Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Hans Christian Thøgersen"'
Autor:
Mikkel Holmen Andersen, Hans Christian Thøgersen, Mette Munch, Thor Las Holtet, Hans Henrik Gad, Povilas Byla, Helle Jacobsen, Rune Hartmann
Publikováno v:
Journal of Biological Chemistry. 285:12096-12100
Inhibition of tumor necrosis factor α (TNFα) is a favorable way of treating several important diseases such as rheumatoid arthritis, Crohn disease, and psoriasis. Therefore, an extensive range of TNFα inhibitory proteins, most of them based upon a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::317634f992e7697e195a34b5834e9e39
https://doi.org/10.1074/jbc.m109.063305
https://doi.org/10.1074/jbc.m109.063305
Autor:
Alexandre M. J. J. Bonvin, Birthe B. Kragelund, Flemming M. Poulsen, Olav M. Andersen, Hans Christian Thøgersen, Ida J. Bjerrum-Bohr, Charlotte O'Shea, Gitte A. Jensen, Michael Etzerodt
Publikováno v:
Journal of Molecular Biology. 362:700-716
The low-density lipoprotein receptor-related protein (LRP) interacts with more than 30 ligands of different sizes and structures that can all be replaced by the receptor-associated protein (RAP). The double module of complement type repeats, CR56, of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0c12f7faa2fb87bcbeeaa72b881318e
https://doi.org/10.1016/j.jmb.2006.07.013
https://doi.org/10.1016/j.jmb.2006.07.013
Publikováno v:
Macromolecules. 36:1157-1161
Molecule chains of spider silk protein readily self-assemble into ordered structure such as ‚-sheets when a filament is pulled away from dilute aqueous solution of spider major ampullate silk protein. There is no need to change the pH, the temperat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::164f54ffdcc2b075d1fdba589aa44c0a
https://doi.org/10.1021/ma0214660
https://doi.org/10.1021/ma0214660
Autor:
Charlotte H. Møller, Hans Christian Thøgersen, Rikke Høegh Lorentsen, Thor Las Holtet, Michael Etzerodt
Publikováno v:
Org. Biomol. Chem.. 1:1657-1663
A library of blood coagulation factor Xa (FXa)–trypsin hybrid proteases was generated and displayed on phage for selection of derivatives with the domain “architecture” of trypsin and the specificity of FXa. Selection based on binding to soybea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::654982fa70009d7bd55ee416094e5348
https://doi.org/10.1039/b210149a
https://doi.org/10.1039/b210149a
Autor:
Jonas Heilskov Graversen, Søren K. Moestrup, Bent W. Sigurskjold, Rikke Høegh Lorentsen, Hans Christian Thøgersen, Christian Bøtcher Jacobsen, Michael Etzerodt
Publikováno v:
Journal of Biological Chemistry. 275:37390-37396
C-type lectin-like domains are found in many proteins, where they mediate binding to a wide diversity of compounds, including carbohydrates, lipids, and proteins. The binding of a C-type lectin-like domain to a ligand is often influenced by calcium.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::593a965541a26942530d1f0e585d6cd4
https://doi.org/10.1074/jbc.m004873200
https://doi.org/10.1074/jbc.m004873200
Autor:
Christian Jacobsen, Esben S. Sørensen, Hans Christian Thøgersen, Michael Etzerodt, Olav M. Andersen, Lisa Lystbæk Christensen, Søren K. Moestrup, Peter Christensen
Publikováno v:
Journal of Biological Chemistry. 275:21017-21024
The low density lipoprotein receptor-related protein (LRP), a member of the low density lipoprotein receptor family, mediates the internalization of a diverse set of ligands. The ligand binding sites are located in different regions of clusters consi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a7ac2d5c7345543aea0dbe9f292d25f
https://doi.org/10.1074/jbc.m000507200
https://doi.org/10.1074/jbc.m000507200
Autor:
Nigel R. Caterer, Rikke Høegh Lorentsen, Jonas Heilskov Graversen, Hans Christian Thøgersen, Michael Etzerodt
Publikováno v:
Biochemical Journal. 347:83-87
Tetranectin is a homotrimeric plasma and extracellular-matrix protein that binds plasminogen and complex sulphated polysaccharides including heparin. In terms of primary and tertiary structure, tetranectin is related to the collectin family of Ca2+-b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::14b80ebfa2de5cb225398899b3a80e3d
https://doi.org/10.1042/bj3470083
https://doi.org/10.1042/bj3470083
Autor:
Søren K. Moestrup, Michael Etzerodt, Jonas Heilskov Graversen, Christian Jacobsen, Hans Christian Thøgersen, Bent W. Sigurskjold, Rikke Høegh Lorentsen
Publikováno v:
Journal of Biological Chemistry. 273:29241-29246
Tetranectin, a homotrimeric protein belonging to the family of C-type lectins and structurally highly related to corresponding regions of the mannose-binding proteins, is known specifically to bind the plasminogen kringle 4 protein domain, an interac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f16d10ca2883b68a93c71b9f21725b06
https://doi.org/10.1074/jbc.273.44.29241
https://doi.org/10.1074/jbc.273.44.29241
Autor:
Bettina Bryde Nielsen, Jonas Heilskov Graversen, Hans Christian Thøgersen, Michael Etzerodt, Thor Las Holtet, Jette S. Kastrup, Ingrid Kjøller Larsen, Hanne N. Rasmussen
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 54:757-766
Tetranectin (TN) is a C-type lectin involved in fibrinolysis, being the only endogenous ligand known to bind specifically to the kringle 4 domain of plasminogen. TN was originally isolated from plasma, but shows a wide tissue distribution. Furthermor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d16091f3a5345e027e05fc0d7a55c44c
https://doi.org/10.1107/s0907444997016806
https://doi.org/10.1107/s0907444997016806
Autor:
Flemming M. Poulsen, Lars Ellgaard, Peter Reinholt Nielsen, Hans Christian Thøgersen, Michael Etzerodt
Publikováno v:
Proceedings of the National Academy of Sciences. 94:7521-7525
The three-dimensional structure of the N-terminal domain (residues 18–112) of α2-macroglobulin receptor-associated protein (RAP) has been determined by NMR spectroscopy. The structure consists of three helices composed of residues 23–34, 39–65
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ad6f1cad50a33242b664a6ef376464d
https://doi.org/10.1073/pnas.94.14.7521
https://doi.org/10.1073/pnas.94.14.7521