Regulators of G-protein signalling are modulated by bacterial lipopeptides and lipopolysaccharide

Autor: Sabine Riekenberg, Artur J. Ulmer, Günther Jung, Jennifer Debarry, Karl-Heinz Wiesmüller, Katja Farhat, Holger Heine

Publikováno v: FEBS Journal. 276:649-659

Regulators of G-protein signalling accelerate the GTPase activity of G(alpha) subunits, driving G proteins in their inactive GDP-bound form. This property defines them as GTPase activating proteins. Here the effect of different Toll-like receptor ago

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::470e316204ed5f65acfa5fd084bbe21d
https://doi.org/10.1111/j.1742-4658.2008.06813.x

List of Contributors

Autor: Nawaf Al-Maharik, Heidi Annuk, Michael A. Apicella, Ben J. Appelmelk, Ivo G. Boneca, Petra Born, Klaus Brandenburg, Patrick J. Brennan, Volker Briken, Eric D. Brown, Stephen D. Carrington, Paola Cescutti, Delphi Chatterjee, Marguerite Clyne, Richard M. Cooper, Anthony P. Corfield, Monica M. Cunneen, Piet W.J. de Groot, Gennaro De Libero, Clara G. de los Reyes-Gavilán, Tamara L. Doering, Max Dow, Nicole N. Driessen, Jeffrey C. Dyason, Eva Maria Egelseer, Alan D. Elbein, Mario F. Feldman, Eamonn Fitz Patrick, Yukari Fujimoto, Koichi Fukase, Patrick Garidel, Jeroen Geurtsen, Marlyn Gonzalez, I. Darren Grice, Patricia Guerry, Thomas Gutsmann, Holger Heine, Joanne Heng, Otto Holst, Harold. J Jennings, Michael P. Jennings, Margaret I. Kanipes, Dennis L. Kasper, Wafa Khamri, Milton J. Kiefel, Dionne C.G. Klein, Frans M. Klis, Yuriy A. Knirel, Thomas Kohler, Paul Kosma, Emir Kulauzovic, Shoichi Kusumoto, John R. Lawrence, Clifford A. Lingwood, Peter N. Lipke, Susan M. Logan, Radia Mahfoud, Malcolm J. McConville, Rachel M. McLoughlin, Paul Messner, Antonio Molinaro, Anthony P. Moran, Thomas Naderer, Thomas R. Neu, Mari-Anne Newman, Andrei V. Nikolaev, Christian M. Pedersen, Mark P. Pereira, Andreas Peschel, Stefan Pöhlmann, Robert A. Pon, Stuart A. Ralph, Peter R. Reeves, Anne N. Reid, Colm J. Reid, Morgann C. Reilly, Sabine Riekenberg, Patricia Ruas-Madiedo, Nuria Salazar, Christina Schäffer, Richard R. Schmidt, Ian C. Schoenhofen, Marit Sletmoen, Uwe B. Sleytr, Evelyn C. Soo, Imke Steffen, Daniel C. Stein, Bjørn T. Stokke, Christine M. Szymanski, Joe Tiralongo, Jennifer A. Tee, Mark R. Thursz, M. Stephen Trent, Theodros S. Tsegaye, Jean van Heijenoort, Waldemar Vollmer, Mark von Itzstein, Jennifer C. Wilson, Guoqing Xia

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f309f19d53c57b2a7fee9813b303d0ea
https://doi.org/10.1016/b978-0-12-374546-0.00053-5

Identification of full length bovine TLR1 and functional characterization of lipopeptide recognition by bovine TLR2/1 heterodimer

Autor: Katja Farhat, Artur J. Ulmer, Günther Jung, Karl-Heinz Wiesmüller, Sabine Riekenberg, Thomas W. Jungi

Publikováno v: Veterinary Research
Veterinary Research, BioMed Central, 2010, 41 (3), ⟨10.1051/vetres/2010006⟩

International audience; Toll-like receptors (TLR) are highly conserved pattern recognition receptors of the innate immune system. Toll-like receptor 2 (TLR2) recognizes bacterial lipopeptides in a heterodimeric complex with TLR6 or TLR1, thereby disc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30376d4098b804f9666f07b06eb14c57
http://europepmc.org/articles/PMC2831532

Heterodimerization of TLR2 with TLR1 or TLR6 expands the ligand spectrum but does not lead to differential signaling

Autor: Katja Farhat, Artur J. Ulmer, Ute Buwitt-Beckmann, Karl-Heinz Wiesmüller, Jörg Mages, Holger Heine, Sabine Riekenberg, Günther Jung, Kristina Röschmann, Jennifer Debarry, Roland Lang

Publikováno v: Journal of leukocyte biology. 83(3)

TLR are primary triggers of the innate immune system by recognizing various microorganisms through conserved pathogen-associated molecular patterns. TLR2 is the receptor for a functional recognition of bacterial lipopeptides (LP) and is up-regulated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fc358b3182da7ff081cbafab7162322
https://pubmed.ncbi.nlm.nih.gov/18056480

Identification of EhICP1, a chagasin-like cysteine protease inhibitor of Entamoeba histolytica

Autor: Henning Scholze, B. Witjes, Mirela Šarić, Iris Bruchhaus, Sabine Riekenberg

Publikováno v: FEBS Letters. (7):1573-1578

Based on the Entamoeba histolytica genome project ( www.sanger.ac.uk/Projects/E_histolytica/ ) we have identified a cysteine protease inhibitor, EhICP1 (amoebiasin 1), with significant homology to chagasin. Recombinant EhICP1 inhibited the protease a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71aac2215dd7bf19b372de997c98d3fc