Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Mary Ann Sells"'
Autor:
Annette Schürmann, Sandra L. Schmid, Jonathan Chernoff, Gary M. Bokoch, Mary Ann Sells, Suranganie Dharmawardhane
Publikováno v:
Molecular Biology of the Cell. 11:3341-3352
The process of macropinocytosis is an essential aspect of normal cell function, contributing to both growth and motile processes of cells. p21-activated kinases (PAKs) are targets for activated Rac and Cdc42 guanosine 5′-triphosphatases and have be
Publikováno v:
The Journal of Cell Biology
The p21 (Cdc42/Rac) activated kinase Pak1 regulates cell morphology and polarity in most, if not all, eukaryotic cells. We and others have established that Pak's effects on these parameters are mediated by changes in the organization of cortical acti
Autor:
Juliane P. Caviston, Mary Ann Sells, Jonathan Chernoff, Justin T. Barratt, Sabine Ottilie, Ekkehard Leberer
Publikováno v:
Journal of Biological Chemistry. 273:18490-18498
p21-activated kinases (PAKs) bind to and are activated by Rho family GTPases such as Cdc42 and Rac. Since these GTPases play key roles in regulating cell polarity, stress responses, and cell cycle progression, the ability of PAK to affect these proce
Publikováno v:
Scopus-Elsevier
We have recently shown that protein tyrosine phosphatase 1B (PTP1B) associates with the docking protein p130Cas in 3Y1 rat fibroblasts. This interaction is mediated by a proline-rich sequence on PTP1B and the SH3 domain on p130Cas. Expression of wild
Autor:
Gary M. Bokoch, Mary Ann Sells, Jonathan Chernoff, Ulla G. Knaus, Diane M. Ambrose, Shubha Bagrodia
Publikováno v:
Current Biology. 7:202-210
Background: The Rho family GTPases Cdc42, Rac1 and RhoA regulate the reorganization of the actin cytoskeleton induced by extracellular signals such as growth factors. In mammalian cells, Cdc42 regulates the formation of filopodia, whereas Rac regulat
Autor:
Andrew S. McDaniel, Shi Chen, Waylan K. Bessler, Jeffrey B. Travers, Ethel Derr-Yellin, Su Jung Park, Sarah J. Burgin, Jayme D. Allen, Clemens Hofmann, Zahara M. Jaffer, Mary Ann Sells, Simon J. Atkinson, Elizabeth G. Michels, David A. Ingram, Jonathan Chernoff, D. Wade Clapp
Mast cells are key participants in allergic diseases via activation of high-affinity IgE receptors (FcϵRI) resulting in release of proinflammatory mediators. The biochemical pathways linking IgE activation to calcium influx and cytoskeletal changes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9be012ae42cb0ab872caa92fb35724db
https://europepmc.org/articles/PMC2661857/
https://europepmc.org/articles/PMC2661857/
Autor:
Shengjia Zhang, Mary Ann Sells, Jonathan Chernoff, Richard J. Ulevitch, Ulla G. Knaus, Jiahuai Han, Gary M. Bokoch
Publikováno v:
Journal of Biological Chemistry. 270:23934-23936
The stress-activated p38 mitogen-activated protein (MAP) kinase defines a subgroup of the mammalian MAP kinases that appear to play a key role in regulating inflammatory responses. Co-expression of constitutively active forms of Rac and Cdc42 leads t
Publikováno v:
The Journal of Cell Biology
p21-activated kinases (Paks) are effectors of the small GTPases Cdc42 and Rac, and are thought to mediate some of the cytoskeletal and transcriptional activities of these proteins. To localize activated Pak1 in cells, we developed an antibody directe
Autor:
Gary M. Bokoch, L. C. Sanders, Andrew Mooney, Mary Ann Sells, John C. Reed, Hong Gang Wang, Annette Schürmann
Publikováno v:
Molecular and cellular biology. 20(2)
Bad is a critical regulatory component of the intrinsic cell death machinery that exerts its death-promoting effect upon heterodimerization with the antiapoptotic proteins Bcl-2 and Bcl-x(L). Growth factors promote cell survival through phosphorylati
Autor:
Ulla G. Knaus, Yan Wang, Lawrence A. Quilliam, Benjamin P. Bohl, Gary M. Bokoch, Mary Ann Sells
Publikováno v:
The Journal of biological chemistry. 271(42)
The p21-activated kinases (PAKs) link G protein-coupled receptors and growth factor receptors (S. Dharmawardhane, R. H. Daniels, and G. M. Bokoch, submitted for publication) to activation of MAP kinase cascades and to cytoskeletal reorganization (M.