Results 301 to 310 of about 246,437 (319)
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Nature Reviews Cancer, 2002
The RAS oncogenes were identified almost 20 years ago. Since then, we have learnt that they are members of a large family of small GTPases that bind GTP and hydrolyse it to GDP. This is then exchanged for GTP and the cycle is repeated. The switching between these two states regulates a wide range of cellular processes.
Christopher J. Marshall, Erik Sahai
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The RAS oncogenes were identified almost 20 years ago. Since then, we have learnt that they are members of a large family of small GTPases that bind GTP and hydrolyse it to GDP. This is then exchanged for GTP and the cycle is repeated. The switching between these two states regulates a wide range of cellular processes.
Christopher J. Marshall, Erik Sahai
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Trends in Cell Biology, 2002
Guidance molecules such as the netrins, the semaphorins or ephrins are key regulators of development of the central nervous system. These signals are thought to modulate neurite extension by providing instructive cues that act as attractants or repellents in different cell types.
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Guidance molecules such as the netrins, the semaphorins or ephrins are key regulators of development of the central nervous system. These signals are thought to modulate neurite extension by providing instructive cues that act as attractants or repellents in different cell types.
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1993
Since Ras proteins negotiate many signalling pathways leading to cell growth or differentiation, the regulation of Ras activity is vital to cellular health. Ras activity, which derives from a collaboration between Ras and GTP, is terminated by the GTPase activating protein (GAP)-catalyzed hydrolysis of the GTP. Hence, a simple regulatory scheme emerges:
G Bollag, F McCormick
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Since Ras proteins negotiate many signalling pathways leading to cell growth or differentiation, the regulation of Ras activity is vital to cellular health. Ras activity, which derives from a collaboration between Ras and GTP, is terminated by the GTPase activating protein (GAP)-catalyzed hydrolysis of the GTP. Hence, a simple regulatory scheme emerges:
G Bollag, F McCormick
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, 2005 Rho-family GTPases (p21s) are molecular switches related to the protooncogene Ras: these function in complementary pathways to orchestrate the actin cytoskeleton, regulate cell polarity, microtubule dynamics, membrane transport pathways and modulate a variety of transcriptional events. Rho GTPases are biochemically and structually simple proteins: they
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Biochemical Society Transactions, 2012
Rho GTPases comprise a family of molecular switches that control signal transduction pathways in eukaryotic cells. A conformational change induced upon binding GTP promotes an interaction with target (effector) proteins to generate a cellular response. A highly conserved function of Rho GTPases from yeast to humans is to control the actin cytoskeleton,
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Rho GTPases comprise a family of molecular switches that control signal transduction pathways in eukaryotic cells. A conformational change induced upon binding GTP promotes an interaction with target (effector) proteins to generate a cellular response. A highly conserved function of Rho GTPases from yeast to humans is to control the actin cytoskeleton,
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Current Opinion in Cell Biology, 1999
The Rho GTPases are simple enzymes with complex roles in regulating cell morphology, gene transcription, cell cycle progression, apoptosis and tumour progression. The picture has been further complicated by the steady rise in the number of known Rho GTPases as well as in the number of known regulators and target proteins of these GTPases.
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The Rho GTPases are simple enzymes with complex roles in regulating cell morphology, gene transcription, cell cycle progression, apoptosis and tumour progression. The picture has been further complicated by the steady rise in the number of known Rho GTPases as well as in the number of known regulators and target proteins of these GTPases.
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Biochemical Society Transactions, 2018
Leucine-rich repeat kinase 2 (LRRK2) is mutated in familial Parkinson's disease, and pathogenic mutations activate the kinase activity. A tour de force screen by Mann and Alessi and co-workers identified a subset of Rab GTPases as bona fide LRRK2 substrates.
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Leucine-rich repeat kinase 2 (LRRK2) is mutated in familial Parkinson's disease, and pathogenic mutations activate the kinase activity. A tour de force screen by Mann and Alessi and co-workers identified a subset of Rab GTPases as bona fide LRRK2 substrates.
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2005
The Rho (Ras-homologous) family of proteins constitutes a major branch of the Ras superfamily of small GTPases, and is evolutionarily conserved across several phyla. Thus far, 25 members have been identified, and these may be divided into 6 subfamilies based on amino acid sequence identity, structural motifs, and biological function.
Pinella Buongiorno, Bharati Bapat
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The Rho (Ras-homologous) family of proteins constitutes a major branch of the Ras superfamily of small GTPases, and is evolutionarily conserved across several phyla. Thus far, 25 members have been identified, and these may be divided into 6 subfamilies based on amino acid sequence identity, structural motifs, and biological function.
Pinella Buongiorno, Bharati Bapat
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Immunological Reviews, 2003
Summary: Guanine nucleotide binding proteins rapidly cycle between a guanosine diphosphate (GDP)‐bound and guanosine triphosphate (GTP)‐bound state, and they operate as binary switches that control cell activation in response to environmental cues. GTPases adopt different conformations when binding GTP vs. GDP.
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Summary: Guanine nucleotide binding proteins rapidly cycle between a guanosine diphosphate (GDP)‐bound and guanosine triphosphate (GTP)‐bound state, and they operate as binary switches that control cell activation in response to environmental cues. GTPases adopt different conformations when binding GTP vs. GDP.
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Biochemical Society Transactions, 2012
LRRK2 (leucine-rich repeat kinase 2) is a large protein encoding multiple functional domains, including two catalytically active domains, a kinase and a GTPase domain. The LRRK2 GTPase belongs to the Ras-GTPase superfamily of GTPases, more specifically to the ROC (Ras of complex proteins) subfamily.
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LRRK2 (leucine-rich repeat kinase 2) is a large protein encoding multiple functional domains, including two catalytically active domains, a kinase and a GTPase domain. The LRRK2 GTPase belongs to the Ras-GTPase superfamily of GTPases, more specifically to the ROC (Ras of complex proteins) subfamily.
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