PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31611389-5 2019 Structures of the wild type and G13D mutant of KRAS in complex with neurofibromin (RasGAP domain) provide the structural basis for neurofibromin-mediated GTP hydrolysis. Guanosine Triphosphate 154-157 RAS p21 protein activator 1 Homo sapiens 83-89 31041977-0 2019 Diversity of mechanisms in Ras-GAP catalysis of guanosine triphosphate hydrolysis revealed by molecular modeling. Guanosine Triphosphate 48-70 RAS p21 protein activator 1 Homo sapiens 27-34 31041977-2 2019 We show that molecular modeling of GTP hydrolysis in the Ras-GAP active site reveals a diversity of mechanisms of the intrinsic chemical reaction depending on molecular groups at position 61 in Ras occupied by glutamine in the wild-type enzyme. Guanosine Triphosphate 35-38 RAS p21 protein activator 1 Homo sapiens 57-64 27043216-4 2016 The mechanism suggested in this study retains the main features of GTP hydrolysis by the Ras-GAP complex, but the relative energies of the corresponding intermediates are different and an additional intermediate exists in the Arl3-RP2 complex compared with the Ras-GAP. Guanosine Triphosphate 67-70 RAS p21 protein activator 1 Homo sapiens 89-96 31041977-6 2019 The results emphasize the role of the Ras residue Gln61 in Ras-GAP catalysis and explain the retained catalytic activity of the Ras-GAP complex towards GTP hydrolysis in the Gln61NGln and Gln61Glu mutants of Ras. Guanosine Triphosphate 152-155 RAS p21 protein activator 1 Homo sapiens 128-135 27214270-0 2016 Theoretical vibrational spectroscopy of intermediates and the reaction mechanism of the guanosine triphosphate hydrolysis by the protein complex Ras-GAP. Guanosine Triphosphate 88-110 RAS p21 protein activator 1 Homo sapiens 145-152 27214270-1 2016 The structures and vibrational spectra of the reacting species upon guanosine triphosphate (GTP) hydrolysis to guanosine diphosphate and inorganic phosphate (Pi) trapped inside the protein complex Ras-GAP were analyzed following the results of QM/MM simulations. Guanosine Triphosphate 68-90 RAS p21 protein activator 1 Homo sapiens 197-204 27214270-1 2016 The structures and vibrational spectra of the reacting species upon guanosine triphosphate (GTP) hydrolysis to guanosine diphosphate and inorganic phosphate (Pi) trapped inside the protein complex Ras-GAP were analyzed following the results of QM/MM simulations. Guanosine Triphosphate 92-95 RAS p21 protein activator 1 Homo sapiens 197-204 27214270-3 2016 A good correlation between the theoretical and experimental vibrational data provides a strong support to the reaction mechanism of GTP hydrolysis by the Ras-GAP enzyme system revealed by the recent QM/MM modeling. Guanosine Triphosphate 132-135 RAS p21 protein activator 1 Homo sapiens 154-161 27043216-4 2016 The mechanism suggested in this study retains the main features of GTP hydrolysis by the Ras-GAP complex, but the relative energies of the corresponding intermediates are different and an additional intermediate exists in the Arl3-RP2 complex compared with the Ras-GAP. Guanosine Triphosphate 67-70 RAS p21 protein activator 1 Homo sapiens 261-268 24224811-10 2013 (ii) The increase in the level of GTP-bound Ras occurs because the HRas mutations perturb the action of p120GAP on Ras. Guanosine Triphosphate 34-37 RAS p21 protein activator 1 Homo sapiens 104-111 26866994-6 2016 The validation involves the study of the S(N)2 step of the reaction catalyzed by haloakene dehalogenase (DhlA) and the GTP hydrolysis in the RasGAP system. Guanosine Triphosphate 119-122 RAS p21 protein activator 1 Homo