2 edition of Regulation of the Ras exchange factor Ras-GRF2. found in the catalog.
Regulation of the Ras exchange factor Ras-GRF2.
Carmen Lenore De Hoog
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|Number of Pages||161|
Differential involvement of Ras-GRF1 and Ras-GRF2 in L-DOPA-induced dyskinesia. Annals of Clinical and Translational Neurology 2(6), pp. (/acn). Advances in Neuropharmacology Book Series: International Review of Neurobiology, +. Colotta V, Lenzi O, Catarzi D, Varano F, Filacchioni G, Martini C, Trincavelli L, Ciampi O, Pugliese AM, Traini C, Pedata F, Morizzo E and Moro S () Pyrido[2,3- e ]-1,2,4-triazolo[4,3- a ]pyrazinone as a New Scaffold To Develop Potent and.
Comments. Transcription. Descargar versión en castellano. Signal Transduction, Second Edition; Library of Congress Cataloging-in-Publication Data A catalog record for this book is available from the Library of Congress British Library Cataloging in Publication Data A catalogue record for this book is available from the British Library ISBN: For information on all Academic Press.
Lee SY, Wenk MR, Kim Y, Nairn AC, De Camilli P () Regulation of synaptojanin 1 by cyclin-dependent kinase 5 at synapses. Proc Natl Acad Sci U S A – Lee SY, Voronov S, Letinic K, Nairn AC, Di Paolo G, De Camilli P () Regulation of the interaction between PIPKI gamma and talin by proline-directed protein kinases. Buday L. and Downward J. () Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor. Cell, 73, Buday L., Warne P.H. and Downward J. () Down-regulation of the Ras activation pathway by MAP kinase phosphorylation of Sos.
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Regulation of the Ras Exchange Factor Ras-GRF2 Carmen Lenore de Hoog Doctor of Philosophy, 1 Department of Molecular and Medical Genetics University of Toronto ABSTRACT The Ras GTPases play a pivotal role in cellular proliferation and differentiation and become activated in response to a variety of extracellular sipals, including gowth andAuthor: de Hoog, Carmen Lenore.
Ensembl ENSG n/a UniProt O P RefSeq (mRNA) NM_ NM_ RefSeq (protein) NP_ NP_ Location (UCSC) Chr 5: – Mb n/a PubMed search Wikidata View/Edit Human View/Edit Mouse Ras-specific guanine nucleotide-releasing factor 2 is a protein that in humans is encoded by the RASGRF2 gene.
RAS (MIM ) GTPases Aliases: RASGRF2, GRF2, RAS-GRF2, Ras. Ras-GRF2, and its close relative Ras-GRF1 (also known as Cdc25Mm), which is expressed primarily in neurons, binds calmodulin (CaM) and activates Ras in response to an elevation in intracellular calcium.Analysis of activated GTP-bound Ras in cell lysates expressing Ras-GRF2 indicated that activation of Ras by Ras-GRF2 requires the Cdc25 domain, but can occur in the absence of the DH domain ().Cited by: Ras-GRF2 (GRF2) is a widely expressed guanine nucleotide exchange factor (GEF) that stimulates the release of bound guanine nucleotide by the low-molecular-weight G protein Ras (6, 10).GRF2 stimulates the conversion of Ras from its GDP-bound state into a GTP-bound activated by: Ras-GRF2 (GRF2) is a widely expressed GEF which catalyzes nucleotide exchange on Ras through its Cdc25 domain (7, 14).
GRF2 is a bifunctional GEF; in addition to having activity on Ras, GRF2 is capable of binding to another small G protein, Rac1, through its Dbl homology (DH) by: Regulation of Ras Exchange Factors and Cellular Localization of Ras Activation by Lipid Messengers in T Available via license: CC BY Content may be subject to copyright.
The Ras guanine-nucleotide exchange factor Ras-GRF/Cdc25(Mn) harbors a complex array of structural motifs that include a Dbl-homology (DH) domain, usually found in proteins that interact.
specificity exchange factor for the Ras and Rac GTPases. A recombinant giutathione S-transferase hision protein containing the Cdc25 domain of Ras-GRF2 stimulated net nucleotide exchange on Ras, in vitro. Consistent with this result, Ras-GRF2 was dso able to activate.
RasGRP represents the prototype of a new class of guanine nucleotide exchange factors that activate small GTPases. The guanyl nucleotide-releasing protein (GRP) family members contain catalytic domains related to CDC25, the Ras exchange factor of Saccharomyces cerevisiae.
