PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33145412-0 2020 GTP-State-Selective Cyclic Peptide Ligands of K-Ras(G12D) Block Its Interaction with Raf. Guanosine Triphosphate 0-3 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 85-88 28855513-4 2017 In this biosensor, two inactive luciferase fragments are sandwiched by Raf-1, whose conformation changes upon GTP-Ras binding. Guanosine Triphosphate 110-113 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 71-76 32649863-1 2020 CRAF activation requires binding to membrane-anchored and active GTP-bound RAS. Guanosine Triphosphate 65-68 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 0-4 32673148-5 2021 Here, we investigated the structural dynamics of ZIKV NS5 MTase domain free and bound to Guanosine-5"-triphosphate (GTP) and S-Adenosyl-Lmethionine (SAM), to identify the molecular dynamics changes related to ligand binding and methyl transfer reaction. Guanosine Triphosphate 116-119 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 54-57 30951555-6 2019 The basic residue K28 also participates in GTP binding and competition experiments indicate that NS5 dimerization is disrupted at high GTP concentrations. Guanosine Triphosphate 43-46 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 97-100 30951555-6 2019 The basic residue K28 also participates in GTP binding and competition experiments indicate that NS5 dimerization is disrupted at high GTP concentrations. Guanosine Triphosphate 135-138 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 97-100 28783719-5 2017 The mutants bind more tightly than wild-type BRAF to RAS-GTP, and their binding to and activation of wild-type CRAF is enhanced, leading to increased ERK signalling. Guanosine Triphosphate 57-60 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 111-115 28630043-5 2017 Using enzyme kinetic assays under identical conditions, we observed clear differences between the three isoforms in intrinsic catalysis of GTP by Ras in the absence and presence of the Ras-binding domain (RBD) of the c-Raf kinase protein (Raf-RBD). Guanosine Triphosphate 139-142 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 217-222 24696348-6 2014 The N-terminal domain of NS5 has distinct GTP and S-adenosylmethionine (SAM) binding sites. Guanosine Triphosphate 42-45 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 25-28 25775415-3 2015 We determined a crystal structure of the full-length NS5 protein from Dengue virus serotype 3 (DENV3) at a resolution of 2.3 A in the presence of bound SAH and GTP. Guanosine Triphosphate 160-163 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 53-56 24696348-7 2014 The role of GTP binding site is implicated in guanylyltransferase (GTase) activity of NS5. Guanosine Triphosphate 12-15 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 86-89 20230813-7 2010 Biochemical analyses indicated that TAP-1 operates at the level of Raf, since TAP-1 function negatively regulated the amount of Raf-1 recruited to GTP-bound Ras at the cell membrane. Guanosine Triphosphate 147-150 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 128-133 21862573-0 2011 Activation kinetics of RAF protein in the ternary complex of RAF, RAS-GTP, and kinase on the plasma membrane of living cells: single-molecule imaging analysis. Guanosine Triphosphate 70-73 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 23-26 16569214-8 2006 Assays for GTP loading and H-Ras interactions with the Ras-binding domain on Raf-1 demonstrated a decrease in H-Ras activity in the presence of NO*. Guanosine Triphosphate 11-14 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 77-82 18458061-2 2008 We show using high-resolution spatial mapping that Raf-1 is recruited to and retained in K-Ras-GTP nanoclusters. Guanosine Triphosphate 95-98 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 51-56 18458061-4 2008 Similarly, upon epidermal growth factor receptor activation, Raf-1 is preferentially recruited to K-Ras-GTP and not H-Ras-GTP nanoclusters. Guanosine Triphosphate 104-107 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 61-66 15067337-3 2004 Activated GTP bound Ras binds the upstream protein kinases Raf-1 and B-Raf. Guanosine Triphosphate 10-13 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 59-64 16475808-7 2006 We further demonstrate that NO/O(2) and O(2)(*)(-) promote Ras GDP exchange with GTP in the presence of a radical-quenching agent, ascorbate, or NO, and generation of Ras-GTP promotes high-affinity binding of the Ras-binding domain of Raf-1, a downstream effector of Ras. Guanosine Triphosphate 81-84 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 235-240 16475808-7 2006 We further demonstrate that NO/O(2) and O(2)(*)(-) promote Ras GDP exchange with GTP in the presence of a radical-quenching agent, ascorbate, or NO, and generation of Ras-GTP promotes high-affinity binding of the Ras-binding domain of Raf-1, a downstream effector of Ras. Guanosine Triphosphate 171-174 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 235-240 11971897-8 2002 Thus, retinoids bound c-Raf with high affinity, priming the molecule for UV/reactive oxygen