sapiens 141-147 26370130-0 2015 Why does mutation of Gln61 in Ras by the nitro analog NGln maintain activity of Ras-GAP in hydrolysis of guanosine triphosphate? Guanosine Triphosphate 105-127 RAS p21 protein activator 1 Homo sapiens 80-87 26370130-1 2015 Interpretation of the experiments showing that the Ras-GAP protein complex maintains activity in guanosine triphosphate (GTP) hydrolysis upon replacement of Glu61 in Ras with its unnatural nitro analog, NGln, is an important issue for understanding details of chemical transformations at the enzyme active site. Guanosine Triphosphate 97-119 RAS p21 protein activator 1 Homo sapiens 51-58 26370130-1 2015 Interpretation of the experiments showing that the Ras-GAP protein complex maintains activity in guanosine triphosphate (GTP) hydrolysis upon replacement of Glu61 in Ras with its unnatural nitro analog, NGln, is an important issue for understanding details of chemical transformations at the enzyme active site. Guanosine Triphosphate 121-124 RAS p21 protein activator 1 Homo sapiens 51-58 25820867-0 2015 Computational characterization of the chemical step in the GTP hydrolysis by Ras-GAP for the wild-type and G13V mutated Ras. Guanosine Triphosphate 59-62 RAS p21 protein activator 1 Homo sapiens 77-84 25820867-1 2015 The free energy profiles for the chemical reaction of the guanosine triphosphate hydrolysis GTP + H2O GDP + Pi by Ras-GAP for the wild-type and G13V mutated Ras were computed by using molecular dynamics protocols with the QM(ab initio)/MM potentials. Guanosine Triphosphate 58-80 RAS p21 protein activator 1 Homo sapiens 116-123 25820867-1 2015 The free energy profiles for the chemical reaction of the guanosine triphosphate hydrolysis GTP + H2O GDP + Pi by Ras-GAP for the wild-type and G13V mutated Ras were computed by using molecular dynamics protocols with the QM(ab initio)/MM potentials. Guanosine Triphosphate 92-95 RAS p21 protein activator 1 Homo sapiens 116-123 25663768-10 2015 In addition, pre-miR-21-LV or siRASA1 (down-regulation of RASA1) cells showed higher cell proliferation, reduced apoptosis, increased expression of RAS-GTP, p-AKT, Raf-1, KRAS, and p-ERK1/2, and higher invasion and tumor formation ability, compared with control, anti-miR-21-LV or pcDNA3.1-RASA1 (up-regulation of RASA1) cells (P < 0.05). Guanosine Triphosphate 152-155 RAS p21 protein activator 1 Homo sapiens 32-37 25663768-10 2015 In addition, pre-miR-21-LV or siRASA1 (down-regulation of RASA1) cells showed higher cell proliferation, reduced apoptosis, increased expression of RAS-GTP, p-AKT, Raf-1, KRAS, and p-ERK1/2, and higher invasion and tumor formation ability, compared with control, anti-miR-21-LV or pcDNA3.1-RASA1 (up-regulation of RASA1) cells (P < 0.05). Guanosine Triphosphate 152-155 RAS p21 protein activator 1 Homo sapiens 58-63 25663768-10 2015 In addition, pre-miR-21-LV or siRASA1 (down-regulation of RASA1) cells showed higher cell proliferation, reduced apoptosis, increased expression of RAS-GTP, p-AKT, Raf-1, KRAS, and p-ERK1/2, and higher invasion and tumor formation ability, compared with control, anti-miR-21-LV or pcDNA3.1-RASA1 (up-regulation of RASA1) cells (P < 0.05). Guanosine Triphosphate 152-155 RAS p21 protein activator 1 Homo sapiens 58-63 25339142-0 2014 Modeling the role of G12V and G13V Ras mutations in the Ras-GAP-catalyzed hydrolysis reaction of guanosine triphosphate. Guanosine Triphosphate 97-119 RAS p21 protein activator 1 Homo sapiens 56-63 25339142-4 2014 QM/MM optimization of geometry parameters in the Ras-GAP-GTP complex and QM/MM-MD simulations were performed with a quantum subsystem