PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
31638832-9	2019	Conclusions - p.Gly23Val-MRAS is both necessary and sufficient to elicit a cardiac hypertrophy phenotype in iPSC-CMs that includes increased cell size, changes in cardiac gene expression, and abnormal calcium handling- providing further evidence to establish the monogenetic pathogenicity of p.Gly23Val-MRAS in Noonan syndrome with cardiac hypertrophy.	Calcium	201-208	muscle RAS oncogene homolog	Homo sapiens	25-29
28289718-3	2017	Mutation analysis using in silico mutation prediction tools and molecular dynamics simulations predicted the identified variant, p.Gly23Val-MRAS, to be damaging to normal protein function and adversely affect effector interaction regions and the GTP-binding site.	Guanosine Triphosphate	246-249	muscle RAS oncogene homolog	Homo sapiens	140-144
31770223-6	2019	In relation to lipid profile, rs40593, rs751357, rs6782181 were associated with increased total cholesterol (TC) levels.Summarily, this study suggested that MRAS rs40593 may contribute to the increased risk of area of cerebral infarction of IS in Han population.	Cholesterol	96-107	muscle RAS oncogene homolog	Homo sapiens	157-161
20479006-2	2010	Here, to clarify the mechanism of state transition, we have carried out x-ray crystal structure analyses of a series of mutant H-Ras and M-Ras in complex with guanosine 5"-(beta,gamma-imido)triphosphate (GppNHp), representing various intermediate states of the transition.	Guanylyl Imidodiphosphate	159-202	muscle RAS oncogene homolog	Homo sapiens	137-142
21388959-6	2011	Comparison among the two structures and other state 1 and state 2 structures of H-Ras/M-Ras reveal two new structural features playing critical roles in state dynamics; interaction of residues 31/41 (H-Ras/M-Ras) with residues 29/39 and 30/40, which induces a conformational change of switch I favoring its interaction with the gamma-phosphate, and the hydrogen-bonding interaction of switch II with its neighboring alpha-helix, alpha3-helix, which induces a conformational change of switch II favoring its interaction with the gamma-phosphate.	Hydrogen	353-361	muscle RAS oncogene homolog	Homo sapiens	86-91
21388959-6	2011	Comparison among the two structures and other state 1 and state 2 structures of H-Ras/M-Ras reveal two new structural features playing critical roles in state dynamics; interaction of residues 31/41 (H-Ras/M-Ras) with residues 29/39 and 30/40, which induces a conformational change of switch I favoring its interaction with the gamma-phosphate, and the hydrogen-bonding interaction of switch II with its neighboring alpha-helix, alpha3-helix, which induces a conformational change of switch II favoring its interaction with the gamma-phosphate.	Hydrogen	353-361	muscle RAS oncogene homolog	Homo sapiens	206-211
21388959-6	2011	Comparison among the two structures and other state 1 and state 2 structures of H-Ras/M-Ras reveal two new structural features playing critical roles in state dynamics; interaction of residues 31/41 (H-Ras/M-Ras) with residues 29/39 and 30/40, which induces a conformational change of switch I favoring its interaction with the gamma-phosphate, and the hydrogen-bonding interaction of switch II with its neighboring alpha-helix, alpha3-helix, which induces a conformational change of switch II favoring its interaction with the gamma-phosphate.	gamma-phosphate	328-343	muscle RAS oncogene homolog	Homo sapiens	86-91
21388959-6	2011	Comparison among the two structures and other state 1 and state 2 structures of H-Ras/M-Ras reveal two new structural features playing critical roles in state dynamics; interaction of residues 31/41 (H-Ras/M-Ras) with residues 29/39 and 30/40, which induces a conformational change of switch I favoring its interaction with the gamma-phosphate, and the hydrogen-bonding interaction of switch II with its neighboring alpha-helix, alpha3-helix, which induces a conformational change of switch II favoring its interaction with the gamma-phosphate.	gamma-phosphate	328-343	muscle RAS oncogene homolog	Homo sapiens	206-211
