Results 171 to 180 of about 221,192 (198)

Hydrolysis of GTP by the α‐chain of G_s and other GTP binding proteins

Proteins: Structure, Function, and Bioinformatics, 1989
AbstractThe functions of G proteins—like those of bacterial elongation factor (EF) Tu and the 21 kDa ras proteins (p21ras)—depend upon their abilities to bind and hydrolyze GTP and to assume different conformations in GTP‐ and GDP‐bound states. Similarities in function and amino acid sequence indicate that EF‐Tu, p21ras, and G protein α‐chains evolved ...
Henry R. Bourne, Susan B. Masters, Claudia A. Landis   +2 more
openaire   +3 more sources

Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis.

Science, 1994
Mechanisms of guanosine triphosphate (GTP) hydrolysis by members of the G protein alpha subunit-p21ras superfamily of guanosine triphosphatases have been studied extensively but have not been well understood.
D. Coleman, A. Berghuis, Ethan Lee, M. Linder, A. Gilman, S. Sprang   +5 more
semanticscholar   +1 more source

GTP binding and growth control

Current Opinion in Cell Biology, 1990
Guanosine triphosphate (GTP)-binding proteins are involved, directly or indirectly, in virtually every aspect of cellular growth control and metabolism. At least three major classes of GTP-binding protein have been identified. The first includes elongation factors and initiation factors that are part of the machinery of protein synthesis, and also part
openaire   +3 more sources

An Expression Cloning Method to Identify Monomeric GTP-Binding Proteins by GTP Overlay

Analytical Biochemistry, 1997
We have developed a method for identifying monomeric GTP-binding proteins that is based on probing plasmid expression libraries with [alpha-32P]GTP. The method involves the production of nitrocellulose replica filter lifts from a plasmid cDNA expression library and treatment of the filters with chloroform vapor to lyse the Escherichia coli and to ...
Keiko Kadono-Okuda, Douglas A. Andres
openaire   +3 more sources

Regulation of phosphoenolpyruvate carboxykinase (GTP) gene expression.

Annual Review of Biochemistry, 1997
Phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) (PEPCK) is a key enzyme in the synthesis of glucose in the liver and kidney and of glyceride-glycerol in white adipose tissue and the small intestine. The gene for the cytosolic form of PEPCK (PEPCK-C)
R. Hanson, L. Reshef
semanticscholar   +1 more source

Control of Differentiation by GTP

Nucleosides, Nucleotides and Nucleic Acids, 1989
Abstract A partial deficienc of GTP or GDP induces the differentiation of microorganisms and certain cells of higher organisms. The mechanism of this control may be retained during evolution.
openaire   +2 more sources

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.
openaire   +3 more sources

The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors

Cell, 1992
A. Ridley, A. Hall
semanticscholar   +1 more source

The P-loop--a common motif in ATP- and GTP-binding proteins.

TIBS -Trends in Biochemical Sciences. Regular ed, 1990
M. Saraste, P. R. Sibbald, A. Wittinghofer   +2 more
semanticscholar   +1 more source

The role of hormone receptors and GTP-regulatory proteins in membrane transduction

Nature, 1980
M. Rodbell
semanticscholar   +1 more source