Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Krzysztof Paliga"'
Autor:
Krzysztof Paliga, Alex Schneede, Jürgen Scheller, Stefan Rose-John, Jessica Gewiese, Lina Fleig, Karsten Krieger, Athena Chalaris
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1803(2):234-245
Interleukin-6 (IL6) signals are mediated by classic and trans-signaling. In classic signaling, IL6 first binds to the membrane bound Interleukin-6 Receptor (IL6R) whereas in trans-signaling, IL6 acts via a soluble form of the IL6R. Trans-signaling vi
Autor:
Björn Rabe, Krzysztof Paliga, Simon Arnett Jones, Stefan Rose-John, Ceri Alan Fielding, Athena Chalaris, Jürgen Scheller, Tamas Laskay, Hans Lange
Publikováno v:
Blood. 110:1748-1755
Interleukin 6 (IL6) trans-signaling has emerged as a prominent regulator of immune responses during both innate and acquired immunity. Regulation of IL6 trans-signaling is reliant upon the release of soluble IL6 receptor (sIL6R), which binds IL6 to c
Autor:
Konrad Beyreuther, Simone Eggert, Genevieve Evin, Peter Soba, Krzysztof Paliga, Andreas Weidemann, Colin L. Masters
Publikováno v:
Journal of Biological Chemistry. 279:18146-18156
Amyloid precursor protein (APP) processing is of major interest in Alzheimer's disease research, since sequential cleavages by β- and γ-secretase lead to the formation of the 4-kDa amyloid Aβ protein peptide that accumulates in Alzheimer's disease
Autor:
Friedrich B M Reinhard, Krzysztof Paliga, Konrad Beyreuther, Simone Eggert, Genevieve Evin, Andreas Weidemann, Markus Vogel, Colin L. Masters, Gottfried Baier
Publikováno v:
Biochemistry. 41:2825-2835
Proteolytic processing of the transmembrane domain of the amyloid precursor protein (APP) is a key component of Alzheimer's disease pathogenesis. Using C-terminally tagged APP derivatives, we have identified by amino-terminal sequencing a novel cleav
Publikováno v:
Neurochemistry International. 36:175-184
The Alzheimer's disease amyloid protein precursor (APP) gene is part of a multi-gene super-family from which sixteen homologous amyloid precursor-like proteins (APLP) and APP species homologues have been isolated and characterised. Comparison of exon
Identification of cis-Elements Regulating Exon 15 Splicing of the Amyloid Precursor Protein Pre-mRNA
Publikováno v:
Journal of Biological Chemistry. 275:2046-2056
Alternative splicing of exon 15 of the amyloid precursor protein (APP) pre-mRNA generates two APP isoform groups APP(ex15) (containing exon 15) and L-APP (without exon 15), which show a cell-specific distribution in non-neuronal cells and neurons of
Autor:
Andreas Weidemann, Colin L. Masters, Krzysztof Paliga, Friedrich B M Reinhard, Genevieve Evin, Oliver Schuckert, Ulrike Dürrwang
Publikováno v:
Journal of Biological Chemistry. 274:5823-5829
Alzheimer's disease is characterized by neurodegeneration and deposition of betaA4, a peptide that is proteolytically released from the amyloid precursor protein (APP). Missense mutations in the genes coding for APP and for the polytopic membrane pro
Autor:
Alexander Schulte, S. Rose John, J. Achilles, Christian Hundhausen, Michael G. Andrzejewski, Andreas Ludwig, S. Mletzko, Krzysztof Paliga, Christian Weber, Karina Reiss, Beate Schulz
Publikováno v:
Biochemical and biophysical research communications. 358(1)
The chemokines CX3CL1/Fractalkine and CXCL16 are expressed as transmembrane molecules and can mediate cell-cell-adhesion. By proteolytic processing, CX3CL1 and CXCL16 are released from the cell surface by proteolytic shedding resulting in the generat
Autor:
Friedrich B M Reinhard, Genevieve Evin, Andreas Weidemann, Dai Zhang, Colin L. Masters, Ulrike Dürrwang, Krzysztof Paliga, Konrad Beyreuther, Rupert Sandbrink
The genes encoding presenilin-1 (PS1) and presenilin-2 (PS2) were identified as the genes that harbour mutations that cause more than 60% of early onset familial Alzheimer's disease cases (FAD) (1-3). So far, more than 40 missense mutations have been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::631d0d33eb60be4b791285841cb9418f
https://doi.org/10.1385/1-59259-195-7:333
https://doi.org/10.1385/1-59259-195-7:333
Autor:
Dennis J. Selkoe, W. Taylor Kimberly, Dominic M. Walsh, Simone Eggert, Julia V. Fadeeva, Krzysztof Paliga, Matthew J. LaVoie, Wilma Wasco
Publikováno v:
Biochemistry. 42(22)
Regulated intramembrane proteolysis (RIP) of the amyloid precursor protein (APP) produces amyloid beta-protein (Abeta), the probable causative agent of Alzheimer's disease (AD), and is therefore an important target for therapeutic intervention. Howev