Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Bettina Griesshaber"'
Autor:
Götz Ehlerding, Wolfgang Ries, Manuela Kempkes-Koch, Ekkehard Ziegler, Petra Ronová, Mária Krizsán, Jana Verešová, Mária Böke, Ansgar Erlenkötter, Robert Nitschel, Adam M. Zawada, James P. Kennedy, Jennifer Braun, John W. Larkin, Natalia Korolev, Thomas Lang, Bertram Ottillinger, Manuela Stauss-Grabo, Bettina Griesshaber
Publikováno v:
BMC Nephrology, Vol 25, Iss 1, Pp 1-12 (2024)
Abstract Background Hemodialyzers should efficiently eliminate small and middle molecular uremic toxins and possess exceptional hemocompatibility to improve well-being of patients with end-stage kidney disease. However, performance and hemocompatibil
Externí odkaz:
https://doaj.org/article/4b66a40a5a4e402184c83ded7f823087
Autor:
Peter W Janes, Sabine H Wimmer-Kleikamp, Achilleas S Frangakis, Kane Treble, Bettina Griesshaber, Ola Sabet, Markus Grabenbauer, Alice Y Ting, Paul Saftig, Philippe I Bastiaens, Martin Lackmann
Publikováno v:
PLoS Biology, Vol 7, Iss 10, p e1000215 (2009)
Release of cell surface-bound ligands by A-Disintegrin-And-Metalloprotease (ADAM) transmembrane metalloproteases is essential for signalling by cytokine, cell adhesion, and tyrosine kinase receptors. For Eph receptor ligands, it provides the switch b
Externí odkaz:
https://doaj.org/article/208a197eb2a04790bf321370e02d3201
Autor:
Lena Rauber, Sebastian Zschätzsch, Stephan Wagner, Manuela Kempkes-Koch, Ansgar Erlenkötter, Adelheid Gauly, Manuela Stauss-Grabo, Götz Ehlerding, Adam M Zawada, Wolfgang Ries, James Kennedy, Hans Schmidt-Gürtler, Bettina Griesshaber
Publikováno v:
Kidney360
BACKGROUND: High-flux dialyzers effectively remove uremic toxins, are hemocompatible to minimize intradialytic humoral and cellular stimulation, and have long-term effects on patient outcomes. A new dialyzer with a modified membrane surface has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a9657abd3624e0f0070c2262618a188
https://pubmed.ncbi.nlm.nih.gov/35373083
https://pubmed.ncbi.nlm.nih.gov/35373083
Autor:
Peter W. Janes, Andrew W. Boyd, Tony Pawson, Bryan W. Day, Claus Jørgensen, Linda L. Hii, Philippe I. H. Bastiaens, Anneloes Mensinga, Bettina Griesshaber, Martin Lackmann, Chanly Chheang, Eva Nievergall, Lakmali Atapattu
Publikováno v:
The Journal of Cell Biology
Beyond homotypic receptor interactions that are required for Eph signaling, ligand-independent association and crosstalk between members of the EphA and -B subclasses determine cell signaling outcomes.
Eph receptors interact with ephrin ligands
Eph receptors interact with ephrin ligands
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::827806ed9bca07bdccb4dceb2d613405
https://pubmed.ncbi.nlm.nih.gov/22144690
https://pubmed.ncbi.nlm.nih.gov/22144690
Autor:
Eckhard Mandelkow, Bettina Griesshaber, Anja Thiessen, Eva-Maria Mandelkow, Xiaoyu Li, Cindy Johne, Jian Jiao, Dorthe Matenia
Publikováno v:
Molecular biology of the cell. 16(9)
MARK/Par-1 is a kinase involved in development of embryonic polarity. In neurons, MARK phosphorylates tau protein and causes its detachment from microtubules, the tracks of axonal transport. Because the target sites of MARK on tau occur at an early s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8aa61b2f54128f2364a8e7f8845d0639
https://pubmed.ncbi.nlm.nih.gov/16014608
https://pubmed.ncbi.nlm.nih.gov/16014608
Autor:
Paul Saftig, Achilleas S. Frangakis, Martin Lackmann, Bettina Griesshaber, Peter W. Janes, Alice Y Ting, Kane Treble, Sabine H Wimmer-Kleikamp, Ola Sabet, Marcus Grabenbauer, Phillippe I Bastiaens
Publikováno v:
PLoS Biology
PLoS Biology, Vol 7, Iss 10, p e1000215 (2009)
PLoS
PLoS Biology, Vol 7, Iss 10, p e1000215 (2009)
PLoS
Novel imaging strategies reveal a conformational shift in a receptor tyrosine kinase domain that controls ligand shedding by an ADAM metalloprotease.
Release of cell surface-bound ligands by A-Disintegrin-And-Metalloprotease (ADAM) transmembrane
Release of cell surface-bound ligands by A-Disintegrin-And-Metalloprotease (ADAM) transmembrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49df4f1af8d6c0a9c624d6d9e20f01d6
https://doi.org/10.1371/journal.pbio.1000215
https://doi.org/10.1371/journal.pbio.1000215