Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Benjamin P. Bohl"'
Publikováno v:
Journal of Biological Chemistry. 283:12736-12746
The NADPH oxidases (Noxs) are a family of superoxide-generating enzymes implicated in a variety of biological processes. Full activity of Nox1, -2, and -3 requires the action of a Rac GTPase. A direct regulatory interaction of Rac with Nox2 has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f7445e3da2789e363ac9609d7186ec0
https://doi.org/10.1074/jbc.m801010200
https://doi.org/10.1074/jbc.m801010200
Publikováno v:
Journal of Biological Chemistry. 274:13198-13204
A major function of Rac2 in neutrophils is the regulation of oxidant production important in bacterial killing. Rac and the related GTPase Cdc42 also regulate the dynamics of the actin cytoskeleton, necessary for leukocyte chemotaxis and phagocytosis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76e316cde0136f8ed4c4285963137fe9
https://doi.org/10.1074/jbc.274.19.13198
https://doi.org/10.1074/jbc.274.19.13198
Publikováno v:
Journal of Biological Chemistry. 269:30749-30752
When the neutrophil NADPH oxidase is activated to generate superoxide, the cytosolic components, p47phox, p67phox, and the GTP-binding protein Rac, become stably associated with the plasma membrane. The translocation of p47phox and p67phox is depende
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f616a09b014af6686603adcaf2aa0747
https://doi.org/10.1016/s0021-9258(18)47341-3
https://doi.org/10.1016/s0021-9258(18)47341-3
Publikováno v:
Journal of Biological Chemistry. 269:31674-31679
GTP-binding proteins of the Rho family are maintained as cytosolic complexes with RhoGDI in resting cells, but are released and translocate to the membrane during the course of cell activation. Membrane association of Rac/Rho/CDC42 was specifically i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::68e07416c26e70387f5246dce0c51d56
https://doi.org/10.1016/s0021-9258(18)31748-4
https://doi.org/10.1016/s0021-9258(18)31748-4
Publikováno v:
Journal of Biological Chemistry. 268:26206-26211
Members of the Rho family of GTP-binding proteins are localized in the cytosol of cells by complexation with a protein known as (Rho)GDI. We show by sucrose gradient equilibrium sedimentation analysis that all of the Rac protein present in human neut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::34c75ff81974a6204e3eb6da71928ec6
https://doi.org/10.1016/s0021-9258(19)74301-4
https://doi.org/10.1016/s0021-9258(19)74301-4
Autor:
Gary M. Bokoch, Benjamin P. Bohl, Charles C. King, Mira Krendel, Céline DerMardirossian, Frank Zenke
Publikováno v:
The Journal of biological chemistry. 279(18)
GEF-H1 is a guanine nucleotide exchange factor for Rho whose activity is regulated through a cycle of microtubule binding and release. Here we identify a region in the carboxyl terminus of GEF-H1 that is important for suppression of its guanine nucle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d5ea5f7625fed6cd7bfcf9a7eb34e2c
https://pubmed.ncbi.nlm.nih.gov/14970201
https://pubmed.ncbi.nlm.nih.gov/14970201
Autor:
Kersi Pestonjamasp, Gary M. Bokoch, Chester E. Chamberlain, Elisabeth Gardiner, Benjamin P. Bohl, Klaus M. Hahn
Publikováno v:
Current biology : CB. 12(23)
The ability of cells to recognize and respond with directed motility to chemoattractant agents is critical to normal physiological function. Neutrophils represent the prototypic chemotactic cell in that they respond to signals initiated through the b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eaddb36435d3c973945a47c9f9fa8bce
https://pubmed.ncbi.nlm.nih.gov/12477392
https://pubmed.ncbi.nlm.nih.gov/12477392
Autor:
Gary M. Bokoch, Benjamin P. Bohl, Elisabeth M. Gardiner, Charles C. King, Brian A. Hemmings, Alexandra C. Newton, Frank Zenke
Publikováno v:
The Journal of biological chemistry. 275(52)
In this study, we show that phosphorylated 3-phosphoinositide-dependent kinase 1 (PDK1) phosphorylates p21-activated kinase 1 (PAK1) in the presence of sphingosine. We identify threonine 423, a conserved threonine in the activation loop of kinase sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e67326d25ac450a8f24c18131fabec6c
https://pubmed.ncbi.nlm.nih.gov/10995762
https://pubmed.ncbi.nlm.nih.gov/10995762
Publikováno v:
Science. 254:1794-1796
Rap1A is a low molecular weight guanosine triphosphate (GTP)-binding protein in human neutrophil membranes whose cellular function is unknown. Rap1A was found to form stoichiometric complexes with the cytochrome b558 component of the phagocyte nicoti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55a50957773d4f33e91e1fbd22038120
https://doi.org/10.1126/science.1763330
https://doi.org/10.1126/science.1763330
Publikováno v:
The Journal of biological chemistry. 274(46)
p21-activated kinases (Pak)/Ste20 kinases are regulated in vitro and in vivo by the small GTP-binding proteins Rac and Cdc42 and lipids, such as sphingosine, which stimulate autophosphorylation and phosphorylation of exogenous substrates. The mechani
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0706f420136f9848bc33da5e58bdae2
https://pubmed.ncbi.nlm.nih.gov/10551809
https://pubmed.ncbi.nlm.nih.gov/10551809