species-mediated changes of the CRD that set off GTP-Ras interaction and, in context with an appropriate phosphorylation pattern, lead to full phosphotransferase capacity. Guanosine Triphosphate 141-144 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 22-27 12748287-6 2003 TPR1 was found to compete with the Ras-binding domain (RBD) of Raf-1 for binding to the active Ras, suggesting that it may also compete with Ras GTPase-activating protein, thus contributing to the accumulation of GTP-bound Ras. Guanosine Triphosphate 145-148 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 63-68 12894505-6 2003 MATERIALS AND METHODS: The interaction of Raf-1 with Ras was examined by investigating the association of cytosolic Raf-1, from ET-18-OCH3-treated and untreated cells with purified GST-Ras-GTP-gamma-S bound to agarose beads. Guanosine Triphosphate 189-192 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 42-47 11953426-12 2002 Ras association with Raf was GTP dependent as previously demonstrated for C-Raf-RBD fragments. Guanosine Triphosphate 29-32 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 74-79 12801936-2 2003 We show here that phosphorylation of all three sites blocks Raf-1 binding to Ras.GTP in vivo and that cAMP stimulates binding of 14-3-3 proteins to Ser233 and Ser259. Guanosine Triphosphate 81-84 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 60-65 12446733-3 2003 Raf-1 is also thought to be recruited to the small G protein Rap1 upon GTP loading of Rap1. Guanosine Triphosphate 71-74 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 0-5 12006650-7 2002 To examine the localization of the GTP-bound form of Ras, we used a FRET assay that exploits the specific interaction of GTP-bound CFP-Ras with the YFP-fused Ras binding domain of c-Raf. Guanosine Triphosphate 35-38 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 180-185 12006650-7 2002 To examine the localization of the GTP-bound form of Ras, we used a FRET assay that exploits the specific interaction of GTP-bound CFP-Ras with the YFP-fused Ras binding domain of c-Raf. Guanosine Triphosphate 121-124 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 180-185 9525855-0 1998 Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C. Receptor tyrosine kinase-mediated activation of the Raf-1 protein kinase is coupled to the small guanosine triphosphate (GTP)-binding protein Ras. Guanosine Triphosphate 179-201 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 55-60 10319320-4 1999 16K hPRL indirectly increased cAMP levels; however, the blockade of Raf-1 activation was not dependent on the stimulation of cAMP-dependent protein kinase (PKA), but rather on the inhibition of the GTP-bound Ras. Guanosine Triphosphate 198-201 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 68-73 10234739-2 1999 Wild-type Ras cycles between the activated GTP-bound and the inactivated GDP-bound state, and the GTPase reaction is a timer for the interaction between Ras-GTP and effector molecules such as Raf-1 protein kinase. Guanosine Triphosphate 43-46 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 192-197 9780005-8 1998 Injection of antibodies to p21ras itself, or a recombinant Raf-1 protein domain which binds to the effector region of ras in a GTP-dependent manner, results in the inhibition of cell cycle progression throughout G1 phase. Guanosine Triphosphate 127-130 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 59-64 10712905-1 2000 Activation of the protein kinase Raf-1 is a complex process involving association with the GTP-bound form of Ras (Ras-GTP), membrane translocation and both serine/threonine and tyrosine phosphorylation (reviewed in [1]). Guanosine Triphosphate 91-94 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 33-38 9931261-9 1999 A molecular dynamics simulation of a model structure of the Raf-1 RBD.Ras.GTP complex suggested that Lys84 in Raf-1 might instead form a tight salt bridge with Asp33 in Ras. Guanosine Triphosphate 74-77 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 60-65 9931261-9 1999 A molecular dynamics simulation of a model structure of the Raf-1 RBD.Ras.GTP complex suggested that Lys84 in Raf-1 might instead form a tight salt bridge with Asp33 in Ras. Guanosine Triphosphate 74-77 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 110-115 9525855-0 1998 Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C. Receptor tyrosine kinase-mediated activation of the Raf-1 protein kinase is coupled to the small guanosine triphosphate (GTP)-binding protein Ras. Guanosine Triphosphate 179-201 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 134-139 9525855-0 1998 Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C. Receptor tyrosine kinase-mediated activation of the Raf-1 protein kinase is coupled to the small guanosine triphosphate (GTP)-binding protein Ras. Guanosine Triphosphate 19-22 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 55-60 9525855-0 1998 Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C. Receptor tyrosine kinase-mediated activation of the Raf-1 protein kinase is coupled to the small guanosine triphosphate (GTP)-binding