PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31199148-1 2019 Mutations at the arginine residue (R132) in isocitrate dehydrogenase 1 (IDH1) are frequently identified in various human cancers. Arginine 17-25 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 44-70 31199148-1 2019 Mutations at the arginine residue (R132) in isocitrate dehydrogenase 1 (IDH1) are frequently identified in various human cancers. Arginine 17-25 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 72-76 30194083-3 2018 IDH1 and IDH2 mutations are restricted to specific arginine residues in the active site of the enzymes and are gain-of-function, i.e. they confer a neomorphic enzyme activity resulting in the accumulation of D-2-hydroxyglutarate (2-HG). Arginine 51-59 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 0-4 29743236-0 2018 IDH1 Arg-132 mutant promotes tumor formation through down-regulating p53. Arginine 5-8 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 0-4 29382206-3 2018 Owing to a mutation in an important arginine residue in the catalytic pocket, mutant IDH1 catalyzes the production of 2-hydroxyglutarate (2-HG) instead of its wild type product alpha-ketoglutarate (alpha-KG), which is involved in multiple cellular pathways involving the hydroxylation of proteins, ribonucleic acid, and deoxyribose nucleic acid (DNA). Arginine 36-44 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 85-89 29670690-1 2018 Somatic point mutations at a key arginine residue (R132) within the active site of the metabolic enzyme isocitrate dehydrogenase 1 (IDH1) confer a novel gain of function in cancer cells, resulting in the production of d-2-hydroxyglutarate (2-HG), an oncometabolite. Arginine 33-41 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 132-136 27406240-1 2017 Arginine 132 (R132) mutations to histidine or cysteine frequently occur to cytosolic NADP+ -isocitrate dehydrogenase (IDH1) in secondary glioblastoma multiforme (GBM) patients, in which GBM develops from a lower grade astroctyoma. Arginine 0-8 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 118-122 29303363-1 2018 In recent years, de novo missense structural mutations in the IDH1 gene of arginine at site 132 (R132) have become a standard for diagnostication and prognostication in glioma management. Arginine 75-83 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 62-66 27406240-7 2017 As human IDH1 Arg132 mutation is cancer-associated, the present study provides new information for the in-depth investigation of the metabolic influence of EcIDH Arg mutation in vivo. Arginine 14-17 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 9-13 26188014-3 2016 IDH enzymes normally catalyze the decarboxylation of isocitrate to generate alpha-ketoglutarate (alphaKG), but recurrent mutations at Arg(132) of IDH1 and Arg(172) of IDH2 confer a neomorphic enzyme activity that catalyzes reduction of alphaKG into the putative oncometabolite D-2-hydroxyglutate (D2HG). Arginine 134-137 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 146-150 26967252-12 2016 Within arginine and proline metabolism, levels of intermediate metabolites in creatine pathway were all significantly lower in IDH mutation positive than in negative patients, suggesting an increased activity of creatine pathway in IDH mutation positive tumors. Arginine 7-15 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 127-130 27956631-1 2016 Oncogenic isocitrate dehydrogenase (IDH)1 and IDH2 mutations at three hotspot arginine residues cause an enzymatic gain of function that leads to the production and accumulation of the metabolite 2-hydroxyglutarate (2HG), which contributes to the development of a number of malignancies. Arginine 78-86 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 0-41 27956631-2 2016 In the hematopoietic system, mutations in IDH1 at arginine (R) 132 and in IDH2 at R140 and R172 are commonly observed in acute myeloid leukemia, and elevated 2HG is observed in cells and serum. Arginine 50-58 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 42-46 26147657-1 2015 In recent years, frequent isocitrate dehydrogenase 1/2 (IDH1/IDH2) gene mutations were found in a variety of tumors, which specifically alter arginine residues of catalytic active site in IDH1/IDH2 and confer new enzymatic function of directly catalyzing alpha-ketoglutarate (alpha-KG) to R-2-hydroxyglutarate (2-HG). Arginine 142-150 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 56-60 26147657-1 2015 In recent years, frequent isocitrate dehydrogenase 1/2 (IDH1/IDH2) gene mutations were found in a variety of tumors, which specifically alter arginine residues of catalytic active site in IDH1/IDH2 and confer new enzymatic function of directly catalyzing alpha-ketoglutarate (alpha-KG) to R-2-hydroxyglutarate (2-HG). Arginine 142-150 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 188-192 26198745-9 2015 Deep parallel sequencing of the dedifferentiated component showed a nonsynonymous mutation at exon 4 of IDH1 gene at codon R132 leading to a substitution of arginine, with serine confirming glandular differentiation in dedifferentiated chondrosarcoma. Arginine 157-165 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 104-108 24590270-3 2014 Mutations of IDH1 have been identified at codon 132, with arginine being replaced with histidine in most cases. Arginine 58-66 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 13-17 25787993-2 2015 An example is the identification of arginine missense mutations of isocitrate dehydrogenases-1 and -2 (IDH1/2) in glioma, acute myeloid leukemia (AML), chondrosarcomas, and cholangiocarcinoma. Arginine 36-44 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 103-109 25853107-2 2015 In particular, missense mutations in isocitrate dehydrogenase-1 (IDH1) at arginine 132, mostly substituted into histidine (IDH1-R132H) were observed to frequently occur in glioma patients. Arginine 74-82 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 37-63 25853107-2 2015 In particular, missense mutations in isocitrate dehydrogenase-1 (IDH1) at arginine 132, mostly substituted into histidine (IDH1-R132H) were observed to frequently occur in glioma patients. Arginine 74-82 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 65-69 25853107-2 2015 In particular, missense mutations in isocitrate dehydrogenase-1 (IDH1) at arginine 132, mostly substituted into histidine (IDH1-R132H) were observed to frequently occur in glioma patients. Arginine 74-82 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 123-127 25324168-2 2015 In gliomas, IDH mutations uniformly occur in the functionally critical arginine 132 residue (R132) of IDH1 and arginine 172 residue (R172) of IDH2. Arginine 71-79 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 12-15 25324168-2 2015 In gliomas, IDH mutations uniformly occur in the functionally critical arginine 132 residue (R132) of IDH1 and arginine 172 residue (R172) of IDH2. Arginine 71-79 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 102-106 25324168-2 2015 In gliomas, IDH mutations uniformly occur in the functionally critical arginine 132 residue (R132) of IDH1 and arginine 172 residue (R172) of IDH2. Arginine 111-119 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 12-15 24898068-5 2014 The IDH mutations are remarkably specific to arginine 132 (R132) in IDH1 and arginine 172 (R172) or arginine 140 (R140) in IDH2; IDH1/2 mutations are known to convert alpha-ketoglutarate to oncometabolite R(-)-2-hydroxyglutarate. Arginine 45-53 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 4-7 24898068-5 2014 The IDH mutations are remarkably specific to arginine 132 (R132) in IDH1 and arginine 172 (R172) or arginine 140 (R140) in IDH2; IDH1/2 mutations are known to convert alpha-ketoglutarate to oncometabolite R(-)-2-hydroxyglutarate. Arginine 45-53 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 68-72 24898068-5 2014 The IDH mutations are remarkably specific to arginine 132 (R132) in IDH1 and arginine 172 (R172) or arginine 140 (R140) in IDH2; IDH1/2 mutations are known to convert alpha-ketoglutarate to oncometabolite R(-)-2-hydroxyglutarate. Arginine 77-85 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 4-7 24898068-5 2014 The IDH mutations are remarkably specific to arginine 132 (R132) in IDH1 and arginine 172 (R172) or arginine 140 (R140) in IDH2; IDH1/2 mutations are known to convert alpha-ketoglutarate to oncometabolite R(-)-2-hydroxyglutarate. Arginine 77-85 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 4-7 24626950-4 2014 The present study, showed that forced expression of an IDH1 mutant, of which the 132th amino acid residue arginine is substituted by histidine (IDH1R132H), promoted cell proliferation in cultured cells, while wild-type IDH1 overexpression had no effect on cell proliferation. Arginine 106-114 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 55-59 24626950-4 2014 The present study, showed that forced expression of an IDH1 mutant, of which the 132th amino acid residue arginine is substituted by histidine (IDH1R132H), promoted cell proliferation in cultured cells, while wild-type IDH1 overexpression had no effect on cell proliferation. Arginine 106-114 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 144-148 23267435-2 2012 Almost all described mutations are heterozygous missense mutations affecting a conserved arginine residue in the substrate binding site of IDH1 (R132) or IDH2 (R172). Arginine 89-97 