Results 251 to 260 of about 4,439,363 (293)

Regulation of macrophage adhesion and migration by Rho GTP‐binding proteins

Journal of Microscopy, 2008
SummaryThe Rho family proteins Rac and Rho are believed to be key regulators of cell migration through their effects on the cytoskeleton and cell adhesion. However, recent studies in macrophages indicate that they are not always essential for migration, although they do affect cell shape and adhesion.
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The Role of Prenylated Small GTP-Binding Proteins in the Regulation of Osteoclast Function

Calcified Tissue International, 2003
The Ras superfamily of small GTP-binding proteins (also known as small GTPases) comprises more than 80 highly conserved proteins of the Ras, Rho, and Rab subfamilies that are involved in multiple intracellular signalling pathways. These proteins are able to function as molecular switches in the transduction of signals from membrane receptors by cycling
F P, Coxon, M J, Rogers
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Regulation of phospholipase D by low molecular weight GTP-binding proteins

Journal of Lipid Mediators and Cell Signalling, 1996
Phospholipase D (PLD) is believed to play an important role in cell signal transduction: PLD catalyzes the hydrolysis primarily of phosphatidylcholine (PC) to produce phosphatidic acid that may serve as a lipid second messenger. Although the mechanism of PLD activation has not yet been fully understood, a member of the low molecular weight GTP-binding ...
Y, Kanaho, T, Yokozeki, H, Kuribara
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Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins

Current Opinion in Cell Biology, 1994
Recent progress in our understanding of the regulation of the phagocyte NADPH oxidase by the Rac GTP-binding protein(s) has provided the first detailed glimpse into the mechanisms of leukocyte regulation by a small GTP-binding protein. Studies over the past year have indicated that the activity of the NADPH oxidase can be modulated by regulation of the
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Regulation of phagocyte function by low molecular weight GTP‐binding proteins

European Journal of Haematology, 1993
Abstract:  The mechanisms used by phagocytic leukocytes in the process of bacterial killing are regulated by GTP‐binding proteins of the Ras superfamily. In particular, the formation of toxic oxygen metabolites via the NADPH oxidase requires the action of both Rac and Rap1A proteins.
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Regulation of rod GTP binding protein by guanine nucleotides.

Journal of biochemistry, 1985
The rod GTP-binding protein in the bovine disk membrane seems to exist as oligomers in the dark. G alpha and G beta do not interact strongly, and G gamma may be required for G alpha . GDP to dimerize.
H, Shichi, R L, Somers
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Common Properties of Receptors Coupled to GTP Binding Regulator Proteins

1989
A number of membrane receptors coupled to GTP binding regulatory proteins have recently been shown to share structural propertie at the level both of the genes and of the corresponding proteins (Fig. 1 and 2). By comparing results obtained for α2-, β1- and β2-adrenergic catecholamine receptors, M1 to M5 muscarinic acetylcholine receptors as well as ...
L. Emorine, S. Marullo, M.-M. Sutren, C. Delavier, Y. Eshdat, G. Raposo, A. D. Strosberg   +6 more
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Regulation of G protein-coupled receptor endocytosis by ARF6 GTP-binding proteins

Biochemistry and Cell Biology, 2004
The function of G protein-coupled receptors is regulated by a broad variety of membrane-bound and intracellular proteins. These act in concert to activate signaling pathways that will lead to the desensitization of activated receptors and, for most receptor types, their trafficking to intracellular compartments.
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Rab3 Small GTP—Binding Proteins: Regulation by Calcium/Calmodulin

2003
Rab proteins, forming a subfamily of 52 predominantly membrane-bound, low molecular weight GTP-binding proteins (G-proteins) of the Ras superfamily, are involved in vesicle traffic between intracellular organelles, endocytosis and exocytosis, and may be regulated by calcium (Ca2 +) and/or calmodulin (CaM).
Ranjinder S. Sidhu, Richard R. Clough, Rajinder P. Bhullar   +2 more
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Integrin-mediated signalling: regulation by protein tyrosine kinases and small GTP-binding proteins

Current Opinion in Cell Biology, 1996
Integrin signalling requires the activation of protein tyrosine kinases and members of the Rho family of small GTP-binding proteins. Recent evidence shows that coordinated regulation of these signalling molecules is central to the control of cell adhesion, formation of the actin cytoskeleton and activation of intracellular signalling cascades.
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