Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Eva Louise Lange"'
Autor:
Tobias Kromann-Hansen, Eva Louise Lange, Hans Peter Sørensen, Gholamreza Hassanzadeh-Ghassabeh, Mingdong Huang, Jan K. Jensen, Serge Muyldermans, Paul J. Declerck, Elizabeth A. Komives, Peter A. Andreasen
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Abstract Although trypsin-like serine proteases have flexible surface-exposed loops and are known to adopt higher and lower activity conformations, structural determinants for the different conformations have remained largely obscure. The trypsin-lik
Externí odkaz:
https://doaj.org/article/409897e4334a4c2c81d516f9a73f9d64
Autor:
Tobias Kromann-Hansen, Eva Louise Lange, Ida K Lund, Gunilla Høyer-Hansen, Peter A Andreasen, Elizabeth A Komives
Publikováno v:
PLoS ONE, Vol 13, Iss 2, p e0192661 (2018)
The catalytic activity of trypsin-like serine proteases is in many cases regulated by conformational changes initiated by binding of physiological modulators to exosites located distantly from the active site. A trypsin-like serine protease of partic
Externí odkaz:
https://doaj.org/article/e330651c2ec4416eab304ecffe07f697
Autor:
Ida K. Lund, Tobias Kromann-Hansen, Eva Louise Lange, Gunilla Høyer-Hansen, Elizabeth A. Komives, Peter A. Andreasen
Publikováno v:
PLoS ONE, Vol 13, Iss 2, p e0192661 (2018)
Kromann-Hansen, T, Lange, E L, Lund, I K, Høyer-Hansen, G, Andreasen, P A & Komives, E A 2018, ' Ligand binding modulates the structural dynamics and activity of urokinase-Type plasminogen activator : A possible mechanism of plasminogen activation ', PLoS ONE, vol. 13, no. 2, e0192661, pp. 1-16 . https://doi.org/10.1371/journal.pone.0192661
PLoS ONE
Kromann-Hansen, T, Lange, E L, Lund, I K, Høyer-Hansen, G, Andreasen, P A & Komives, E A 2018, ' Ligand binding modulates the structural dynamics and activity of urokinase-type plasminogen activator : A possible mechanism of plasminogen activation ', P L o S One, vol. 13, no. 2, e0192661 . https://doi.org/10.1371/journal.pone.0192661
Kromann-Hansen, T, Lange, E L, Lund, I K, Høyer-Hansen, G, Andreasen, P A & Komives, E A 2018, ' Ligand binding modulates the structural dynamics and activity of urokinase-Type plasminogen activator : A possible mechanism of plasminogen activation ', PLoS ONE, vol. 13, no. 2, e0192661, pp. 1-16 . https://doi.org/10.1371/journal.pone.0192661
PLoS ONE
Kromann-Hansen, T, Lange, E L, Lund, I K, Høyer-Hansen, G, Andreasen, P A & Komives, E A 2018, ' Ligand binding modulates the structural dynamics and activity of urokinase-type plasminogen activator : A possible mechanism of plasminogen activation ', P L o S One, vol. 13, no. 2, e0192661 . https://doi.org/10.1371/journal.pone.0192661
The catalytic activity of trypsin-like serine proteases is in many cases regulated by conformational changes initiated by binding of physiological modulators to exosites located distantly from the active site. A trypsin-like serine protease of partic
Autor:
Hans Peter Sørensen, Gholamreza Hassanzadeh-Ghassabeh, Tobias Kromann-Hansen, Jan K. Jensen, Eva Louise Lange, Paul Declerck, Mingdong Huang, Peter A. Andreasen, Serge Muyldermans, Elizabeth A. Komives
Publikováno v:
Scientific reports 7(1), 3385 (2017). doi:10.1038/s41598-017-03457-7
Kromann-Hansen, T, Louise Lange, E, Peter Sørensen, H, Hassanzadeh-Ghassabeh, G, Huang, M, Jensen, J K, Muyldermans, S, Declerck, P J, Komives, E A & Andreasen, P A 2017, ' Discovery of a novel conformational equilibrium in urokinase-type plasminogen activator ', Scientific Reports, vol. 7, no. 1, 3385 . https://doi.org/10.1038/s41598-017-03457-7
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Kromann-Hansen, T, Louise Lange, E, Peter Sørensen, H, Hassanzadeh-Ghassabeh, G, Huang, M, Jensen, J K, Muyldermans, S, Declerck, P J, Komives, E A & Andreasen, P A 2017, ' Discovery of a novel conformational equilibrium in urokinase-type plasminogen activator ', Scientific Reports, vol. 7, no. 1, 3385 . https://doi.org/10.1038/s41598-017-03457-7
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific reports 7(1), 3385(2017). doi:10.1038/s41598-017-03457-7
Although trypsin-like serine proteases have flexible surface-exposed loops and are known to adopt higher and lower activity conformations, structural determinants for the differ
Although trypsin-like serine proteases have flexible surface-exposed loops and are known to adopt higher and lower activity conformations, structural determinants for the differ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b8a60fa2e54ed2bb651d377a867684d
https://bib-pubdb1.desy.de/record/330033
https://bib-pubdb1.desy.de/record/330033
Autor:
Terry F. Plasse, Christine R. Schar, Jan K. Jensen, Emil Oldenburg, Mark L. Levitt, Eric M. Towler, Eva Louise Lange, Reza Fathi, Danielle T. Abramson
Publikováno v:
Cancer Research. 78:4200-4200
WX-UK1 (the active metabolite of upamostat) was originally developed as an inhibitor of the serine protease urokinase (uPA) with a Ki ~1 uM. To identify more sensitive targets, we performed a bioinformatic analysis of the ~200 human trypsin-like seri
Autor:
Eva Louise Lange, Reza Fathi, Danielle T. Abramson, Mark L. Levitt, Jan K. Jensen, Terry F. Plasse, Christine R. Schar, Emil Oldenberg
Publikováno v:
Molecular Cancer Therapeutics. 17:B055-B055
WX-UK1, a multi-serine protease inhibitor, was believed to function primarily as a synthetic small-molecule inhibitor of urokinase (uPA). We now reveal that WX-UK1 is a potent and rather specific inhibitor of human trypsin-2 and human trypsin-3, and