They also contain a motif resembling a pair of calcium-binding EF-hands and a C1 domain similar to the Cited by: R-Ras proteins share 46–67 percent amino acid identity with each other, and 52–55 percent amino acid identity with H-Ras (Figure b), primarily in the consensus guanine nucleotide binding motifs and the switch I and II regions of Ras that alter conformation based on the bound guanine nucleotide (GTP or GDP), permitting function as GDP/GTP-regulated molecular switches (Figure a).Author: Gretchen A.
Repasky, Adrienne D. Cox, Ariella B. Hanker, Natalia Mitin, Channing J. Der. Carmen Lenore De Hoog has written: 'Regulation of the Ras exchange factor Ras-GRF2' Asked in Authors, Poets, and Playwrights What has the author Lenore Kletter written.
RasGrf1 and RasGrf2 are large proteins composed by multiple modular domains accounting for protein-protein or protein-lipid interactions which are responsible for functional coupling to upstream and downstream signaling and for fine regulation of their intrinsic exchange activity.
GTP-bound R-Ras and H-Ras can also bind to the p catalytic subunit of PI 3-kinase and Rlf, a guanine nucleotide exchange factor for the Ral family of small GTP-binding proteins. Consequently, we examined the role of these effectors in integrin affinity modulation. Wang, Z. and Moran, M. () Phospholipase C a Phospholipase and Guanine Nucleotide Exchange Factor.
Molecular Intervention 2: Chen, X. and Wang, Z. () Regulation of epidermal growth factor receptor endocytosis by wortmannin through activation of Rab5 rather than inhibition of phosphatidylinositol 3-kinase. phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 2 N16Rik, DEP.2, DEPDC2, P-REX2, PPP1R PRKAA1 Ras protein-specific guanine nucleotide-releasing factor 2 GRF2, RAS-GRF2 RASGRP1 RAS guanyl-releasing protein 1 CALDAG-GEFI, CALDAG-GEFII, RASGRP, V, hRasGRP1 RASGRP2.
Membrane association of the tumor suppressor, annexin A6 (AnxA6), has been shown to regulate plasma membrane permeability to extracellular Ca2+, inhibit anchorage-independent tumor cell growth and paradoxically, promote tumor cell motility by mechanisms that remains poorly understood.
Here, we identified RasGRF2, a Ca2+-activated Ras-specific guanine nucleotide exchange factor, as a major. However, under calcium treatment, RAS is activated by other factors, the RAS-guanine-nucleotide-releasing factor 1 (RAS-GRF1) and 2 (RAS-GRF2) (Cullen and Lockyer, ).
Because RAS-GRF1 is mainly expressed in the nerve system and RAS-GRF2 is widely expressed in many tissues (Farnsworth et al., ; Fam et al., ), we therefore. "Dematin interacts with the Ras-guanine nucleotide exchange factor Ras-GRF2 and modulates mitogen-activated protein kinase pathways".
European journal of biochemistry / FEBS. (2): – The exchange factor Ras-GRF2 activates Ras-dependent and Rac-dependent mitogen-activated protein kinase pathways. Regulation of the Rac1-specific exchange factor Tiam1 involves both phosphoinositide 3-kinase-dependent and -independent components.
Ras-dependent growth factor regulation of MEK kinase in PC12 cells. Science– Ras-specific guanine nucleotide-releasing factor 2 Eukaryotic translation initiation factor 4E-binding protein 1 GRF2, RAS-GRF2 CALDAG-GEFI, CALDAG-GEFII, RASGRP, V, hRasGRP1 RASGRP2 CALDAG-GEFI, CDC25L hSPRY1 hSPRY2 HSPRY3, spry-3 HH.
The effect of amphetamine and cocaine on Ras-guanine nucleotide releasing factor 1 (Ras-GRF1) and Ras-GRF2 protein expression in the rat striatum in vivo. Annual Midwest Anesthesiology Residents Conference, St. Louis, MO, AprilRas-guanine nucleotide-releasing factor 2 (Ras-GRF2) is a Ca 2+ /Calmodulin (CaM) sensor mediating GluN2A-containing NMDAR signaling in mature neurons, Author: Luca Franchini, Nicolò Carrano, Monica Di Luca, Fabrizio Gardoni.Inhibition of Ras-guanine nucleotide-releasing factor 1 (Ras-GRF1) signaling in the striatum reverts motor symptoms associated with L-dopa-induced dyskinesia.
Proceedings of the National Academy of Sciences (50), pp. (/pnas) Visigalli, al.