Results 101 to 110 of about 12,400 (144)
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GTP-binding proteins and early embryogenesis in Xenopus
Cellular Signalling, 1995During early embryogenesis the specification of body axes and the determination of cell subtypes proceeds through cell interactions and movements which involve the decoding of various signals in a spatial and temporal manner. An increasingly abundant literature has revealed the participation of growth factors and their receptors in the induction and ...
Laurent Paquereau, Yves Audigier
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GE: A GTP-Binding Protein Mediating Exocytosis
Annual Review of Physiology, 1990Recent advances in the field of exocytotic secretion have depended almost exclusively on the use of permeabilized cells that allow the composition of the cytosol to be precisely controlled. Many agents and strategies for plasma membrane permeabilization have been utilized (see Table 1), and it is impor tant to appreciate that these generate, in the ...
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Activation of Small GTP-Binding Proteins
1999Guanosine triphosphate- (GTP-) binding proteins act as molecular switches: active in GTP-bound form and inactivated when bound GTP is hydrolyzed. Switching on these proteins initiates a wide range of cellular responses and is controlled by multiple factors.
Anna Koffer, Richard Sullivan
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Dynamin: A microtubule-associated GTP-binding protein
Journal of Cell Science, 1991ABSTRACT We recently identified dynamin as a third nucleotide-sensitive microtubule-associated protein in brain tissue, in addition to kinesin and cytoplasmic dynein. Molecular cloning analysis has revealed that dynamin contains the three consensus elements characteristic of GTP-binding proteins, and biochemical results support a role ...
Robert A. Obar+2 more
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GTP-Binding Proteins: Structures, interactions and relationships
Current Biology, 1994Recently available crystal structures show that some, though not all, GTP-binding proteins have a common 'G-domain' topology, variations on which confer distinct functional properties.
Alfred Wittinghofer, Thomas Schweins
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Signal transducing gtp-binding proteins in olfaction
Comparative Biochemistry and Physiology Part A: Physiology, 19901. Several members of the family of heterotrimeric signal transducing GTP-binding proteins have been identified in the olfactory epithelium of vertebrates by biochemical and molecular cloning techniques. 2. Biochemical and electrophysiological evidence indicates that one or more GTP-binding proteins mediate many olfactory responses by coupling stimulus
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Small GTP-binding protein-coupled receptors
Biochemical Society Transactions, 2004Heterotrimeric GPCRs (G-protein-coupled receptors) form the largest group of integral membrane receptor proteins and mediate diverse physiological processes. In addition to signalling via heterotrimeric G-proteins, GPCRs can also signal by interacting with various small G-proteins to regulate downstream effector pathways.
Andy V. Babwah+5 more
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Partial characterization of GTP-binding proteins in Neurospora
Biochemical and Biophysical Research Communications, 1987Six fractions of GTP-binding proteins separated by gel filtration of a mycelial extract containing membrane components of Neurospora crassa were partially characterized. [35S]GTP gamma S bound to GTP-binding protein was assayed by repeated treatments with a Norit solution and centrifugation.
Yukie Miyamoto-Shinohara+2 more
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Regulatory Role for GTP-Binding Proteins in Endocytosis
Science, 1989Guanosine 5′-triphosphate (GTP)-binding proteins have been implicated in the transport of newly synthesized proteins along the secretory pathway of yeast and mammalian cells. Early vesicle fusion events that follow receptor-mediated endocytosis as measured by three in vitro assays were blocked by guanosine 5′- O -(3-
Philip D. Stahl, R Diaz, Luis S. Mayorga
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The Cellular Functions of Small GTP-Binding Proteins
Science, 1990A substantial number of novel guanine nucleotide binding regulatory proteins have been identified over the last few years but the function of many of them is largely unknown. This article will discuss a particular family of these proteins, structurally related to the Ras oncoprotein.
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