Results 211 to 220 of about 258,313 (263)
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The Interferon-Inducible GTPases
Annual Review of Cell and Developmental Biology, 2006Mammalian cells respond to interferons (IFNs) secreted during infection by the transcriptional upregulation of as many as a thousand genes. This remarkable transition prepares cells and organisms for resistance to infection, and many IFN-regulated gene products are players in well-understood resistance programs.
Martens, Sascha, Howard, Jonathan
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Current Opinion in Structural Biology, 1995
The past year has witnessed a tremendous increase in our understanding of the structures and interactions of the GTPases. The highlights include crystal structures of G alpha subunits, as well as the first complex between a GTPase (Rap1A) and an effector molecule (c-Raf1 Ras-binding domain).
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The past year has witnessed a tremendous increase in our understanding of the structures and interactions of the GTPases. The highlights include crystal structures of G alpha subunits, as well as the first complex between a GTPase (Rap1A) and an effector molecule (c-Raf1 Ras-binding domain).
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2017
GTPases (GTP hydrolases, GTP binding proteins) are a large family of enzymes that direct various cellular functions, including signal transduction, protein biosynthesis, cell division and transport of vesicles. They are molecular switches that cycle between two conformational states (Figure 1): the inactive guanosine-5'-diphosphate (GDP)-bound state ...
Stefanini, Lucia +2 more
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GTPases (GTP hydrolases, GTP binding proteins) are a large family of enzymes that direct various cellular functions, including signal transduction, protein biosynthesis, cell division and transport of vesicles. They are molecular switches that cycle between two conformational states (Figure 1): the inactive guanosine-5'-diphosphate (GDP)-bound state ...
Stefanini, Lucia +2 more
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The International Journal of Biochemistry & Cell Biology, 2002
Eps8, originally identified as a substrate for the kinase activity of the epidermal growth factor receptor (EGFR), displays a domain organization typical of a signaling molecule that includes a putative N-terminal PTB domain, a central SH3 domain, and a C-terminal "effector region".
P.P. Di Fiore, G. Scita
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Eps8, originally identified as a substrate for the kinase activity of the epidermal growth factor receptor (EGFR), displays a domain organization typical of a signaling molecule that includes a putative N-terminal PTB domain, a central SH3 domain, and a C-terminal "effector region".
P.P. Di Fiore, G. Scita
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The Journal of the Florida Medical Association, 1993
GTPases represent a large family of proteins involved in a wide variety of cellular processes. They function as switches in which they are "on" in the GTP bound state and "off" in the GDP bound state. The "on" and "off" states are regulated by proteins which interact with the GTPases and enhance their rate of either GTP hydrolysis or GDP-GTP exchange ...
R K, Keller, M, Standert
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GTPases represent a large family of proteins involved in a wide variety of cellular processes. They function as switches in which they are "on" in the GTP bound state and "off" in the GDP bound state. The "on" and "off" states are regulated by proteins which interact with the GTPases and enhance their rate of either GTP hydrolysis or GDP-GTP exchange ...
R K, Keller, M, Standert
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Experimental Cell Research, 1999
Rho GTPases regulate many important processes in all eukaryotic cells, including the organization of the actin cytoskeleton, gene transcription, cell cycle progression, and membrane trafficking. Their activity is regulated by signals originating from different classes of surface receptors including G-protein-coupled receptors, tyrosine kinase receptors,
L, Kjoller, A, Hall
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Rho GTPases regulate many important processes in all eukaryotic cells, including the organization of the actin cytoskeleton, gene transcription, cell cycle progression, and membrane trafficking. Their activity is regulated by signals originating from different classes of surface receptors including G-protein-coupled receptors, tyrosine kinase receptors,
L, Kjoller, A, Hall
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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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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.
Erik, Sahai, Christopher J, Marshall
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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.
Erik, Sahai, Christopher J, Marshall
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