Results 1 to 10 of about 82,135 (263)
The GTP binding proteins Gem and Rad are negative regulators of the Rho–Rho kinase pathway [PDF]
The Journal of Cell Biology, 2002 The cytoskeletal changes that alter cellular morphogenesis and motility depend upon a complex interplay among molecules that regulate actin, myosin, and other cytoskeletal components. The Rho family of GTP binding proteins are important upstream mediators of cytoskeletal organization.
Yvona Ward +6 more
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Small GTP-binding protein Rho-mediated signaling promotes proliferation of rheumatoid synovial fibroblasts. [PDF]
Arthritis Research & Therapy, 2005 AbstractRho is a major small GTP-binding protein that is involved in the regulation of various cell functions, including proliferation and cell migration, through activation of multiple signaling molecules in various types of cells. We studied its roles in synovial fibroblasts (SFs) in patients with rheumatoid arthritis (RA) and clarified its relevance
Shingo Nakayamada +4 more
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Interaction of mastoparan with the low molecular mass GTP‐binding proteins rho/rac [PDF]
FEBS Letters, 1991 Mastoparan, which has been shown to active G proteins [1], inhibits the ADP‐ribosylation of 20 kDa human platelet membrane proteins catalyzed by Clostridium botulinum exoenzyme C3 half‐maximally and maximally (90%) at 20 and 100 μM concentrations, respectively. Inhibition of ADP‐ribosylation was enhanced by GTP‐γS.
Gertrud Koch +4 more
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Signal transduction through the GTP-binding proteins Rac and Rho [PDF]
Journal of Cell Science, 1994 ABSTRACT Actin reorganization is an early response to many extra- cellular factors. In Swiss 3T3 fibroblasts, the Ras-related GTP-binding proteins Rho and Rac act as key signal trans- ducers in these responses: Rho is required for growth factor-induced formation of stress fibres and focal adhesions, whereas membrane ruffling is regulated
Anne J. Ridley
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Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton [PDF]
The EMBO Journal, 1999 Soluble factors from serum such as lysophosphatidic acid (LPA) are thought to activate the small GTP-binding protein Rho based on their ability to induce actin stress fibers and focal adhesions in a Rho-dependent manner. Cell adhesion to extracellular matrices (ECM) has also been proposed to activate Rho, but this point has been controversial due to ...
Xiang-Dong Ren
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Flux Analysis in Process Models via Causality [PDF]
Electronic Proceedings in Theoretical Computer Science, 2010 We present an approach for flux analysis in process algebra models of biological systems. We perceive flux as the flow of resources in stochastic simulations. We resort to an established correspondence between event structures, a broadly recognised model
Ozan Kahramanoğulları
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Structure of the Rho Family GTP-Binding Protein Cdc42 in Complex with the Multifunctional Regulator RhoGDI [PDF]
Cell, 2000 The RhoGDI proteins serve as key multifunctional regulators of Rho family GTP-binding proteins. The 2.6 A X-ray crystallographic structure of the Cdc42/RhoGDI complex reveals two important sites of interaction between GDI and Cdc42. First, the amino-terminal regulatory arm of the GDI binds to the switch I and II domains of Cdc42 leading to the ...
Gregory R. Hoffman +2 more
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Fluoride Activation of the Rho Family GTP-binding Protein Cdc42Hs [PDF]
Journal of Biological Chemistry, 1998 Aluminum tetrafluoride (AlF4-) activation of heterotrimeric G-protein alpha-subunits is a well established aspect of the biochemistry of these proteins; however, until recently it has been thought that AlF4- does not mediate effects on the Ras superfamily of low molecular weight GTP-binding proteins.
Gregory R. Hoffman +3 more
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Intrasynaptosomal distribution of the ras, rho and smg-25A GTP-binding proteins in bovine brain [PDF]
Molecular Brain Research, 1989 We have purified to near homogeneity and characterized three small molecular weight (Mr) GTP-binding proteins, the c-Ki-ras protein (c-Ki-ras p21), the rho protein (rho p20) and a novel smg-25A protein (smg p25A), from bovine brain crude membranes.
Shigekuni Kim +3 more
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rho, a Small GTP-Binding Protein, Is Essential for Shigella Invasion of Epithelial Cells [PDF]
The Journal of Experimental Medicine, 1997 Shigella, the causative agents of bacillary dysentery, are capable of invading mammalian cells that are not normally phagocytic. Uptake of bacteria by the mammalian cells is directed by bacterial factors named IpaB, IpaC, and IpaD invasins, in which Ipa invasins secreted into the bacterial environment can interact with α5β1 integrin.
Masahisa Watarai +3 more
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