Zobrazeno 1 - 10
of 32
pro vyhledávání: 'Lüllmann-Rauch, Renate'
Autor:
Dante Neculai, Saskia Heybrock, Sergio Grinstein, Régis Pomès, Renate Lüllmann-Rauch, Ying Meng, Christopher Ing, Kristiina Kanerva, Paul Saftig, Michael Schwake, Joerg Heeren, Wim Annaert, William S. Trimble, Anna Liang, Xialian Weng, Elina Ikonen, Gilbert G. Privé, Richard F. Collins, Young Ah Kim, Zi-Jian Xiong
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Nature Communications
Nature Communications
The intracellular transport of cholesterol is subject to tight regulation. The structure of the lysosomal integral membrane protein type 2 (LIMP-2, also known as SCARB2) reveals a large cavity that traverses the molecule and resembles the cavity in S
Autor:
Julia Bär, Renate Lüllmann-Rauch, Mahmoud Bassal, André R. A. Marques, Lina Schmidt, Markus Damme, Markus Glatzel, Marina Mikhaylova, Niklas Thießen, Steffen E. Storck, Alessandro Di Spiezio, Udo Bartsch, Jens Fogh, Joachim Grötzinger, Paul Saftig, Claus U. Pietrzik
Publikováno v:
Autophagy
CTSD (cathepsin D) is one of the major lysosomal proteases indispensable for the maintenance of cellular proteostasis by turning over substrates of endocytosis, phagocytosis and autophagy. Consequently, CTSD deficiency leads to a strong impairment of
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:
Wolf, Heike, Damme, Markus, Stroobants, Stijn, D'Hooge, Rudi, Beck, Hans Christian, Hermans-Borgmeyer, Irm, Lüllmann-Rauch, Renate, Dierks, Thomas, Lübke, Torben
Publikováno v:
Disease Models & Mechanisms, Vol 9, Iss 9, Pp 1015-1028 (2016)
Wolf, H, Damme, M, Stroobants, S, D'Hooge, R, Beck, H C, Hermans-Borgmeyer, I, Lüllmann-Rauch, R, Dierks, T & Lübke, T 2016, ' A mouse model for fucosidosis recapitulates storage pathology and neurological features of the milder form of the human disease ', Disease Models & Mechanisms, vol. 9, no. 9, pp. 1015-1028 . https://doi.org/10.1242/dmm.025122
Disease Models & Mechanisms
Wolf, H, Damme, M, Stroobants, S, D'Hooge, R, Beck, H C, Hermans-Borgmeyer, I, Lüllmann-Rauch, R, Dierks, T & Lübke, T 2016, ' A mouse model for fucosidosis recapitulates storage pathology and neurological features of the milder form of the human disease ', Disease Models & Mechanisms, vol. 9, no. 9, pp. 1015-1028 . https://doi.org/10.1242/dmm.025122
Disease Models & Mechanisms
Fucosidosis is a rare lysosomal storage disorder caused by the inherited deficiency of the lysosomal hydrolase α-L-fucosidase, which leads to an impaired degradation of fucosylated glycoconjugates. Here, we report the generation of a fucosidosis mou
Autor:
Vivian Adamski, Torben Mentrup, Regina Fluhrer, Martina Haug-Kröper, Uddipta Biswas, Rolf Jessberger, Ronny Heidasch, Verena Dederer, Bernd Schröder, Paul Saftig, Alkmini A Papadopoulou, Rieke Meyer, Stefan F. Lichtenthaler, Johannes Niemeyer, Renate Lüllmann-Rauch, Martin Bergmann, Artur Mayerhofer, Gunther Wennemuth, Marius K. Lemberg, Stephan A. Müller
Publikováno v:
EMBO reports 20(3), e46449 (2019). doi:10.15252/embr.201846449
Signal peptide peptidase (SPP) and the four homologous SPP‐like (SPPL) proteases constitute a family of intramembrane aspartyl proteases with selectivity for type II‐oriented transmembrane segments. Here, we analyse the physiological function of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1418b4ad477efe0f728a4ddd7233c8b6
https://opus.bibliothek.uni-augsburg.de/opus4/frontdoor/index/index/docId/51759
https://opus.bibliothek.uni-augsburg.de/opus4/frontdoor/index/index/docId/51759
Autor:
Rudi D'Hooge, Cecilia Weigelt, Volkmar Gieselmann, Claes Andersson, Carl Eistrup, Ulrich Matzner, Jens Fogh, Renate Lüllmann-Rauch, Stijn Stroobants
Publikováno v:
Molecular Therapy. 17(4):600-606
Inherited deficiencies of lysosomal hydrolases cause lysosomal storage diseases (LSDs) that are characterized by a progressive multisystemic pathology and premature death. Repeated intravenous injection of the active counterpart of the deficient enzy
Autor:
Stijn Stroobants, Paul Saftig, Renate Lüllmann-Rauch, Claes Andersson, Rudi D'Hooge, Meike Lüdemann, Jens Fogh, Willy Morelle, Judith Blanz, Helena Reuterwall, Jean Claude Michalski
Publikováno v:
Human Molecular Genetics. 17:3437-3445
Despite the progress in the treatment of lysosomal storage disorders (LSDs) mainly by enzyme replacement therapy, only limited success was reported in targeting the appropriate lysosomal enzyme into the brain. This prevents efficient clearance of neu
Autor:
Volkmar Gieselmann, Kerstin Khalaj Hedayati, Hariharasubramanian Ramakrishnan, Hans-Hilmar Goebel, Renate Lüllmann-Rauch, Simon Ngamli Fewou, Matthias Eckhardt, Carsten Wessig, Helena Maier
Publikováno v:
The Journal of Neuroscience. 27:9482-9490
Metachromatic leukodystrophy (MLD) is a lysosomal storage disorder caused by the deficiency of arylsulfatase A (ASA). This results in accumulation of sulfated glycosphingolipids, mainly 3-O-sulfogalactosylceramide (sulfatide), in the nervous system a
Autor:
Franziska Dierck, Renate Lüllmann-Rauch, Dieter Adam, Norbert Frey, Sabine Adam-Klages, Constantin Kühl, Justyna Sosna, Susanne Hille, Christian Kuhn
Publikováno v:
Cardiovascular research. 110(3)
Aims Down syndrome-associated dual-specificity tyrosine-(Y)-phosphorylation-regulated kinase 1A (DYRK1A) is a ubiquitously expressed protein kinase. Up to date a variety of targets have been identified, establishing a key role for Dyrk1a in selected
Autor:
Peter Heimann, Thomas Dierks, Markus Damme, Steven U. Walkley, Tomo Sawada, Theresa Ortkras, Björn Kowalewski, Renate Lüllmann-Rauch
Publikováno v:
Human molecular genetics. 24(7)
Deficiency of arylsulfatase G (ARSG) leads to a lysosomal storage disease in mice resembling biochemical and pathological features of the mucopolysaccharidoses and particularly features of mucopolysaccharidosis type III (Sanfilippo syndrome). Here we