Results 141 to 150 of about 11,723 (175)

Evidence of a role for heterotrimeric GTP-binding proteins in endosome fusion

Science, 1992
Guanosine triphosphate (GTP)-binding proteins are required for intracellular vesicular transport. Mastoparan is a peptide component of wasp venom that increases nucleotide exchange in some classes of Gα subunits of regulatory heterotrimeric GTP-binding proteins (G proteins).
Maria I Colombo   +2 more
exaly   +4 more sources

Activation of Heterotrimeric GTP-Binding Proteins

open access: yes, 1999
Guanosine triphosphate- (GTP-) binding proteins constitute a supergene family of proteins that utilize GTP binding and hydrolysis as a chemical switch. These proteins are activated by exchanging bound guanosine diphosphate (GDP) with GTP and are subsequently inactivated by hydrolyzing bound GTP to GDP.1–3 Hence, by shuttling between an inactive, GDP ...
Ronit Sagi-Eisenberg
openaire   +2 more sources

Immunological Probes of the Structure, Function, and Expression of Heterotrimeric GTP-Binding Proteins

open access: yes, 1992
G-proteins convey extracellular signals from cell surface receptors to diverse effectors such as enzymes of second messenger metabolism and ion channels. Receptor-effector coupling G-proteins are composed of three subunits, α, β, and γ, each separate gene products. Multiple forms of each type of subunit have been identified at the DNA and protein level
Allen M. Spiegel   +5 more
openaire   +2 more sources

Purification of heterotrimeric GTP-binding proteins from brain: identification of a novel form of Go

Biochemistry, 1988
Using high-resolution Mono-Q anion-exchange chromatography, we purified four distinct GTP-binding proteins from bovine brain. Each consists of alpha and associated beta/gamma subunits, and each is a substrate for pertussis toxin catalyzed ADP-ribosylation.
Paul Goldsmith   +2 more
exaly   +3 more sources

Volatile anesthetics modulate the binding of guanine nucleotides to the α subunits of heterotrimeric GTP binding proteins

European Journal of Pharmacology, 1999
The effects of volatile anesthetics on guanine nucleotide binding to the purified alpha subunits of heterotrimeric GTP binding (G) proteins were studied. At sub-anesthetic doses, halothane, isoflurane, enflurane and sevoflurane inhibit exchange of GTPgammaS for GDP bound to Galpha subunits and markedly enhance the dissociation of GTPgammaS, but fail to
Mario J Rebecchi
exaly   +3 more sources

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