. 1, 2240 . https://doi.org/10.1038/s41467-019-10152-w

The beta-site APP cleaving enzyme 1 (BACE1) is known primarily for its initial cleavage of the amyloid precursor protein (APP), which ultimately leads to the generation of Aβ peptides. Here, we provide evidence that altered BACE1 levels and activity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bf630cd51ee1f2a56bef962775e7fbd
http://link.springer.com/article/10.1038/s41467-019-10152-w

The amyloid-β degradation intermediate Aβ34 is pericyte-associated and reduced in brain capillaries of patients with Alzheimer’s disease

Autor: Christoph Hock, Roger M. Nitsch, Luka Kulic, Serena Rigotti, Alessandro Siccoli, Gerhard Multhaup, Adeola Shobo, Filip Liebsch, Tunahan Kirabali

Publikováno v: Acta Neuropathologica Communications, Vol 7, Iss 1, Pp 1-14 (2019)
Acta Neuropathologica Communications

An impairment of amyloid β-peptide (Aβ) clearance is suggested to play a key role in the pathogenesis of sporadic Alzheimer’s disease (AD). Amyloid degradation is mediated by various mechanisms including fragmentation by enzymes like neprilysin,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1439ab702f2cd4b1048d9408d59db96e
https://doi.org/10.1186/s40478-019-0846-8

Full-length cellular β-secretase has a trimeric subunit stoichiometry, and its sulfur-rich transmembrane interaction site modulates cytosolic copper compartmentalization

Autor: Rikard Blunck, Filip Liebsch, Gerd Multhaup, Silvia Scolari, Tobias Bethge, Hugo McGuire, Derek Bowie, Mark R. P. Aurousseau, Andreas Herrmann

Publikováno v: Journal of Biological Chemistry. 292:13258-13270

The β-secretase (BACE1) initiates processing of the amyloid precursor protein (APP) into Aβ peptides, which have been implicated as central players in the pathology of Alzheimer disease. BACE1 has been described as a copper-binding protein and its

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31e2dbb3a70c9321dc90a77c81ff8bdf
https://doi.org/10.1074/jbc.m117.779165