21388959-6	2011	Comparison among the two structures and other state 1 and state 2 structures of H-Ras/M-Ras reveal two new structural features playing critical roles in state dynamics; interaction of residues 31/41 (H-Ras/M-Ras) with residues 29/39 and 30/40, which induces a conformational change of switch I favoring its interaction with the gamma-phosphate, and the hydrogen-bonding interaction of switch II with its neighboring alpha-helix, alpha3-helix, which induces a conformational change of switch II favoring its interaction with the gamma-phosphate.	Phosphates	334-343	muscle RAS oncogene homolog	Homo sapiens	86-91
21388959-6	2011	Comparison among the two structures and other state 1 and state 2 structures of H-Ras/M-Ras reveal two new structural features playing critical roles in state dynamics; interaction of residues 31/41 (H-Ras/M-Ras) with residues 29/39 and 30/40, which induces a conformational change of switch I favoring its interaction with the gamma-phosphate, and the hydrogen-bonding interaction of switch II with its neighboring alpha-helix, alpha3-helix, which induces a conformational change of switch II favoring its interaction with the gamma-phosphate.	Phosphates	334-343	muscle RAS oncogene homolog	Homo sapiens	206-211
20479006-2	2010	Here, to clarify the mechanism of state transition, we have carried out x-ray crystal structure analyses of a series of mutant H-Ras and M-Ras in complex with guanosine 5"-(beta,gamma-imido)triphosphate (GppNHp), representing various intermediate states of the transition.	Guanylyl Imidodiphosphate	204-210	muscle RAS oncogene homolog	Homo sapiens	137-142
15994326-0	2005	Crystal structure of M-Ras reveals a GTP-bound "off" state conformation of Ras family small GTPases.	Guanosine Triphosphate	37-40	muscle RAS oncogene homolog	Homo sapiens	21-26
15994326-2	2005	We have solved the crystal structure of M-Ras in the GDP-bound and guanosine 5"-(beta,gamma-imido)triphosphate (Gpp(NH)p)-bound forms.	Guanosine Diphosphate	53-56	muscle RAS oncogene homolog	Homo sapiens	40-45
15994326-2	2005	We have solved the crystal structure of M-Ras in the GDP-bound and guanosine 5"-(beta,gamma-imido)triphosphate (Gpp(NH)p)-bound forms.	Guanylyl Imidodiphosphate	67-110	muscle RAS oncogene homolog	Homo sapiens	40-45
15994326-2	2005	We have solved the crystal structure of M-Ras in the GDP-bound and guanosine 5"-(beta,gamma-imido)triphosphate (Gpp(NH)p)-bound forms.	Guanylyl Imidodiphosphate	112-121	muscle RAS oncogene homolog	Homo sapiens	40-45
15994326-3	2005	The overall structure of M-Ras resembles those of H-Ras and Rap2A, except that M-Ras-Gpp(NH)p exhibits a distinctive switch I conformation, which is caused by impaired intramolecular interactions between Thr-45 (corresponding to Thr-35 of H-Ras) of the effector region and the gamma-phosphate of Gpp(NH)p. Previous 31P NMR studies showed that H-Ras-Gpp(NH)p exists in two interconverting conformations, states 1 and 2.	Threonine	204-207	muscle RAS oncogene homolog	Homo sapiens	25-30
15994326-3	2005	The overall structure of M-Ras resembles those of H-Ras and Rap2A, except that M-Ras-Gpp(NH)p exhibits a distinctive switch I conformation, which is caused by impaired intramolecular interactions between Thr-45 (corresponding to Thr-35 of H-Ras) of the effector region and the gamma-phosphate of Gpp(NH)p. Previous 31P NMR studies showed that H-Ras-Gpp(NH)p exists in two interconverting conformations, states 1 and 2.	Threonine	204-207	muscle RAS oncogene homolog	Homo sapiens	79-84
15994326-3	2005	The overall structure of M-Ras resembles those of H-Ras and Rap2A, except that M-Ras-Gpp(NH)p exhibits a distinctive switch I conformation, which is caused by impaired intramolecular interactions between Thr-45 (corresponding to Thr-35 of H-Ras) of the effector region and the gamma-phosphate of Gpp(NH)p. Previous 31P NMR studies showed that H-Ras-Gpp(NH)p exists in two interconverting conformations, states 1 and 2.	Threonine	229-232	muscle RAS oncogene homolog	Homo sapiens	25-30
15994326-3	2005	The overall structure of M-Ras resembles those of H-Ras and Rap2A, except that M-Ras-Gpp(NH)p exhibits a distinctive switch I conformation, which is caused by impaired intramolecular interactions between Thr-45 (corresponding to Thr-35 of H-Ras) of the effector region and the gamma-phosphate of Gpp(NH)p. Previous 31P NMR studies showed that H-Ras-Gpp(NH)p exists in two interconverting conformations, states 1 and 2.	Threonine	229-232	muscle RAS oncogene homolog	Homo sapiens	79-84
