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Neutrophils engage the kallikrein-kinin system to open up the endothelial barrier in acute inflammation.
Kenne E, Rasmuson J, Renné T, Vieira ML, Müller-Esterl W, Herwald H, Lindbom L. Kenne E, et al. Among authors: herwald h. FASEB J. 2019 Feb;33(2):2599-2609. doi: 10.1096/fj.201801329R. Epub 2018 Oct 3. FASEB J. 2019. PMID: 30281335
-Kenne, E., Rasmuson, J., Renne, T., Vieira, M. L., Muller-Esterl, W., Herwald, H., Lindbom, L. Neutrophils engage the kallikrein-kinin system to open up the endothelial barrier in acute inflammation....
-Kenne, E., Rasmuson, J., Renne, T., Vieira, M. L., Muller-Esterl, W., Herwald, H., Lindbom, L. Neutrophils engage the kallikr …
Isolation and characterization of the kininogen-binding protein p33 from endothelial cells. Identity with the gC1q receptor.
Herwald H, Dedio J, Kellner R, Loos M, Müller-Esterl W. Herwald H, et al. J Biol Chem. 1996 May 31;271(22):13040-7. doi: 10.1074/jbc.271.22.13040. J Biol Chem. 1996. PMID: 8662673 Free article.
Two domains of the kininogens expose major cell binding sites: domain D3 that is shared by H- and L-kininogen and domain D5H that is exclusively present in H-kininogen. Previously we have mapped the kininogen cell binding sites to 27 residues of D3 ("LDC27") and 20 …
Two domains of the kininogens expose major cell binding sites: domain D3 that is shared by H- and L-kininogen and domain D5H that is …
183 results