protein Ras. Guanosine Triphosphate 19-22 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 134-139 7604263-4 1995 Loading of plasma membranes from transformed cells with guanosine triphosphate (GTP) resulted in inactivation of endogenous or exogenous Raf-1; inactivation was blocked by inclusion of protein phosphatase inhibitors. Guanosine Triphosphate 56-78 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 137-142 8626511-7 1996 These results indicate that although GAP, NF1, Raf-1, and ralGDS all interact with H-Ras in a GTP-dependent manner and they are able to compete against each other for binding to H-Ras, these factors share overlapping but not identical binding domains on H-Ras. Guanosine Triphosphate 94-97 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 47-52 8607981-10 1995 Using mutagenesis, peptide epitope scanning, and in vitro reconstitution of protein interactions, we have identified specific sites of association between the Ras-GTP and c-Raf-1 proteins. Guanosine Triphosphate 163-166 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 171-176 7542586-7 1995 Using mutants of Raf-1 at Tyr340/341, we show that in addition to tyrosine phosphorylation at these sites, there is an additional activation step resulting from p21Ras-GTP recruiting p74Raf-1 to the plasma membrane. Guanosine Triphosphate 168-171 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 17-22 7576990-5 1995 This GTP-bound form of p21ras interacts with the protein kinase raf1 and induces the activation of a kinase cascade, resulting in various cellular responses. Guanosine Triphosphate 5-8 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 64-68 9199317-5 1997 OSM stimulation of Raf-1 correlated with GTP loading of Ras, whereas IFN-beta activation of Raf-1 was Ras independent. Guanosine Triphosphate 41-44 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 19-24 7604263-4 1995 Loading of plasma membranes from transformed cells with guanosine triphosphate (GTP) resulted in inactivation of endogenous or exogenous Raf-1; inactivation was blocked by inclusion of protein phosphatase inhibitors. Guanosine Triphosphate 80-83 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 137-142 7983008-1 1994 A critical event in a signal transduction pathway downstream of receptor tyrosine kinases is the physical association of GTP-liganded Ras with the serine/threonine kinase, Raf-1. Guanosine Triphosphate 121-124 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 172-177 8002932-0 1994 The Ras-related protein R-ras interacts directly with Raf-1 in a GTP-dependent manner. Guanosine Triphosphate 65-68 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 54-59 8002932-3 1994 This interaction requires only the N-terminal regulatory domain (amino acids 1-256) of Raf-1, and is observed with both the wild type and a constitutively active R-ras mutant, but not with a deletion mutant that lacks the potential effector domain or a mutant of R-ras impaired for GTP binding. Guanosine Triphosphate 282-285 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 87-92 8002932-4 1994 Moreover, using an in vitro binding assay we show a direct GTP-dependent interaction of purified R-ras with a purified Raf-1 fragment corresponding to the proposed 81-amino-acid H-Ras-binding domain of Raf-1 (amino acids 51-131). Guanosine Triphosphate 59-62 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 119-124 8002932-4 1994 Moreover, using an in vitro binding assay we show a direct GTP-dependent interaction of purified R-ras with a purified Raf-1 fragment corresponding to the proposed 81-amino-acid H-Ras-binding domain of Raf-1 (amino acids 51-131). Guanosine Triphosphate 59-62 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 202-207 8378348-0 1993 GTP-dependent association of Raf-1 with Ha-Ras: identification of Raf as a target downstream of Ras in mammalian cells. Guanosine Triphosphate 0-3 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 29-34 8503013-0 1993 Complexes of Ras.GTP with Raf-1 and mitogen-activated protein kinase kinase. Guanosine Triphosphate 17-20 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 26-31 8503013-3 1993 Forms of Ras activated either by mutation (Gly12Val) or by binding of the GTP analog, guanylyl-imidodiphosphate (GMP-PNP) interacted specifically with Raf-1 whereas an effector domain mutant, Ile36Ala, failed to interact with Raf-1. Guanosine Triphosphate 74-77 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 151-156 8024815-4 1994 Notable advances were made in defining tyrosine kinase receptor regulation of Ras, and these discoveries were combined with the identification of Raf-1, a serine-threonine protein kinase in the MAPK pathway, as an effector for Ras GTP. Guanosine Triphosphate 231-234 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 146-151 8349650-4 1993 Here we demonstrate that expression of activated forms of the GTP-binding protein Ras or of the serine/threonine kinase Raf-1 results in the activation of transcription specifically through kappa B sites. Guanosine Triphosphate 62-65 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 120-125