comprising a large fraction of the enzyme active site. Guanosine Triphosphate 57-60 RAS p21 protein activator 1 Homo sapiens 49-56 25339142-8 2014 The obtained computational results correlate well with the recent kinetic measurements of the Ras-GAP-catalyzed hydrolysis of GTP. Guanosine Triphosphate 126-129 RAS p21 protein activator 1 Homo sapiens 94-101 25202123-6 2014 In TNBC cells, including cells with mutation of RAS, the suppression of either RASA1 or SPRED1 increased the levels of GTP-bound, wild-type RAS and activated ERK 1/2. Guanosine Triphosphate 119-122 RAS p21 protein activator 1 Homo sapiens 79-84 22664862-7 2012 This is the first report demonstrating that PAG inhibits the proliferation and invasion potential of prostate cancer cells via the interaction with RasGAP to recruit RasGAP to the cell membrane, where RasGAP hydrolyzes GTP to GDP, reduces the level of activated Ras, and ultimately suppresses the activation of ERK1/2, cyclin D1 and other effectors of the Ras signaling pathway. Guanosine Triphosphate 243-246 RAS p21 protein activator 1 Homo sapiens 172-178 23236136-5 2012 During generation of the RabGAP Rab:GTP complex, there is a rapid conformational change in which the cis-glutamine is replaced by a glutamine from RabGAP (trans-glutamine); this differs from the RasGAP mechanism, where the cis-glutamine is also important for GAP catalysis. Guanosine Triphosphate 36-39 RAS p21 protein activator 1 Homo sapiens 195-201 23650596-2 2012 A novel GTP-hydrolysis mechanism is employed by MnmE, YqeH and FeoB, where a potassium ion plays a role analogous to the Arginine finger of the Ras-RasGAP system, to accelerate otherwise slow GTP hydrolysis rates. Guanosine Triphosphate 8-11 RAS p21 protein activator 1 Homo sapiens 148-154 23650596-2 2012 A novel GTP-hydrolysis mechanism is employed by MnmE, YqeH and FeoB, where a potassium ion plays a role analogous to the Arginine finger of the Ras-RasGAP system, to accelerate otherwise slow GTP hydrolysis rates. Guanosine Triphosphate 192-195 RAS p21 protein activator 1 Homo sapiens 148-154 19321438-3 2009 However, instead of accelerating hydrolysis of bound GTP on Ras IQGAP1, using its GAP-related domain (GRD) binds to Cdc42 and Rac1 and stabilizes their GTP-bound states. Guanosine Triphosphate 53-56 RAS p21 protein activator 1 Homo sapiens 66-69 20018863-6 2010 On the other hand, the mant tag inhibits TSC2GAP-catalyzed GTP hydrolysis by Rheb but promotes p120 RasGAP-catalyzed GTP hydrolysis by H-Ras. Guanosine Triphosphate 117-120 RAS p21 protein activator 1 Homo sapiens 95-99 19321438-3 2009 However, instead of accelerating hydrolysis of bound GTP on Ras IQGAP1, using its GAP-related domain (GRD) binds to Cdc42 and Rac1 and stabilizes their GTP-bound states. Guanosine Triphosphate 152-155 RAS p21 protein activator 1 Homo sapiens 66-69 19321438-10 2009 Assuming a mode of interaction similar to that displayed in the Ras-RasGAP complex, we created an energy-minimized model of Cdc42.GTP bound to the GRD. Guanosine Triphosphate 130-133 RAS p21 protein activator 1 Homo sapiens 68-74 19022332-1 2009 p120-RasGAP (Ras GTPase activating protein) plays a key role in the regulation of Ras-GTP bound by promoting GTP hydrolysis via its C-terminal catalytic domain. Guanosine Triphosphate 17-20 RAS p21 protein activator 1 Homo sapiens 0-11 19022332-1 2009 p120-RasGAP (Ras GTPase activating protein) plays a key role in the regulation of Ras-GTP bound by promoting GTP hydrolysis via its C-terminal catalytic domain. Guanosine Triphosphate 86-89 RAS p21 protein activator 1 Homo sapiens 0-11 18682833-1 2008 The Ras GTPase-activating