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Angiostatin binds ATP synthase on the surface of human endothelial cells

Autor: Moser, T L, Stack, M S, Asplin, I, Enghild, J J, Højrup, P, Everitt, L, Hubchak, S, Schnaper, H W, Pizzo, S V

Publikováno v: Moser, T L, Stack, M S, Asplin, I, Enghild, J J, Højrup, P, Everitt, L, Hubchak, S, Schnaper, H W & Pizzo, S V 1999, ' Angiostatin binds ATP synthase on the surface of human endothelial cells ', Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 6, pp. 2811-6 .

Udgivelsesdato: 1999-Mar-16 Angiostatin, a proteolytic fragment of plasminogen, is a potent antagonist of angiogenesis and an inhibitor of endothelial cell migration and proliferation. To determine whether the mechanism by which angiostatin inhibits

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pure_au_____::31c4c1af0bd1606ce5b27f6b154100ca
https://pure.au.dk/portal/da/publications/angiostatin-binds-atp-synthase-on-the-surface-of-human-endothelial-cells(50cfdf20-8657-11dd-a5a8-000ea68e967b).html

Isolation of an angiostatin receptor from the membranes of human umbilical vein endothehal cells

Autor: Moser, T. L., Pizzo, S. V., Jan Johannes Enghild, Hubchak, S., Sharon Stack, M.

Publikováno v: Moser, T L, Pizzo, S V, Enghild, J J, Hubchak, S & Sharon Stack, M 1997, ' Isolation of an angiostatin receptor from the membranes of human umbilical vein endothehal cells ', Fibrinolysis and Proteolysis, vol. 11, no. SUPPL. 3 .
Scopus-Elsevier

Angiostatin, a kringle-containing fragment of plasminogen, is a potent antagonist of angiogenesis, resulting from its ability to inhibit endothelial cell migration and proliferation. To test the hypothesis that alteration of the biologic properties o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::146cf48494bd994857bd52c139c184d6
https://pure.au.dk/portal/da/publications/isolation-of-an-angiostatin-receptor-from-the-membranes-of-human-umbilical-vein-endothehal-cells(77fa620f-3ded-43a6-bb16-a0eb462bb506).html

The potential role of alpha 2-macroglobulin in the control of cysteine proteinases (gingipains) from Porphyromonas gingivalis

Autor: Grøn, H, Pike, R, Potempa, J, Travis, J, Thøgersen, I B, Enghild, J J, Pizzo, S V

Publikováno v: Grøn, H, Pike, R, Potempa, J, Travis, J, Thøgersen, I B, Enghild, J J & Pizzo, S V 1997, ' The potential role of alpha 2-macroglobulin in the control of cysteine proteinases (gingipains) from Porphyromonas gingivalis ', Journal of Periodontal Research, vol. 32, no. 1 Pt 1, pp. 61-8 .

Udgivelsesdato: 1997-Jan Porphyromonas gingivalis is closely associated with the development of some forms of periodontitis. The major cysteine proteinases released by this bacterium hydrolyze peptide bonds only after arginyl (gingipain R) or lysyl r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pure_au_____::edac68290c367fdea3cf06cc3c857a89
https://pure.au.dk/portal/da/publications/the-potential-role-of-alpha-2macroglobulin-in-the-control-of-cysteine-proteinases-gingipains-from-porphyromonas-gingivalis(548f4d90-8656-11dd-a5a8-000ea68e967b).html

Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein

Autor: Valnickova, Z, Thøgersen, Ida, Christensen, S, Chu, C T, Pizzo, S V, Enghild, J J

Publikováno v: Valnickova, Z, Thøgersen, I, Christensen, S, Chu, C T, Pizzo, S V & Enghild, J J 1996, ' Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein ', Journal of Biological Chemistry, vol. 271, no. 22, pp. 12937-43 .

Udgivelsesdato: 1996-May-31 A 66-kDa glycosylated carboxypeptidase, plasma pro-carboxypeptidase B (pro-plasma CPB), has recently been identified in human blood (Eaton, D. L., Malloy, B. E., Tsai, S. P., Henzel, W., and Drayna, D. (1991) J. Biol. Chem

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pure_au_____::f2f8fb0f81341a6247e5859d623da3eb
https://pure.au.dk/portal/da/publications/activated-human-plasma-carboxypeptidase-b-is-retained-in-the-blood-by-binding-to-alpha2macroglobulin-and-pregnancy-zone-protein(e5b74bc0-8655-11dd-a5a8-000ea68e967b).html