15994326-3	2005	The overall structure of M-Ras resembles those of H-Ras and Rap2A, except that M-Ras-Gpp(NH)p exhibits a distinctive switch I conformation, which is caused by impaired intramolecular interactions between Thr-45 (corresponding to Thr-35 of H-Ras) of the effector region and the gamma-phosphate of Gpp(NH)p. Previous 31P NMR studies showed that H-Ras-Gpp(NH)p exists in two interconverting conformations, states 1 and 2.	Phosphates	283-292	muscle RAS oncogene homolog	Homo sapiens	25-30
15994326-3	2005	The overall structure of M-Ras resembles those of H-Ras and Rap2A, except that M-Ras-Gpp(NH)p exhibits a distinctive switch I conformation, which is caused by impaired intramolecular interactions between Thr-45 (corresponding to Thr-35 of H-Ras) of the effector region and the gamma-phosphate of Gpp(NH)p. Previous 31P NMR studies showed that H-Ras-Gpp(NH)p exists in two interconverting conformations, states 1 and 2.	Phosphates	283-292	muscle RAS oncogene homolog	Homo sapiens	79-84
15994326-3	2005	The overall structure of M-Ras resembles those of H-Ras and Rap2A, except that M-Ras-Gpp(NH)p exhibits a distinctive switch I conformation, which is caused by impaired intramolecular interactions between Thr-45 (corresponding to Thr-35 of H-Ras) of the effector region and the gamma-phosphate of Gpp(NH)p. Previous 31P NMR studies showed that H-Ras-Gpp(NH)p exists in two interconverting conformations, states 1 and 2.	ET bromodomain inhibitor	315-318	muscle RAS oncogene homolog	Homo sapiens	25-30
15994326-3	2005	The overall structure of M-Ras resembles those of H-Ras and Rap2A, except that M-Ras-Gpp(NH)p exhibits a distinctive switch I conformation, which is caused by impaired intramolecular interactions between Thr-45 (corresponding to Thr-35 of H-Ras) of the effector region and the gamma-phosphate of Gpp(NH)p. Previous 31P NMR studies showed that H-Ras-Gpp(NH)p exists in two interconverting conformations, states 1 and 2.	ET bromodomain inhibitor	315-318	muscle RAS oncogene homolog	Homo sapiens	79-84
10934204-1	2000	Regulation of MR-GEF by M-Ras-GTP interaction.	Guanosine Triphosphate	30-33	muscle RAS oncogene homolog	Homo sapiens	24-29
12384416-4	2002	Overexpression of constitutively active mutants of H-Ras, N-Ras, or M-Ras resulted in activation of coexpressed Rac-1 through an Ly29402-resistant, PI-3K-independent mechanism.	ly29402	129-136	muscle RAS oncogene homolog	Homo sapiens	68-73
12138204-1	2002	R-Ras3/M-Ras is a novel member of the Ras subfamily of GTP-binding proteins which has a unique expression pattern highly restricted to the mammalian central nervous system.	Guanosine Triphosphate	55-58	muscle RAS oncogene homolog	Homo sapiens	0-6
12138204-1	2002	R-Ras3/M-Ras is a novel member of the Ras subfamily of GTP-binding proteins which has a unique expression pattern highly restricted to the mammalian central nervous system.	Guanosine Triphosphate	55-58	muscle RAS oncogene homolog	Homo sapiens	7-12
11313946-1	2001	Here, we report the identification and characterization of a new member of the RalGDS-family, which is widely expressed and interacts strongly and selectively with the GTP-bound forms of M-Ras and p21 Ras.	Guanosine Triphosphate	168-171	muscle RAS oncogene homolog	Homo sapiens	187-192
34111428-1	2021	The contributions that the R-Ras subfamily (R-Ras, R-Ras2/TC21 and M-Ras) of small GTP-binding proteins make to normal and aberrant cellular functions have historically been poorly understood.	Guanosine Triphosphate	83-86	muscle RAS oncogene homolog	Homo sapiens	67-72
10498616-7	1999	An S27N mutant of M-Ras, like the analogous H-Ras S17N mutant, was a dominant inhibitor of activation of the c-fos promoter by constitutively active Src Y527F, suggesting that M-Ras and p21 Ras shared guanine nucleotide exchange factors and are likely to be activated in parallel.	Guanine Nucleotides	201-219	muscle RAS oncogene homolog	Homo sapiens	18-23
9400994-3	1997	This novel human ras-related gene, R-ras3, encodes for a protein of 209 amino acids, and shows approximately 60-75% sequence identity in the N-terminal catalytic domain with members of the Ras subfamily of GTP-binding proteins.	Guanosine Triphosphate	206-209	muscle RAS oncogene homolog	Homo sapiens	35-41