protein RasGAP catalyzes the conversion of active GTP-bound Ras into inactive GDP-bound Ras. Guanosine Triphosphate 8-11 RAS p21 protein activator 1 Homo sapiens 34-40 17094109-0 2007 Mechanisms of guanosine triphosphate hydrolysis by Ras and Ras-GAP proteins as rationalized by ab initio QM/MM simulations. Guanosine Triphosphate 14-36 RAS p21 protein activator 1 Homo sapiens 63-66 17094109-9 2007 The results of simulations are compared to the previous findings for the GTP hydrolysis in the Ras-GAP (p21(ras)-p120(GAP)) protein complex. Guanosine Triphosphate 73-76 RAS p21 protein activator 1 Homo sapiens 99-102 17094109-9 2007 The results of simulations are compared to the previous findings for the GTP hydrolysis in the Ras-GAP (p21(ras)-p120(GAP)) protein complex. Guanosine Triphosphate 73-76 RAS p21 protein activator 1 Homo sapiens 113-122 16757310-0 2006 Real-time in vitro measurement of intrinsic and Ras GAP-mediated GTP hydrolysis. Guanosine Triphosphate 65-68 RAS p21 protein activator 1 Homo sapiens 48-55 16052311-1 2005 The structures of the complexes between Ras*GDP bound to RasGAP in the presence of three probable gamma-phosphate analogs (AlF3, AlF4- and MgF3-) for the transition state (TS) of the hydrolysis of guanosine triphosphate (GTP) by the Ras-RasGAP enzymes have been modeled by quantum mechanical-molecular mechanical (QM/MM) calculations. Guanosine Triphosphate 197-219 RAS p21 protein activator 1 Homo sapiens 57-63 15906320-0 2005 QM/MM modeling the Ras-GAP catalyzed hydrolysis of guanosine triphosphate. Guanosine Triphosphate 51-73 RAS p21 protein activator 1 Homo sapiens 19-26 15906320-1 2005 The mechanism of the hydrolysis reaction of guanosine triphosphate (GTP) by the protein complex Ras-GAP (p21(ras) - p120(GAP)) has been modeled by the quantum mechanical-molecular mechanical (QM/MM) and ab initio quantum calculations. Guanosine Triphosphate 44-66 RAS p21 protein activator 1 Homo sapiens 96-103 15906320-1 2005 The mechanism of the hydrolysis reaction of guanosine triphosphate (GTP) by the protein complex Ras-GAP (p21(ras) - p120(GAP)) has been modeled by the quantum mechanical-molecular mechanical (QM/MM) and ab initio quantum calculations. Guanosine Triphosphate 44-66 RAS p21 protein activator 1 Homo sapiens 116-125 15906320-1 2005 The mechanism of the hydrolysis reaction of guanosine triphosphate (GTP) by the protein complex Ras-GAP (p21(ras) - p120(GAP)) has been modeled by the quantum mechanical-molecular mechanical (QM/MM) and ab initio quantum calculations. Guanosine Triphosphate 68-71 RAS p21 protein activator 1 Homo sapiens 96-103 15906320-1 2005 The mechanism of the hydrolysis reaction of guanosine triphosphate (GTP) by the protein complex Ras-GAP (p21(ras) - p120(GAP)) has been modeled by the quantum mechanical-molecular mechanical (QM/MM) and ab initio quantum calculations. Guanosine Triphosphate 68-71 RAS p21 protein activator 1 Homo sapiens 116-125 15906320-4 2005 At the first stage, a unified motion of Arg789 of GAP, Gln61, Thr35 of Ras, and the lytic water molecule results in a substantial spatial separation of the gamma-phosphate group of GTP from the rest of the molecule (GDP). Guanosine Triphosphate 181-184 RAS p21 protein activator 1 Homo sapiens 50-53 15292263-8 2004 RapGAP binding induces a GTP(*) conformation in which the three phosphate groups are oriented such that they are vibrationally coupled to each other, in contrast to what was seen in the intrinsic and the Ras.RasGAP reactions. Guanosine Triphosphate 25-28 RAS p21 protein activator 1 Homo sapiens 208-214 15917201-7 2005 RASA1 reverts active GTP-bound