K
Keld Danø
Researcher at University of Southern Denmark
Publications - 8
Citations - 1072
Keld Danø is an academic researcher from University of Southern Denmark. The author has contributed to research in topics: Plasminogen activator & Urokinase receptor. The author has an hindex of 8, co-authored 8 publications receiving 1039 citations. Previous affiliations of Keld Danø include National Institutes of Health & Icahn School of Medicine at Mount Sinai.
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Journal ArticleDOI
One-chain urokinase-type plasminogen activator from human sarcoma cells is a proenzyme with little or no intrinsic activity.
TL;DR: One-chain u-PA has a variety of properties similar to the one-chain proenzyme forms of other serine proteases and that it should, therefore, be considered as a genuine proen enzyme form of U-PA.
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Plasminogen activator inhibitor from human fibrosarcoma cells binds urokinase-type plasminogen activator, but not its proenzyme.
TL;DR: An approximately 75% pure form of a human Mr approximately 54,000 plasminogen activator inhibitor from conditioned culture fluid of the fibrosarcoma cell line HT-1080 was obtained by a single step of chromatography on concanavalin A-Sepharose.
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Peptide-Derived Antagonists of the Urokinase Receptor. Affinity Maturation by Combinatorial Chemistry, Identification of Functional Epitopes, and Inhibitory Effect on Cancer Cell Intravasation†
Michael Ploug,Søren Østergaard,Henrik Gårdsvoll,Katherine Kovalski,Claus Holst-Hansen,Arne Holm,Liliana Ossowski,Keld Danø +7 more
TL;DR: Design of small organic molecules mimicking the binding determinants of this 9-mer peptide antagonist of the uPA-uPAR interaction demonstrating specific, high-affinity binding to human uPAR may have a potential application in combination therapy for certain types of cancer.
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A urokinase receptor-associated protein with specific collagen binding properties.
TL;DR: A novel protein, designated uPARAP, is a member of the macrophage mannose receptor protein family and contains a putative collagen-binding domain in addition to 8 C-type carbohydrate recognition domains that proved capable of binding strongly to a single type of collagen, collagen V.
Journal ArticleDOI
Ligand interaction between urokinase-type plasminogen activator and its receptor probed with 8-anilino-1-naphthalenesulfonate. Evidence for a hydrophobic binding site exposed only on the intact receptor
TL;DR: It is reported that intact uPAR binds the low molecular weight fluorophore 8-anilino-1-naphthalenesulfonate (ANS) to form a 1:1 stoichiometric complex and that the resulting enhancement of the ANS fluorescence probes the functional state of uPAR as judged by several independent criteria.