Results 11 to 20 of about 80,664 (305)
Oncogene ect2 is related to regulators of small GTP-binding proteins [PDF]
Nature, 1993 We have developed an efficient expression cloning system that allows rapid isolation of complementary DNAs able to induce the transformed phenotype. We searched for molecules expressed in epithelial cells and possessing transforming potential to fibroblasts, and cloned a cDNA for the normal receptor of a growth factor secreted by NIH/3T3 cells. Here we
Toru Miki +4 more
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Abr and Bcr are multifunctional regulators of the Rho GTP-binding protein family. [PDF]
Proceedings of the National Academy of Sciences, 1995 Philadelphia chromosome-positive leukemias result from the fusion of the BCR and ABL genes, which generates a functional chimeric molecule. The Abr protein is very similar to Bcr but lacks a structural domain which may influence its biological regulatory capabilities. Both Abr and Bcr have a GTPase-activating protein (GAP) domain similar to those found
Tsung‐Hsien Chuang +5 more
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The small GTP-binding protein Rac is a regulator of cell death in plants [PDF]
Proceedings of the National Academy of Sciences, 1999 Cell death plays important roles in the development and defense of plants as in other multicellular organisms. Rapid production of reactive oxygen species often is associated with plant defense against pathogens, but their molecular mechanisms are not known.
Tsutomu Kawasaki +6 more
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An essential GTP‐binding protein functions as a regulator for differentiation in Streptomyces coelicolor [PDF]
Molecular Microbiology, 1998 The Streptomyces coelicolor obg gene, which encodes a putative GTP‐binding protein of the Obg/Gtp1 family, was characterized. The obg gene was essential for viability. Introduction of multiple copies of obg into wild‐type S. coelicolor suppressed aerial mycelium formation. A single amino acid substitution at any of six positions was introduced into the
Susumu Okamoto, Kozo Ochi
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Correction: Oncogene ect2 is related to regulators of small GTP-binding proteins [PDF]
Nature, 1993 Nature 362, 462-465 (1993) THE amino-acid numbering of Ect2 and CDC24 in Fig. 2b of this letter is incorrect. The numbers for Ect2 should be 279, 330, 382, 429 and 482 (from top to bottom). Amino acids of CDC24 are numbered according to the initial publication18 and not according to the revised sequence as indicated in the figure legend.
Toru Miki +4 more
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Regulation of lymphocyte-mediated killing by GTP-binding proteins [PDF]
Journal of Leukocyte Biology, 2003 Abstract Exocytosis of granules containing apoptosis-inducing proteins is one mechanism of target cell killing by cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells. Granules containing perforin and granzymes are redistributed to the area of cell contact initiated by specific interactions between surface ligands on a target ...
Dianne Khurana, Paul J. Leibson
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GTP-Binding Proteins and Regulated Exocytosis [PDF]
Critical Reviews in Oral Biology & Medicine, 1999 Regulated exocytosis, which occurs in response to stimuli, is a two-step process involving the docking of secretory granules (SGs) at specific sites on the plasma membrane (PM), with subsequent fusion and release of granule contents. This process plays a crucial role in a number of tissues, including exocrine glands, chromaffin cells, platelets, and ...
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Dual positive and negative regulation of GPCR signaling by GTP hydrolysis [PDF]
, 2009 G protein-coupled receptors (GPCRs) regulate a variety of intracellular pathways through their ability to promote the binding of GTP to heterotrimeric G proteins. Regulator of G protein signaling (RGS) proteins increase the intrinsic GTPase activity of G-
Berg, Hugo van den +8 more
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Molecular architecture of Gαo and the structural basis for RGS16-mediated deactivation [PDF]
, 2008 Heterotrimeric G proteins relay extracellular cues from heptahelical transmembrane receptors to downstream effector molecules. Composed of an α subunit with intrinsic GTPase activity and a βγ heterodimer, the trimeric complex dissociates upon receptor ...
Berman +34 more
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The non-catalytic carboxyl-terminal domain of ARFGAP1 regulates actin cytoskeleton reorganization by antagonizing the activation of Rac1. [PDF]
PLoS ONE, 2011 The regulation of the actin cytoskeleton and membrane trafficking is coordinated in mammalian cells. One of the regulators of membrane traffic, the small GTP-binding protein ARF1, also activates phosphatidylinositol kinases that in turn affect actin ...
Ka Yu Siu +6 more
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