Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Gustavo Glowacki"'
Autor:
Nicole Gerwin, Celeste Scotti, Christine Halleux, Mara Fornaro, Jimmy Elliott, Yunyu Zhang, Kristen Johnson, Jian Shi, Sandra Walter, Yufei Li, Carsten Jacobi, Nelly Laplanche, Magali Belaud, Jochen Paul, Gustavo Glowacki, Thomas Peters, Keith A. Wharton, Igor Vostiar, Florine Polus, Ina Kramer, Sabine Guth, Abdelkader Seroutou, Subhajit Choudhury, Didier Laurent, Joseph Gimbel, Jörg Goldhahn, Matthias Schieker, Sophie Brachat, Ronenn Roubenoff, Michaela Kneissel
Publikováno v:
Nature medicine. 28(12)
Osteoarthritis (OA) is a common, debilitating, chronic disease with no disease-modifying drug approved to date. We discovered LNA043—a derivative of angiopoietin-like 3 (ANGPTL3)—as a potent chondrogenesis inducer using a phenotypic screen with h
Autor:
Gudrun Dubberke, Fabio Malavasi, Friedrich Haag, Ada Funaro, Friedrich Koch-Nolte, Erika Ortolan, Fenja Braasch, Gustavo Glowacki, Peter Bannas
Publikováno v:
Cellular Immunology. 236:66-71
ADP-ribosyltransferases (ARTs) transfer ADP-ribose from NAD to arginine, asparagine, or cysteine residues in target proteins. This post-translational protein modification is the mechanism by which cholera-toxin and other bacterial toxins cause pathol
Autor:
Phillipe Deterre, Michel Seman, Dunja Freese, Christian Krebs, Sahil Adriouch, Felix Scheuplein, Gustavo Glowacki, Friedrich Haag, Friedrich Koch-Nolte
Publikováno v:
Immunity. 19(4):571-582
T cells express a toxin-related ADP-ribosylating ectoenzyme, ART2. Exposure of mature T cells to NAD, the substrate for ADP-ribosylation, induces cell death. ART2-catalyzed ADP-ribosylation activates the cytolytic P2X7 purinoceptor, causing calcium f
Publikováno v:
Europe PubMed Central
Mono(ADP-ribosyl)transferases regulate the function of target proteins by attaching ADP-ribose to specific amino acid residues in the proteins. We have characterized the gene for mouse arginine-specific ADP-ribosyltransferase, Art1. Southern blot ana
Autor:
Christopher D. Buckley, Marion E. Reid, Debbie L. Hardie, Friedrich Haag, Gustavo Glowacki, Sapna Halder, Friedrich Koch-Nolte, Gregory R. Halverson, Fenja Braasch, Sarah Kahl, Ada Funaro, Alissa Schawalder, Ines Parusel, Erika Ortolan, Fabio Malavasi
Publikováno v:
Cellular immunology. 236(1-2)
ART4 (CD297) is a member of the family of toxin-related ADP-ribosyltransferases (ARTs) and is the carrier of the Dombrock blood group alloantigens (Do). Two mouse monoclonal antibodies (MIMA-52 and MIMA-53), and two rat monoclonal antibodies (N0NI-B4
Autor:
Michel Seman, Felix Scheuplein, Gustavo Glowacki, Friedrich Koch-Nolte, Friedrich Haag, Sahahil Adriouch
Publikováno v:
Annals of the New York Academy of Sciences. 1010
Cytotoxicity induced by protein ADP-ribosylation is a common theme of certain bacterial toxins and of the mammalian ectoenzyme ART2. Exposure of T cells to NAD, the substrate for ART2-catalyzed ADP-ribosylation, induces exposure of phosphatidylserine
Autor:
Michel, Seman, Sahil, Adriouch, Felix, Scheuplein, Christian, Krebs, Dunja, Freese, Gustavo, Glowacki, Phillipe, Deterre, Friedrich, Haag, Friedrich, Koch-Nolte
Publikováno v:
Immunity. 19(4)
T cells express a toxin-related ADP-ribosylating ectoenzyme, ART2. Exposure of mature T cells to NAD, the substrate for ADP-ribosylation, induces cell death. ART2-catalyzed ADP-ribosylation activates the cytolytic P2X7 purinoceptor, causing calcium f
Autor:
Friedrich Koch-Nolte, Rickmer Braren, Pedro A. Reche, Fernando Bazan, Marina Cetkovic-Cvrlje, Marion Nissen, Gustavo Glowacki, Kathrin Firner, Friedrich Haag, Edward H. Leiter, Maren Kühl
Publikováno v:
E-Prints Complutense: Archivo Institucional de la UCM
Universidad Complutense de Madrid
E-Prints Complutense. Archivo Institucional de la UCM
instname
Universidad Complutense de Madrid
E-Prints Complutense. Archivo Institucional de la UCM
instname
ADP-ribosyltransferases including toxins secreted by Vibrio cholera, Pseudomonas aerurginosa, and other pathogenic bacteria inactivate the function of human target proteins by attaching ADP-ribose onto a critical amino acid residue. Cross-species pol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b223100673c56df9b67cea766ce475f2
https://eprints.ucm.es/id/eprint/9341/1/16.Glowacki_Reche_etal_PS_2002.pdf
https://eprints.ucm.es/id/eprint/9341/1/16.Glowacki_Reche_etal_PS_2002.pdf
Autor:
Friedrich Koch-Nolte, Marina Cetkovic-Cvrlje, Rickmer Braren, Gustavo Glowacki, Friedrich Haag, Edward H. Leiter
Publikováno v:
Gene. 275(2)
Mono(ADP-ribosyl)transferases regulate the function of target proteins by attaching ADP-ribose to specific amino acid residues in their target proteins. The purpose of this study was to determine the structure, chromosomal localization, and expressio