Results 261 to 270 of about 14,319 (272)
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Changing expression of GTPase activating proteins with differentiation in neuroblastoma

Journal of the Neurological Sciences, 1994
p21ras is a membrane-associated guanine nucleotide-binding protein with intrinsic GTPase activity. Like other guanine nucleotide-binding proteins p21ras is active when GTP bound and inactive when GDP bound. Phosphorylation of p21ras is regulated by the GTPase activity of type I GAP120 and NF1-GRD.
P.A. Berry, S.A. Burchill, I.J. Lewis
openaire   +3 more sources

The GTPase-activating protein Rap1GAP uses a catalytic asparagine

Nature, 2004
Rap1 is a Ras-like guanine-nucleotide-binding protein (GNBP) that is involved in a variety of signal-transduction processes. It regulates integrin-mediated cell adhesion and might activate extracellular signal-regulated kinase. Like other Ras-like GNBPs, Rap1 is regulated by guanine-nucleotide-exchange factors (GEFs) and GTPase-activating proteins ...
Ingrid R. Vetter   +4 more
openaire   +3 more sources

Bacterial mimics of eukaryotic GTPase-activating proteins (GAPs)

Trends in Biochemical Sciences, 2003
Bacterial GTPase-activating proteins (GAPs) subvert their host's eukaryotic Rho GTPases to their own advantage. Studies of bacterial GAPs extend our understanding of the action of eukaryotic GAPs, provide new tools for studies of cytoskeletal dynamics and offer new targets for anti-bacterial drugs.
Zvi Selinger, Yael Litvak
openaire   +3 more sources

p115 Rho GTPase activating protein interacts with MEKK1

Journal of Cellular Physiology, 2002
AbstractMammalian MAP/ERK kinase kinase 1 (MEKK1) was identified as a mammalian homolog of Ste11p of the yeast pheromone‐induced mating pathway. Like Ste11p, MEKK1 is a MAP3 kinase linked to at least two MAP kinase cascades and regulatory events that require cytoskeletal reorganization. MEKK1 is activated by molecules that impact cytoskeletal function.
Ewen D. Gallagher   +7 more
openaire   +3 more sources

Chick kainate binding protein lacks GTPase activity

NeuroReport, 1999
Chick kainate binding protein was solubilized from cerebellar membranes and purified (x19) by use of two chromatographic steps. Measurements of [3H]kainate binding and GTPase activity in the different fractions reveal a consistent decrease of GTPase activity as the purification proceeds so that no GTPase is detectable after the final purification step.
Tasca, C.I.   +4 more
openaire   +4 more sources

Regulation of the GTPase activity of the ras-related rap2 protein

Biochemical and Biophysical Research Communications, 1992
The small GTP-binding protein rap2A exhibits a high level of identity with rap1 and ras proteins (60% and 46%, respectively). Nevertheless, its intrinsic GTPase activity is not stimulated by ras-GAP, and unlike the rap1A protein, it cannot compete with ras proteins for their interaction with ras-GAP.
Isabelle Janoueix-Lerosey   +3 more
openaire   +3 more sources

The Role of ras GTPase Activating Protein in Human Tumorigenesis [PDF]

open access: possiblePathobiology, 1995
Abnormal signal transduction involving activated ras genes plays a major role in the development of a variety of tumors. Ras GTPase-activating protein (rasGAP) is a major contributor to the downregulation of ras by facilitating GTP hydrolysis of activated ras. In addition, GAP participates in the down-stream effector system of the ras signaling pathway.
openaire   +2 more sources

Suppression of c-ras transformation by GTPase-activating protein

Nature, 1990
The ras genes are required for normal cell growth and mediate transformation by oncogenes encoding protein tyrosine kinases. Normal ras can transform cells in vitro and in vivo, but mutationally activated ras does so much more efficiently, and highly transforming mutant versions of ras have been isolated from a variety of human and animal tumours.
Alex G. Papageorge   +5 more
openaire   +3 more sources

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