Ras into inactive GDP-bound form. Guanosine Triphosphate 21-24 RAS p21 protein activator 1 Homo sapiens 0-5 15210132-0 2004 Quantum chemical modeling of the GTP hydrolysis by the RAS-GAP protein complex. Guanosine Triphosphate 33-36 RAS p21 protein activator 1 Homo sapiens 55-62 15340059-3 2004 Rheb and TSC2 comprise a unique pair of GTPase and GAP, because Rheb has high basal GTP levels and TSC2 does not have the catalytic arginine finger found in Ras-GAP. Guanosine Triphosphate 40-43 RAS p21 protein activator 1 Homo sapiens 157-164 15210132-1 2004 We present results of the modeling for the hydrolysis reaction of guanosine triphosphate (GTP) in the RAS-GAP protein complex using essentially ab initio quantum chemistry methods. Guanosine Triphosphate 66-88 RAS p21 protein activator 1 Homo sapiens 102-109 15210132-1 2004 We present results of the modeling for the hydrolysis reaction of guanosine triphosphate (GTP) in the RAS-GAP protein complex using essentially ab initio quantum chemistry methods. Guanosine Triphosphate 90-93 RAS p21 protein activator 1 Homo sapiens 102-109 15210132-4 2004 Our results show that the GTP hydrolysis in the RAS-GAP protein complex can be modeled by a substrate-assisted catalytic mechanism. Guanosine Triphosphate 26-29 RAS p21 protein activator 1 Homo sapiens 48-55 15210132-9 2004 We present arguments favoring the assumption that the first step of the GTP hydrolysis reaction in the RAS-GAP protein complex may be assigned to the breaking of the Pgamma-O(Pbeta) bond prior to the creation of the inorganic phosphate. Guanosine Triphosphate 72-75 RAS p21 protein activator 1 Homo sapiens 103-110 17052120-5 2004 Extracelluar stimuli initiate Ras interactions with GDP/GTP exchange factors such as SOS, and GTP-hydrolysis activating proteins such as RasGAP. Guanosine Triphosphate 94-97 RAS p21 protein activator 1 Homo sapiens 137-143 12787671-1 2003 Ras specific GTPase activating proteins (GAPs), neurofibromin and p120GAP, bind GTP bound Ras and efficiently complement its active site. Guanosine Triphosphate 13-16 RAS p21 protein activator 1 Homo sapiens 66-73 11566491-3 2001 Ras activation (GTP binding) is induced by the GTP exchange factor Sos and its inactivation is regulated through the GAPs (p120GAP and neurofibromin). Guanosine Triphosphate 16-19 RAS p21 protein activator 1 Homo sapiens 123-130 9312123-4 1997 To distinguish the GTPase-activating effect of p120-GAP from other effects dependent on the interaction with activated Ha-Ras, the nonhydrolyzable GTP analogue guanosine 5"-O-(thiotriphosphate) (GTPgammaS) was used. Guanosine Triphosphate 19-22 RAS p21 protein activator 1 Homo sapiens 47-55 11371635-9 2001 We find that the carbonyl oxygen on the backbone of the arginine finger supplied in trans by p120GAP (Arg-789) interacts with a water molecule in the active site that is forming a bridge between the NH(2) group of the Gln-61 and the gamma-phosphate of GTP. Guanosine Triphosphate 252-255 RAS p21 protein activator 1 Homo sapiens 93-100 9312123-9 1997 As a consequence of this inhibition, presence of p120-GAP enhanced the regeneration of Ha-Ras.GTPgammaS by GEF at a GDP:GTPgammaS ratio mimicking the in vivo GDP:GTP ratio. Guanosine Triphosphate 94-97 RAS p21 protein activator 1 Homo sapiens 49-57 9312123-10 1997 Our work describes a novel function of p120-GAP and suggests a mechanism by which GAP protects Ha-Ras.GTP in vivo against unproductive exchanges. Guanosine Triphosphate 102-105 RAS p21 protein activator 1 Homo sapiens 39-47 9312123-11 1997 This constrain is likely involved in the regulation of the physiological GDP/GTP cycle