9400994-9	1997	The close evolutionary conservation between R-ras3 and Ras family members, in contrast to the significant differences in its biological activities and the pattern of tissue expression, raise the possibility that R-ras3 may control novel cellular functions previously not described for other GTP-binding proteins.	Guanosine Triphosphate	291-294	muscle RAS oncogene homolog	Homo sapiens	44-50
9400994-9	1997	The close evolutionary conservation between R-ras3 and Ras family members, in contrast to the significant differences in its biological activities and the pattern of tissue expression, raise the possibility that R-ras3 may control novel cellular functions previously not described for other GTP-binding proteins.	Guanosine Triphosphate	291-294	muscle RAS oncogene homolog	Homo sapiens	212-218
10777492-3	2000	By contrast, guanine nucleotide exchange of M-Ras was promoted by the guanine nucleotide exchange factors (GEFs) for the classical Ras (Ha-, K-, and N-), including mSos, RasGRF, CalDAG-GEFII, and CalDAG-GEFIII.	Guanine Nucleotides	13-31	muscle RAS oncogene homolog	Homo sapiens	44-49
10777492-3	2000	By contrast, guanine nucleotide exchange of M-Ras was promoted by the guanine nucleotide exchange factors (GEFs) for the classical Ras (Ha-, K-, and N-), including mSos, RasGRF, CalDAG-GEFII, and CalDAG-GEFIII.	Guanine Nucleotides	70-88	muscle RAS oncogene homolog	Homo sapiens	44-49
10803462-1	2000	The GTP-binding protein, R-Ras3/M-Ras, is a novel member of the Ras subfamily of GTPases which shows highest sequence similarity to the TC21 gene.	Guanosine Triphosphate	4-7	muscle RAS oncogene homolog	Homo sapiens	25-31
10803462-7	2000	The activation of Akt by R-Ras3 was most likely to be PI3-K-dependent since this biochemical event was blocked by the pharmacological inhibitors, Wortmannin and LY294002, as well as by a dominant negative mutant of PI3-K. More importantly, R-Ras3 affinity-precipitated PI3-K from cell extracts in a GTP-dependent manner, and associated lipid kinase activity was readily detectable in R-Ras3 immune complexes.	Wortmannin	146-156	muscle RAS oncogene homolog	Homo sapiens	25-31
10803462-7	2000	The activation of Akt by R-Ras3 was most likely to be PI3-K-dependent since this biochemical event was blocked by the pharmacological inhibitors, Wortmannin and LY294002, as well as by a dominant negative mutant of PI3-K. More importantly, R-Ras3 affinity-precipitated PI3-K from cell extracts in a GTP-dependent manner, and associated lipid kinase activity was readily detectable in R-Ras3 immune complexes.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	161-169	muscle RAS oncogene homolog	Homo sapiens	25-31
10803462-7	2000	The activation of Akt by R-Ras3 was most likely to be PI3-K-dependent since this biochemical event was blocked by the pharmacological inhibitors, Wortmannin and LY294002, as well as by a dominant negative mutant of PI3-K. More importantly, R-Ras3 affinity-precipitated PI3-K from cell extracts in a GTP-dependent manner, and associated lipid kinase activity was readily detectable in R-Ras3 immune complexes.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	161-169	muscle RAS oncogene homolog	Homo sapiens	240-246
10803462-7	2000	The activation of Akt by R-Ras3 was most likely to be PI3-K-dependent since this biochemical event was blocked by the pharmacological inhibitors, Wortmannin and LY294002, as well as by a dominant negative mutant of PI3-K. More importantly, R-Ras3 affinity-precipitated PI3-K from cell extracts in a GTP-dependent manner, and associated lipid kinase activity was readily detectable in R-Ras3 immune complexes.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	161-169	muscle RAS oncogene homolog	Homo sapiens	240-246
10803462-7	2000	The activation of Akt by R-Ras3 was most likely to be PI3-K-dependent since this biochemical event was blocked by the pharmacological inhibitors, Wortmannin and LY294002, as well as by a dominant negative mutant of PI3-K. More importantly, R-Ras3 affinity-precipitated PI3-K from cell extracts in a GTP-dependent manner, and associated lipid kinase activity was readily detectable in R-Ras3 immune complexes.	Guanosine Triphosphate	299-302	muscle RAS oncogene homolog	Homo sapiens	25-31
10803462-9	2000	As expected, this biological activity of R-Ras3 was also abrogated by the addition of LY294002.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	86-94	muscle RAS oncogene homolog	Homo sapiens	41-47