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The Rheb family of GTP-binding proteins [PDF]
Cellular Signalling, 2004 Rheb proteins represent a novel and unique family of the Ras superfamily GTP-binding proteins that is conserved from yeast to human. Biochemical studies establish that they bind and hydrolyze GTP. Molecular modeling studies reveal a few structural differences between Rheb and Ras, which may suggest that residues involved in biochemical activities ...
Fuyuhiko Tamanoi, Paul-Joseph Aspuria
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GTP-binding proteins in plants
Plant Molecular Biology, 1993Abstract Full length cDNAs of small GTP-binding proteins were inserted into PGEM1 under the control of the T7 promotor as described previously (Chavrier et al. 1990; Huber et al. 1993). GTP-binding proteins were then transiently expressed in BHK 21 cells with the T7 RNA polymeraserecombinant vaccinia virus system (Fuerst et al.
Terryn, N. +2 more
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GTP-binding proteins in plants
Cellular and Molecular Life Sciences CMLS, 1999GTP-binding proteins are found in all organisms. They are important switches that cycle between an active and an inactive state, ensuring vectorial flow of information on the expense of guanosine triphosphate (GTP). In this review, we discuss current progress in the molecular characterization and functional analysis of plant genes encoding ...
K. Palme +3 more
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Physiological Reviews, 2001
Small GTP-binding proteins (G proteins) exist in eukaryotes from yeast to human and constitute a superfamily consisting of more than 100 members. This superfamily is structurally classified into at least five families: the Ras, Rho, Rab, Sar1/Arf, and Ran families.
Takashi Matozaki +2 more
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Small GTP-binding proteins (G proteins) exist in eukaryotes from yeast to human and constitute a superfamily consisting of more than 100 members. This superfamily is structurally classified into at least five families: the Ras, Rho, Rab, Sar1/Arf, and Ran families.
Takashi Matozaki +2 more
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Regulation of small GTP-binding proteins by insulin [PDF]
Biochemical Society Transactions, 2006 Several members of the extensive family of small GTP-binding proteins are regulated by insulin, and have been implicated in insulin action on glucose uptake. These proteins are themselves negatively regulated by a series of specific GAPs (GTPase-activating proteins).
Ingeborg Hers +3 more
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GTP-binding proteins in adrenocortical mitochondria
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995We have identified two GTP-binding proteins in mitochondria from bovine adrenal cortex (fasciculata). Sub-mitochondrial particles were fractionated into inner membrane, contact point and outer membrane vesicles on sucrose density gradients. These sub-mitochondrial fractions were identified by the presence of enzyme markers and electron microscopy ...
Murray Thomson +2 more
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Current Opinion in Structural Biology, 1991
Abstract There has been much progress this year in characterizing the complex series of post-translational modifications important for GTP-binding protein function. In addition, the long-awaited molecular characterization of a G protein that regulates phospholipase C activity has been reported.
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Abstract There has been much progress this year in characterizing the complex series of post-translational modifications important for GTP-binding protein function. In addition, the long-awaited molecular characterization of a G protein that regulates phospholipase C activity has been reported.
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Subunit interactions of GTP‐binding proteins
European Journal of Biochemistry, 1992Fluorescence energy transfer [cf. Förster, T. (1948) Ann. Phys. 6, 55–75] was tested for its suitability to study quantitative interactions of subunits of Go with each other and these subunits or trimeric Go with the β1‐adrenoceptor in detergent micelles or after reconstitution into lipid vesicles [according to Feder, D., Im, M.‐J., Klein, H.
Winchil L.C. Vaz +9 more
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GTP-binding proteins in a cyanobacterium Anabaenacylindrica
Biochemical and Biophysical Research Communications, 1988GTP-binding proteins were detected in a crude extract containing membrane components of Anabaena cylindrica. The crude extract was treated with 1% Lubrol PX and was fractionated by gel filtration. The binding of [35S]GTP gamma S to GTP-binding proteins was prevented in the presence of 0.1 mM GTP and in the presence of 0.1 mM ATP. Six fractions of these
Kazuhiko Furukawa +2 more
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The International Journal of Biochemistry & Cell Biology, 1997
RhoA, RhoB and RhoC are three closely related proteins, and are members of the Ras super-family of small GTP-binding proteins. They bind and hydrolyse GTP, and are active in the GTP-bound form. Their activity in cells is regulated by exchange factors, GTPase activating proteins and guanine nucleotide dissociation inhibitors.
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RhoA, RhoB and RhoC are three closely related proteins, and are members of the Ras super-family of small GTP-binding proteins. They bind and hydrolyse GTP, and are active in the GTP-bound form. Their activity in cells is regulated by exchange factors, GTPase activating proteins and guanine nucleotide dissociation inhibitors.
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