Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Eddie Kohfeldt"'
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,
Publikováno v:
European Journal of Biochemistry. 259:917-926
Domain IV of mouse perlecan, which consists of 14 immunoglobulin superfamily (IG) modules, was prepared from recombinant human cell culture medium in the form of two fragments, IV-1 (IG2–9, 100 kDa) and IV-2 (IG10–15, 66 kDa). Both fragments boun
Publikováno v:
Journal of Molecular Biology. 282:99-109
Human nidogen-2 was cloned and sequenced (1375 residues) and found to share 46% sequence identity and a similar domain arrangement with the previously characterized basement membrane protein nidogen-1. Recombinant nidogen-2 was purified as a 200 kDa
Publikováno v:
Histochemistry and cell biology. 113(2)
Nidogen-1, a key component of basement membranes, is considered to function as a link between laminin and collagen type IV networks. Recently a new member of the nidogen family, nidogen-2, has been characterized. Preliminary immunohistochemical data
Publikováno v:
Annals of the New York Academy of Sciences. 857
High-affinity binding of nidogen to laminins involves a single binding site on the laminin gamma 1 chain and is thus a property shared by almost all laminin isoforms. This binding mediates the connection of laminins to the collagen IV network, perlec
Autor:
Eddie Kohfeldt, Tad A. Holak, Ulrike Mayer, Rupert Timpl, Mon-Li Chu, Walter Göhring, Markus Zweckstetter
Publikováno v:
FEBS Journal
The recombinant Kunitz protease inhibitor module (domain C5) of human collagen alpha 3(VI) chain was previously shown to lack inhibitory activity for proteases with trypsin-like specificity and some other proteases. We have now prepared mutants in th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ad130396b6491c9c09d3f4d9c0647ce
https://hdl.handle.net/11858/00-001M-0000-002B-A31E-A11858/00-001M-0000-002B-A320-2
https://hdl.handle.net/11858/00-001M-0000-002B-A31E-A11858/00-001M-0000-002B-A320-2