Zobrazeno 1 - 10
of 18
pro vyhledávání: 'Lüllmann-Rauch, Renate'
Autor:
Stefan F. Lichtenthaler, Paul Saftig, Tobias B. Huber, Lukas Heintz, Lisa Seipold, Lisa Schebsdat, Maja T. Lindenmeyer, Renate Lüllmann-Rauch, Sebastian Wetzel, Stephanie Zielinski, Oliver Kretz, Catherine Meyer-Schwesinger, Marlies Sachs, Wiebke Sachs, Julia Reichelt, Thorsten Wiech, Stephan A. Müller
Publikováno v:
Journal of the American Society of Nephrology 32(6), 1389-1408 (2021). doi:10.1681/ASN.2020081213
J Am Soc Nephrol
J Am Soc Nephrol
Background Podocytes embrace the glomerular capillaries with foot processes, which are interconnected by a specialized adherens junction to ultimately form the filtration barrier. Altered adhesion and loss are common features of podocyte injury, whic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cd38702448fa14059c39567c6bc8975
Autor:
Sandra Kissing, Renate Lüllmann-Rauch, Albert Haas, Uwe Kornak, Eeva-Liisa Eskelinen, Paul Saftig, Sabrina Jabs, Jef K. De Brabander, Atsuhiro Ichihara, Sönke Rudnik, Jörg Heeren, Markus Damme
Publikováno v:
Autophagy, 13(4):670-685
The vacuolar-type H+-translocating ATPase (v-H+-ATPase) has been implicated in the amino acid-dependent activation of the mechanistic target of rapamycin complex 1 (MTORC1), an important regulator of macroautophagy. To reveal the mechanistic links be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb2812e53387bd2777d9f343a01c0fab
Autor:
Eeva-Liisa Eskelinen, Jürgen Wienands, Paul Saftig, Renate Lüllmann-Rauch, Michael Engelke, Kai Dittmann, Ralf Dressel, Bernd Schröder, Susann Hüttl, Regina Fluhrer, Irm Hermans-Borgmeyer, Janna Schneppenheim
Publikováno v:
Journal of experimental medicine 210(1), 41-58 (2012). doi:10.1084/jem.20121069
Journal of Experimental Medicine; Vol 210
The Journal of Experimental Medicine
Journal of Experimental Medicine; Vol 210
The Journal of Experimental Medicine
The intramembrane protease SPPL2a cleaves the NTF of invariant chain (CD74), which is essential for normal trafficking of MHC class II–containing endosomes and thus for B cell development and function.
Regulated intramembrane proteolysis is a
Regulated intramembrane proteolysis is a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c8dd418de64d7694178a8d6a5818c82
http://hdl.handle.net/10138/42725
http://hdl.handle.net/10138/42725
Publikováno v:
Pharmacology & Toxicology. 79:109-113
The immunomodulatory drug tilorone (2,7-bis[2-(diethylamino)ethoxy]fluoren-9-one) and several congeners are known to disturb the lysosomal degradation of sulphated glycosaminoglycans and thereby induce lysosomal storage of glycosaminoglycans in cultu
Publikováno v:
Toxicology. 110:27-37
The antimalarial agents quinacrine and chloroquine are well known as potent inducers of lysosomal storage of polar lipids (lipidosis) in cell culture and in vivo. In previous experiments on cultured fibroblasts, chloroquine was shown to additionally
Autor:
Bart De Strooper, Annika Schmitz, Johannes Prox, Carl P. Blobel, Silvio Weber, Renate Lüllmann-Rauch, Paul Saftig, Michaela T. Niessen, Ralf Schwanbeck, Carien M. Niessen, Ellen Jorissen
The disintegrin and metalloproteinase Adam10 has been implicated in the regulation of key signaling pathways that determine skin morphogenesis and homeostasis. To address the in vivo relevance of Adam10 in the epidermis, we have selectively disrupted
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab06c9c9f3a056803c973beea0a8de5e
https://europepmc.org/articles/PMC3014635/
https://europepmc.org/articles/PMC3014635/
Molecular characterization and gene disruption of mouse lysosomal putative serine carboxypeptidase 1
Autor:
Kollmann, Katrin, Damme, Markus, Deuschl, Florian, Kahle, Jörg, D'Hooge, Rudi, Lüllmann-Rauch, Renate, Lübke, Torben
The retinoid-inducible serine carboxypeptidase 1 (Scpep1; formerly RISC) is a lysosomal matrix protein that was initially identified in a screen for genes induced by retinoic acid. Recently, it has been spotlighted by several proteome analyses of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::be80dfda506d0c4d58a79f9f8001916c
https://doi.org/10.1111/j.1742-4658.2009.06877.x
https://doi.org/10.1111/j.1742-4658.2009.06877.x
Publikováno v:
Virchows Archiv B Cell Pathology Including Molecular Pathology. 60:99-104
Several di-cationic amphiphilic compounds are known to cause lysosomal accumulation of sulfated glycosaminoglycans (sGAG) in intact rats and in cultured rat fibroblasts. The purpose of the present investigation was to examine whether this drug side e
Autor:
Renate Lüllmann-Rauch, M. Ziegenhagen
Publikováno v:
Histochemistry. 95:263-268
The purpose of the present investigation was to examine whether or not a di-cationic amphiphilic compound that is known (1) to be accumulated in lysosomes and (2) to form insoluble complexes with sulfated glycosaminoglycans (sGAG) in vitro, is able t
Publikováno v:
Archives of Toxicology. 64:291-298
The purpose of the present investigation was to establish a cell culture system suitable for demonstrating the drug-induced lysosomal storage of sulfated glycosaminoglycans (GAGs). This is a drug side-effect which was previously studied in animals tr