Zobrazeno 1 - 10
of 451
pro vyhledávání: '"Rupert Timpl"'
Publikováno v:
Immunochemistry of the Extracellular Matrix ISBN: 9781351073417
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::16ec3bf938c613a682d1f833f3baba3f
https://doi.org/10.1201/9781351073417-9
https://doi.org/10.1201/9781351073417-9
Autor:
Rupert Timpl, Leila Risteli
Publikováno v:
Immunochemistry of the Extracellular Matrix ISBN: 9781351073417
Immunochemistry of the Extracellular Matrix
Immunochemistry of the Extracellular Matrix
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a133f395a375c508b99923a009461e58
https://doi.org/10.1201/9781351073417-13
https://doi.org/10.1201/9781351073417-13
Autor:
George R. Martin, Rupert Timpl
Publikováno v:
Immunochemistry of the Extracellular Matrix ISBN: 9781351073424
Immunochemistry of the Extracellular Matrix
Immunochemistry of the Extracellular Matrix
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a256e283fd441ab2912df240b2472215
https://doi.org/10.1201/9781351073424-5
https://doi.org/10.1201/9781351073424-5
Autor:
Dessislava Markova, Günter Kostka, Mon-Li Chu, Rupert Timpl, Naoyuki Kobayashi, Franz-Georg Hanisch, Hans Peter Bächinger, Douglas R. Keene, Jörg H.O. Garbe, Takako Sasaki, Takeshi Tsuda
Publikováno v:
Journal of Biological Chemistry. 282:11805-11816
Fibulins are a family of five extracellular matrix proteins characterized by tandem arrays of epidermal growth factor-like domains and a C-terminal fibulin-type module. They are widely distributed and often associated with vasculature and elastic tis
Autor:
Anders Aspberg, Anna E. Johnson, Takako Sasaki, Reinhard Fässler, Attila Aszódi, Rupert Timpl, Alexander J. Kvist, Matthias Mörgelin, Karin Lindblom, Erika Gustafsson, Eva Bengtsson
Publikováno v:
Journal of Biological Chemistry. 281:33127-33139
Inactivation of the perlecan gene leads to perinatal lethal chondrodysplasia. The similarity to the phenotypes of the Col2A1 knock-out and the disproportionate micromelia mutation suggests perlecan involvement in cartilage collagen matrix assembly. W
Autor:
Uwe Hansen, Peter Bruckner, Rupert Timpl, Rick T. Owens, Takako Sasaki, Richard Wilson, Jamie Fitzgerald, John F. Bateman, Justin M. Allen
Publikováno v:
Journal of Biological Chemistry. 281:7341-7349
WARP is a novel member of the von Willebrand factor A domain superfamily of extracellular matrix proteins that is expressed by chondrocytes. WARP is restricted to the presumptive articular cartilage zone prior to joint cavitation and to the articular
Autor:
Rupert Timpl, Naomi J Clout, Erhard Hohenester, Axel Ullrich, Walter Göhring, Pjotr Knyazev, Yuri Cheburkin, Takako Sasaki
Publikováno v:
The EMBO Journal. 25:80-87
Receptor tyrosine kinases of the Axl family are activated by the vitamin K-dependent protein Gas6. Axl signalling plays important roles in cancer, spermatogenesis, immunity, and platelet function. The crystal structure at 3.3 A resolution of a minima
Autor:
Takako Sasaki, Daniel E. Michele, Rita Barresi, Jakob S. Satz, Hajime Kusano, Michael D. Henry, Motoi Kanagawa, Rupert Timpl, Kevin P. Campbell
Publikováno v:
FEBS Letters. 579:4792-4796
Dystroglycan is a cell-surface matrix receptor that requires LARGE-dependent glycosylation for laminin binding. Although the interaction of dystroglycan with laminin has been well characterized, less is known about the role of dystroglycan glycosylat
Autor:
Takako Sasaki, Satoshi Amano, Kuniko Kadoya, K. Matsuzaki, Norio Kumagai, Günter Kostka, Rupert Timpl, Toshio Nishiyama, L. Y. Sakai
Publikováno v:
British Journal of Dermatology. 153:607-612
Summary Background Fibulin-5 was recently found as a secreted extracellular matrix protein that functions as a scaffold for elastic fibres. However, the distribution of fibulin-5 in human skin and its changes during the ageing process are not known.
Publikováno v:
Journal of Biological Chemistry. 280:22146-22153
Recently a novel laminin gamma3 chain was identified in mouse and human and shown to have the same modular structure as the laminin gamma1 chain. We expressed two fragments of the gamma3 chain in mammalian cells recombinantly. The first, domain VI/V,