of Ras and in the action of p120-GAP as downstream effector of Ras. Guanosine Triphosphate 77-80 RAS p21 protein activator 1 Homo sapiens 115-123 8816504-9 1996 Thus, activation of PI3K requires not only binding of PI3K to the tyrosine-phosphorylated PDGFR but accumulation of GTP-bound Ras as well. Guanosine Triphosphate 116-119 RAS p21 protein activator 1 Homo sapiens 126-129 9102473-3 1997 It is shown here for p21ras, a well studied example of GTP hydrolysing proteins, that the GTP-hydrolysis rate is significantly faster if Mg2+ is replaced by Mn2+, both in the presence or absence of its GTPase-activating protein Ras-GAP. Guanosine Triphosphate 55-58 RAS p21 protein activator 1 Homo sapiens 228-235 9102473-3 1997 It is shown here for p21ras, a well studied example of GTP hydrolysing proteins, that the GTP-hydrolysis rate is significantly faster if Mg2+ is replaced by Mn2+, both in the presence or absence of its GTPase-activating protein Ras-GAP. Guanosine Triphosphate 90-93 RAS p21 protein activator 1 Homo sapiens 228-235 8607981-5 1995 The GTP-bound form of Ras is capable of interacting directly with RasGAP, neurofibromin, and the Raf kinases. Guanosine Triphosphate 4-7 RAS p21 protein activator 1 Homo sapiens 66-72 8621595-1 1996 The mammalian Ras GTPase-activating protein (p120Ras-GAP) interacts with activated members of the Ras superfamily of GTP-binding proteins to accelerate their deactivation by sharply increasing their rates of GTP hydrolysis. Guanosine Triphosphate 18-21 RAS p21 protein activator 1 Homo sapiens 45-56 8621595-1 1996 The mammalian Ras GTPase-activating protein (p120Ras-GAP) interacts with activated members of the Ras superfamily of GTP-binding proteins to accelerate their deactivation by sharply increasing their rates of GTP hydrolysis. Guanosine Triphosphate 117-120 RAS p21 protein activator 1 Homo sapiens 45-56 8909796-2 1996 GTPase activating proteins (p120GAP, neurofibromin and GAP1) are negative regulators that stimulate hydrolysis of bound GTP to GDP, and guanine nucleotide exchange factors (Sos and Ras-GRF) are positive regulators that stimulate the exchange of GDP bound to Ras for fresh GTP from the cytosol. Guanosine Triphosphate 0-3 RAS p21 protein activator 1 Homo sapiens 28-35 8909796-2 1996 GTPase activating proteins (p120GAP, neurofibromin and GAP1) are negative regulators that stimulate hydrolysis of bound GTP to GDP, and guanine nucleotide exchange factors (Sos and Ras-GRF) are positive regulators that stimulate the exchange of GDP bound to Ras for fresh GTP from the cytosol. Guanosine Triphosphate 120-123 RAS p21 protein activator 1 Homo sapiens 28-35 7492562-1 1995 The rate of GTP hydrolysis on p21ras is accelerated by approximately 10(5) times by the catalytic domains of GTPase-activating proteins (GAPs), p120-GAP (GAP-344) or neurofibromin (NF1-334). Guanosine Triphosphate 12-15 RAS p21 protein activator 1 Homo sapiens 144-152 7499225-1 1995 The effector binding domain and the switch II region of c-Ha-Ras are necessary for p120GAP-stimulated GTP hydrolysis. Guanosine Triphosphate 102-105 RAS p21 protein activator 1 Homo sapiens 83-90 7935432-0 1994 p190 RhoGAP, the major RasGAP-associated protein, binds GTP directly. Guanosine Triphosphate 56-59 RAS p21 protein activator 1 Homo sapiens 23-29 8738474-2 1995 Ras GTPase-activating protein (rasGAP) is a major contributor to the downregulation of ras by facilitating GTP hydrolysis of activated ras. Guanosine Triphosphate 4-7 RAS p21 protein activator 1 Homo sapiens 31-37 8195713-8 1994 Thus, the p210bcr/abl-dependent regulation of p120GAP activity is responsible, in