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GTP-binding proteins in adrenocortical mitochondria

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
We 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 ...
M, Thomson, M, Korn, P F, Hall
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Subunit interactions of GTP‐binding proteins

European Journal of Biochemistry, 1992
Fluorescence 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.
Heithier, H.   +9 more
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The GTP-binding protein Rho

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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GTP-binding proteins in a cyanobacterium Anabaenacylindrica

Biochemical and Biophysical Research Communications, 1988
GTP-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
M, Ohmori, K, Hasunuma, K, Furukawa
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GTP-binding proteins

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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GTP-binding proteins in intracellular transport

Trends in Cell Biology, 1992
One of the most exciting recent discoveries in the area of intracellular protein transport is the finding that many organelles involved in exocytic and endocytic membrane traffic have one or more Ras-like GTP-binding proteins on their cytoplasmic face that are specific for each membranous compartment.
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GTP-binding Proteins and Signal Transduction

2002
Being metabolic regulators, nucleotides play many other roles rather than just providing the alphabets of the genetic code. The pyrimidine bases act as identifiers for metabolites. Purine nucleotides play their main regulatory roles in association with proteins, not metabolites.
Bastien D. Gomperts   +2 more
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The Role of GTP-Binding Proteins in Platelet Activation

Thrombosis and Haemostasis, 1991
SummaryPlatelet activation begins with the binding of an agonist to the cell surface and culminates in the events of platelet aggregation, secretion and clot formation. Recent studies have identified two large families of GTP-binding proteins in platelets that are thought to participate in the events of platelet activation. The first of these are the G
D R, Manning, L F, Brass
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Identification and isoprenylation of plant GTP-binding proteins

Plant Molecular Biology, 1996
To identify isoprenylated plant GTP-binding proteins, Arabidopsis thaliana and Nicotiana tabacum cDNA expression libraries were screened for cDNA-encoded proteins capable of binding [32P]GTP in vitro. ATGB2, an Arabidopsis homologue of the GTP-binding protein Rab2, was found to bind GTP in vitro and to be a substrate for a geranylgeranyl:protein ...
B, Biermann, S K, Randall, D N, Crowell
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GTP Binding Proteins in Platelets

1999
Cells are constantly engulfed in an environment of electrical and chemical stimuli. Specific receptors enable cells to differentiate among the stimuli and relay a specific message that leads to a defined cellular response. The process that translates the stimulus-receptor interaction into an intracellular chemical message is termed signal transduction.
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