Results 241 to 250 of about 82,021 (288)
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Distribution and Regulation of RAB3C, a Small Molecular Weight GTP-Binding Protein
Biochemical and Biophysical Research Communications, 1994We have investigated the expression and regulation of rab3C in rat tissues and rat pheochromocytoma PC12 cells by using a polyclonal antibody that specifically recognizes this protein. Rab3C was expressed in the neuroendocrine systems, as is its highly homologous family member, rab3A.
Y C, Su +5 more
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Cellular responses regulated by rho-related small GTP-binding proteins
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 1993Abstract Rho-related proteins are members of the ras superfamily of small GTP-binding proteins. Their function in fibroblasts has been analysed using microinjection of living cells. Rho appears to link plasma membrane receptors to the assembly of focal adhesions and actin stress fibres.
A, Hall +3 more
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Regulation of the phagocyte respiratory burst by small GTP-binding proteins
Trends in Cell Biology, 1995Bacteria phagocytosed by leukocytes are killed and degraded by toxic oxygen metabolites produced in the phagosome via an NADPH oxidase. NADPH oxidase activity is regulated by small GTP-binding proteins in response to phagocytic stimuli. In this review, Gary Bokoch focuses on the role of Rac in regulating this important phagocytic process.
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The Role of Prenylated Small GTP-Binding Proteins in the Regulation of Osteoclast Function
Calcified Tissue International, 2003The 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 macrophage adhesion and migration by Rho GTP‐binding proteins
Journal of Microscopy, 2008SummaryThe 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 regulation of mitochondrial physiology by organelle‐associated GTP‐binding proteins
Cell Biochemistry and Function, 2002AbstractRecent studies have shown that GTP‐binding proteins can modulate mitochondrial membrane fusion and fission. Furthermore, GTP‐binding proteins can regulate the binding of ribosomes to the mitochondrial membrane and may facilitate the import of proteins through contact points between inner and outer mitochondrial membranes.
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Regulation of phospholipase D by low molecular weight GTP-binding proteins
Journal of Lipid Mediators and Cell Signalling, 1996Phospholipase 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 rod GTP binding protein by guanine nucleotides.
Journal of biochemistry, 1985The 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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Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins
Current Opinion in Cell Biology, 1994Recent 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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Characterization of DRGs, developmentally regulated GTP-binding proteins, from pea and Arabidopsis
Plant Molecular Biology, 1999Developmentally regulated GTP-binding proteins (DRGs) from animals and fungi are highly conserved but have no known function. Here we characterize DRGs from pea (PsDRG) and Arabidopsis (AtDRG). Amino acid sequences of AtDRG and PsDRG were 90% identical to each other and about 65% identical to human DRG.
M L, Devitt, K J, Maas, J P, Stafstrom
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