part, for the maintenance of p21ras in the active GTP-bound form, a crucial requirement for CML cell proliferation. Guanosine Triphosphate 132-135 RAS p21 protein activator 1 Homo sapiens 46-53 7516336-1 1994 Rap 1b is a 22-kDa low molecular mass GTP-binding protein which is both a member of the Ras superfamily and a substrate for cAMP-dependent protein kinase. Guanosine Triphosphate 38-41 RAS p21 protein activator 1 Homo sapiens 88-91 8270251-3 1994 We hypothesized that, if tumor development is related to the p21 ras being in the active GTP-bound state, then a similar malignant phenotype may result from an inactivating mutation in the ras GAP gene in the region that interacts with ras p21 (so-called catalytic domain). Guanosine Triphosphate 89-92 RAS p21 protein activator 1 Homo sapiens 189-196 33125148-1 2020 Ras p21 protein activator 1 (RASA1) is a regulator of Ras GDP and GTP and is involved in numerous physiological processes such as angiogenesis, cell proliferation, and apoptosis. Guanosine Triphosphate 66-69 RAS p21 protein activator 1 Homo sapiens 0-27 8262937-2 1993 Single turnover and equilibrium binding measurements on the interaction of Gly-12 and Pro-12 Ras.GTP with the catalytic domains of the GTPase-activating proteins, p120-GAP and neurofibromin, have been made utilizing fluorescent 2"(3")O-(N-methylanthraniloyl)-nucleotides. Guanosine Triphosphate 97-100 RAS p21 protein activator 1 Homo sapiens 163-171 8262937-5 1993 Both p120-GAP and neurofibromin increased the rate constant of the GTP hydrolysis step of Pro-12 Ras, but the maximal activation at 30 degrees C was 120-fold and 560-fold, as compared with 70,000- and 52,000-fold, with Gly-12 Ras. Guanosine Triphosphate 67-70 RAS p21 protein activator 1 Homo sapiens 5-13 8338843-1 1993 The mechanism of the hydrolysis of GTP by p21N-ras and its activation by the catalytic domain of p120 GTPase activating protein (GAP) have been studied using a combination of chemical and fluorescence measurements with the fluorescent GTP analogue, 2"(3")-O-(N-methylanthraniloyl)GTP (mantGTP). Guanosine Triphosphate 35-38 RAS p21 protein activator 1 Homo sapiens 97-101 8338843-1 1993 The mechanism of the hydrolysis of GTP by p21N-ras and its activation by the catalytic domain of p120 GTPase activating protein (GAP) have been studied using a combination of chemical and fluorescence measurements with the fluorescent GTP analogue, 2"(3")-O-(N-methylanthraniloyl)GTP (mantGTP). Guanosine Triphosphate 102-105 RAS p21 protein activator 1 Homo sapiens 97-101 1939245-5 1991 We observed that both Rap1A-GDP and Rap1A-guanosine 5"-3-O-(thio)triphosphate (GTP gamma S) were able to block the inhibitory effect of Ras-GAP upon channel activation. Guanosine Triphosphate 79-82 RAS p21 protein activator 1 Homo sapiens 136-143 1939245-8 1991 The effectiveness of Rap1A to inhibit Ras-GAP is dependent upon the amount of Ras-GAP present in the assay and can also be overcome by the addition of GTP-bound N-Ras (GC-43), suggesting a competitive mechanism is operative. Guanosine Triphosphate 151-154 RAS p21 protein activator 1 Homo sapiens 38-45 2115644-5 1990 We have, therefore, mutated thr61 of p21rap1A to glutamine and shown that ras-GAP is now able to accelerate the rate of hydrolysis of GTP. Guanosine Triphosphate 134-137 RAS p21 protein activator 1 Homo sapiens 74-81 33125148-1 2020 Ras p21 protein activator 1 (RASA1) is a regulator of Ras GDP and GTP and is involved in numerous physiological processes such as angiogenesis, cell proliferation, and apoptosis. Guanosine Triphosphate 66-69 RAS p21 protein activator 1 Homo sapiens 29-34