Results 201 to 210 of about 153,070 (268)

The regulation of mitochondrial physiology by organelle‐associated GTP‐binding proteins

Cell Biochemistry and Function, 2002
AbstractRecent 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 the phagocyte respiratory burst by small GTP-binding proteins

Trends in Cell Biology, 1995
Bacteria 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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Cellular responses regulated by rho-related small GTP-binding proteins

Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 1993
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, H F, Paterson, P, Adamson, A J, Ridley   +3 more
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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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Arf Proteins and Their Regulators: At the Interface Between Membrane Lipids and the Protein Trafficking Machinery

Ras Superfamily Small G Proteins: Biology and Mechanisms 2, 2014
The Arf small GTP-binding (G) proteins regulate membrane traffic and organelle structure in eukaryotic cells through a regulated cycle of GTP binding and hydrolysis.
C. L. Jackson
semanticscholar   +1 more source

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 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 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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