Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Ariel Mizrahi"'
Autor:
Monat Shay, Possti Maayan, Junaid Ullah, Yaniv Ariel, Mizrahi Bar, Drori Ofek, Seifert Avraham
Publikováno v:
Aerospace Europe Conference 2020 (AEC2020)
Publikováno v:
Journal of Biological Chemistry. 282:22122-22139
The superoxide-generating NADPH oxidase is converted to an active state by the assembly of a membrane-localized cytochrome b(559) with three cytosolic components: p47(phox), p67(phox), and GTPase Rac1 or Rac2. Assembly involves two sets of protein-pr
Autor:
Yevgeny Berdichevsky, Shahar Molshanski-Mor, Yara Gorzalczany, Iris Dahan, Miriam Hirshberg, Nathalie Alloul, Rive Sarfstein, Yael Nakash, Yelena Ugolev, Edgar Pick, Ariel Mizrahi
Publikováno v:
Journal of Leukocyte Biology. 79:881-895
Phagocytes generate superoxide (O2.−) by an enzyme complex known as reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase. Its catalytic component, responsible for the NADPH-driven reduction of oxygen to O2.−, is flavocytochrome b55
Autor:
Carolyn Weinbaum, Shahar Molshanski-Mor, Ariel Mizrahi, Miriam Hirshberg, Yi Zheng, Edgar Pick
Publikováno v:
Journal of Biological Chemistry. 280:3802-3811
Activation of the phagocyte NADPH oxidase is the consequence of the assembly of membranal cytochrome b559 with the cytosolic components p47phox, p67phox, and the GTPase Rac and is mimicked by a cell-free system comprising these components and an acti
Autor:
Carolyn Weinbaum, Yara Gorzalczany, Ariel Mizrahi, Miriam Hirshberg, Shahar Molshanski-Mor, Rive Sarfstein, Edgar Pick, Marie-Claire Dagher, Yevgeny Berdichevsky
Publikováno v:
Journal of Biological Chemistry. 279:16007-16016
NADPH oxidase activation involves the assembly of membrane-localized cytochrome b559 with the cytosolic components p47phox, p67phox, and the small GTPase Rac. Assembly is mimicked by a cell-free system consisting of membranes and cytosolic components
Autor:
Jacek Biesiada, Jarek Meller, William L. Seibel, Yi Zheng, Sachin Kumar, Kathleen Szczur, Ariel Mizrahi, Marie-Dominique Filippi, Filippo Marchioni, Mirosław Kordos, Edgar Pick, Emily E. Bosco
Summary The NADPH oxidase enzyme complex, NOX2, is responsible for reactive oxygen species production in neutrophils and has been recognized as a key mediator of inflammation. Here, we have performed rational design and in silico screen to identify a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::baadaaabe1321dd53d925e712b077e53
https://europepmc.org/articles/PMC3292765/
https://europepmc.org/articles/PMC3292765/
Publikováno v:
The Journal of biological chemistry. 285(33)
The superoxide-generating NADPH oxidase complex of resting phagocytes includes cytochrome b(559), a membrane-associated heterodimer composed of two subunits (Nox2 and p22(phox)), and four cytosolic proteins (p47(phox), p67(phox), Rac, and p40(phox)).
Autor:
Shahar, Molshanski-Mor, Ariel, Mizrahi, Yelena, Ugolev, Iris, Dahan, Yevgeny, Berdichevsky, Edgar, Pick
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 412
The superoxide (O2-)-generating enzyme complex of phagocytes, known as the NADPH oxidase, can be assayed in a number of in vitro cell-free (or broken cell) systems. These consist of a mixture of the individual components of the NADPH oxidase, derived
Publikováno v:
The Journal of biological chemistry. 282(30)
The superoxide-generating NADPH oxidase is converted to an active state by the assembly of a membrane-localized cytochrome b(559) with three cytosolic components: p47(phox), p67(phox), and GTPase Rac1 or Rac2. Assembly involves two sets of protein-pr