Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Ben G.J.M. Bolscher"'
Autor:
Wilhelm Kaulfersch, P. M. Hilarius, Ben G.J.M. Bolscher, Ron S. Weening, Reinhard A. Seger, Dirk Roos, Arthur J. Verhoeven, Jeanette H. W. Leusen
Publikováno v:
The Journal of Experimental Medicine
Journal of experimental medicine, 180(6), 2329-2334. Rockefeller University Press
Journal of experimental medicine, 180(6), 2329-2334. Rockefeller University Press
Src homology 3 (SH3) domains have been suggested to play an important role in the assembly of the superoxide-forming nicotinamide adenine dinucleotide phosphate (NADPH) oxidase upon activation of phagocytes, which involves the association of membrane
Autor:
M de Boer, Stuart H. Orkin, Ben G.J.M. Bolscher, C. I. E. Smith, Anders Åhlin, Ron S. Weening, Mary C. Dinauer, Dirk Roos
Publikováno v:
Blood. 80:1553-1558
Chronic granulomatous disease (CGD) is characterized by the absence of a respiratory burst in activated phagocytes. Defects in at least four different genes lead to CGD. Patients with the X-linked form of CGD have mutations in the gene for the beta-s
Publikováno v:
Journal of Biological Chemistry. 265:15782-15787
Neutrophil NADPH:O2 oxidoreductase activity, essential in the killing of bacteria by neutrophils, can be elicited in a cell-free system that requires plasma membranes, cytosol and sodium dodecyl sulfate. In addition, GTP or its nonhydrolyzable analog
Publikováno v:
Journal of Biological Chemistry. 265:924-930
Phagocytic leukocytes contain an activatable NADPH:O2 oxidoreductase. Components of this enzyme system include cytochrome b558, and three soluble oxidase components (SOC I, SOC II, and SOC III) found in the cytosol of resting cells. Previously, we fo
Autor:
Dirk Roos, Ben G.J.M. Bolscher, R van Zwieten, Arthur J. Verhoeven, L. J. Van Pelt, Ron S. Weening
Publikováno v:
Journal of immunological methods, 191(2), 187-196. Elsevier
Intracellular oxidation of dihydrorhodamine 123 (DHR) to the fluorescent compound rhodamine 123 (Rho123) was used to detect the production of oxygen metabolites in activated neutrophils. Total leukocyte preparations can be used in this assay, which i
Autor:
Jeanette H. W. Leusen, P. M. Hilarius, Ben G.J.M. Bolscher, Arthur J. Verhoeven, Dirk Roos, Kees Fluiter
Publikováno v:
Journal of biological chemistry, 270(19), 11216-11221. American Society for Biochemistry and Molecular Biology Inc.
Activation of the human NADPH oxidase requires the interaction of at least four cytosolic proteins and one membrane-bound heterodimeric protein. Src homology 3 (SH3) domains and their proline-rich counterstructures have been shown to play an importan
Publikováno v:
Mononuclear Phagocytes ISBN: 9789048141715
Phagocytic leukocytes (neutrophilic granulocytes, eosinophilic granulocytes, monocytes and macrophages) are effector cells in our defense against microbial pathogens. Phagocytes kill a variety of microorganisms by ingesting them and attacking them in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::25c94522a1ad177aaddf9cf474b6a316
https://doi.org/10.1007/978-94-015-8070-0_32
https://doi.org/10.1007/978-94-015-8070-0_32
Autor:
Ron S. Weening, Dirk Roos, R van Zwieten, Louis Jan Meerhof, Arthur J. Verhoeven, Ben G.J.M. Bolscher, Jaap Keijer
Publikováno v:
Blood. 73:1686-1694
Monoclonal antibodies (MoAbs) were raised against cytochrome b558, a membrane-bound component of the NADPH:O2 oxidoreductase in human neutrophils. This cytochrome consists of a low-molecular-weight (low- mol-wt) subunit of 22 to 23 Kd, probably encod
Publikováno v:
FEBS Letters. (1):269-273
The NADPH oxidase of human eosinophils, measured in the cell-free system, shows the same characteristics as the enzyme from human neutrophils. All proteins required for activity of the enzyme are expressed in eosinophils at a higher level than in neu
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 784:189-191
Ascorbic acid (vitamin C) was found to stimulate the chlorinating activity of human myeloperoxidase (donor:hydrogen peroxide oxidoreductase, EC 1.11.1.7) 3-fold in vitro and to shift the pH optimum of the reaction to higher pH values. These effects a