Zobrazeno 1 - 10
of 76
pro vyhledávání: '"Friedrich Koch-Nolte"'
Autor:
Mario Leutert, Yinghui Duan, Riekje Winzer, Stephan Menzel, Eva Tolosa, Tim Magnus, Michael O. Hottiger, Friedrich Koch-Nolte, Björn Rissiek
Publikováno v:
Frontiers in Immunology
Frontiers in Immunology, Vol 12 (2021)
Frontiers in Immunology, Vol 12 (2021)
Mouse T cells express the ecto-ADP-ribosyltransferase ARTC2.2, which can transfer the ADP-ribose group of extracellular nicotinamide adenine dinucleotide (NAD+) to arginine residues of various cell surface proteins thereby influencing their function.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b18d2559daa77653aa7887980d915a9
https://doi.org/10.5167/uzh-210701
https://doi.org/10.5167/uzh-210701
Autor:
Björn Rissiek, Friedrich Koch-Nolte, Friedrich Haag, Catherine Meyer-Schwesinger, Andreas Tholey, Tomas Koudelka, Stephan Menzel
Publikováno v:
Frontiers in Immunology, Vol 12 (2021)
Frontiers in Immunology
Frontiers in Immunology
Murine T cells express the GPI-anchored ADP-ribosyltransferase 2.2 (ARTC2.2) on the cell surface. In response to T cell activation or extracellular NAD+ or ATP-mediated gating of the P2X7 ion channel ARTC2.2 is shed from the cell surface as a soluble
Autor:
Andreas Tholey, Björn Rissiek, Marion Nissen, Thomas Jakoby, Stephan Menzel, Nicole Schwarz, Maria Miksiewicz, Friedrich Haag, Friedrich Koch-Nolte, Peter Bannas
Publikováno v:
The Journal of Immunology. 195:2057-2066
ARTC2.2 is a toxin-related, GPI-anchored ADP-ribosyltransferase expressed by murine T cells. In response to NAD+ released from damaged cells during inflammation, ARTC2.2 ADP-ribosylates and thereby gates the P2X7 ion channel. This induces ectodomain
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1813
Mouse T cells express the toxin-related ecto-ADP-ribosyltransferase ARTC2 that catalyzes the posttranslational ADP-ribosylation of cell surface proteins by transferring the ADP-ribose group of its substrate nicotinamide adenine dinucleotide (NAD
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1813
Mammalian ARTCs are expressed as glycosylphosphatidylinositol (GPI)-anchored ectoenzymes (ARTC1-ARTC4) or secretory proteins (ARTC5) by different cell types. The ARTC2 enzymes catalyze mono-ADP-ribosylation of arginine residues in the extracellular d
Autor:
Mercedes Zubiaur, Davide Botta, Ramón Merino, José-Ángel Robles-Guirado, Angel L. Corbí, Elena González-Paredes, Jaime Sancho, Friedrich Koch-Nolte, Nicola Lo Buono, Daniela Cerezo-Wallis, Verónica Prados-Maniviesa, Luz M. Cumba Garcia, Matthias Mack, Eduardo Andrés-León, Salvador Guerrero, Antonio Rosal-Vela, Esther Zumaquero, Frances E. Lund, Sonia García-Rodríguez
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Scientific Reports, Vol 8, Iss 1, Pp 1-19 (2018)
BASE-Bielefeld Academic Search Engine
Scientific Reports
Repisalud
Instituto de Salud Carlos III (ISCIII)
instname
Scientific Reports, Vol 8, Iss 1, Pp 1-19 (2018)
BASE-Bielefeld Academic Search Engine
Scientific Reports
Repisalud
Instituto de Salud Carlos III (ISCIII)
In this study, we investigated the role of CD38 in a pristane-induced murine model of lupus. CD38-deficient (Cd38−/−) but not ART2-deficient (Art2−/−) mice developed less severe lupus compared to wild type (WT) mice, and their protective phen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cff93788b92a90874bf6286a995def38
http://hdl.handle.net/10261/161836
http://hdl.handle.net/10261/161836
Autor:
Maike Cordes, Sarah Behr, Björn Rissiek, Mario Leutert, Anne Rissiek, Sahil Adriouch, Larissa Jank, Stephan Menzel, Peter Ludewig, Friedrich Haag, Michael O. Hottiger, Friedrich Koch-Nolte, Tim Magnus, Mathias Gelderblom
Publikováno v:
Scientific Reports
Scientific Reports, Nature Publishing Group, 2017, 7 (1), ⟨10.1038/s41598-017-16613-w⟩
Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
Scientific Reports, Nature Publishing Group, 2017, 7 (1), ⟨10.1038/s41598-017-16613-w⟩
Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
Mammalian ecto-ADP-ribosyltransferases (ecto-ARTs or also ARTCs) catalyze the ADP-ribosylation of cell surface proteins using extracellular nicotinamide adenine dinucleotide (NAD+) as substrate. By this post-translational protein modification, ecto-A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca64a325ac9d6e3685a189046eafa295
https://hal-normandie-univ.archives-ouvertes.fr/hal-02375773
https://hal-normandie-univ.archives-ouvertes.fr/hal-02375773
Autor:
Friedrich Koch-Nolte, Carrie A. Cowardin, Anna Marei Eichhoff, Carsten Schwan, Mahmoud M. Saleh, Erica L. Buonomo, Stacey L. Burgess, William A. Petri, Sarah A. Kuehne, Nigel P. Minton, Dena Lyras, Klaus Aktories, Madeline G. Wilson
Publikováno v:
Nature microbiology
Clostridium difficile is the most common hospital acquired pathogen in the USA, and infection is, in many cases, fatal. Toxins A and B are its major virulence factors, but expression of a third toxin, known as C. difficile transferase (CDT), is incre
Publikováno v:
Journal of Proteomics. 75:169-176
Mono-ADP-ribosylation of arginine is a protein modification in eukaryotic cells regulating protein activity and thereby influencing signal transduction and metabolism. Due to the complexity of the modification and the fragmentation pattern in MS/MS C
Autor:
Peter Bannas, Friedrich Koch-Nolte, Friedrich Haag, Irm Hermans-Borgmeyer, Lennart Well, Felix Scheuplein
Publikováno v:
Molecular Immunology. 48:1762-1770
T cells constitutively express low amounts of a toxin-related ADP-ribosylating ecto-enzyme, ART2.2. In inflammatory settings, cells release NAD, the substrate for ART2.2. The ART2.2 catalyzed ADP-ribosylation of cell surface proteins induces cell dea