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 139-143 23905201-2 2010 The mutated residue in IDH1 is most commonly arginine 132, which is most often replaced with either histidine or cysteine. Arginine 45-53 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 23-27 23264629-5 2013 Cytosolic IDH1 Arg-132 mutations, although structurally analogous to mutations at mitochondrial IDH2 Arg-172, were only able to elevate intracellular 2HG to comparable levels when an equivalent level of wild-type IDH1 was co-expressed. Arginine 15-18 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 10-14 23264629-5 2013 Cytosolic IDH1 Arg-132 mutations, although structurally analogous to mutations at mitochondrial IDH2 Arg-172, were only able to elevate intracellular 2HG to comparable levels when an equivalent level of wild-type IDH1 was co-expressed. Arginine 15-18 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 213-217 23264629-5 2013 Cytosolic IDH1 Arg-132 mutations, although structurally analogous to mutations at mitochondrial IDH2 Arg-172, were only able to elevate intracellular 2HG to comparable levels when an equivalent level of wild-type IDH1 was co-expressed. Arginine 101-104 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 10-14 23235339-2 2014 The most common IDH1 mutation affects codon 132 and results in the conversion of amino acid residue arginine (R) to histidine (H). Arginine 100-108 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 16-20 21996744-2 2012 To date, mutations in three active site arginine residues, IDH1 R132, IDH2 R172 and IDH2 R140, have been shown to result in the neomorphic production of 2HG. Arginine 40-48 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 59-63 23090985-1 2012 The arginine 132 (R132) mutation of isocitrate dehydrogenase -1 (IDH1(R132)) results in production of 2-hydroxyglutarate (2-HG) and is associated with a better prognosis compared with wild-type (WT) in glioma patients. Arginine 4-12 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 65-69 22396072-1 2012 Isocitrate dehydrogenase 1 (IDH1) mutations, which are early and frequent genetic alterations in astrocytomas, oligodendrogliomas, oligoastrocytomas, and secondary glioblastomas, are specific to arginine 132 (R132). Arginine 195-203 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 0-26 22396072-1 2012 Isocitrate dehydrogenase 1 (IDH1) mutations, which are early and frequent genetic alterations in astrocytomas, oligodendrogliomas, oligoastrocytomas, and secondary glioblastomas, are specific to arginine 132 (R132). Arginine 195-203 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 28-32 22904127-5 2012 We detected 31 (41.9%) heterozygous IDH1 mutations resulting in arginine-to-histidine substitution (R132H;CGT-CAT). Arginine 64-72 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 36-40 22809434-1 2012 BACKGROUND: Mutations at arginine 132 of isocitrate dehydrogenase 1/2 (IDH1/2) have recently been demonstrated to be recurrent gene alterations in acute myeloid leukemia (AML). Arginine 25-33 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 71-77 22238332-2 2012 Arginine 132 (R132) mutations in the enzyme IDH1 result in excess production of the metabolite 2-hydroxyglutarate (2HG), which could be used as a biomarker for this subset of gliomas. Arginine 0-8 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 44-48 21647154-3 2011 The identified IDH1 mutations occurred in codon 132 resulting in replacement of arginine with either cysteine (N=3) or histidine (N=1). Arginine 80-88 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 15-19 21352804-1 2011 Isocitrate dehydrogenase 1 (IDH1) mutations, which are early and frequent genetic alterations in gliomas, are specific to a single codon in the conserved and functionally important Arginine 132 (R132) in IDH1. Arginine 181-189 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 28-32 21352804-1 2011 Isocitrate dehydrogenase 1 (IDH1) mutations, which are early and frequent genetic alterations in gliomas, are specific to a single codon in the conserved and functionally important Arginine 132 (R132) in IDH1. Arginine 181-189 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 204-208 20692206-3 2010 The heterozygous somatic mutations at arginine R132 (IDH1) and at R140 or R172 (IDH2) in the enzyme active site confer a gain of function to the enzymes, which can both produce the metabolite 2-hydroxyglutarate. Arginine 38-46 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 53-57 20513808-5 2010 IDH1 and IDH2 mutations are remarkably specific to codons that encode conserved functionally important arginines in the active site of each enzyme. Arginine 103-112 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 0-4 22442146-3 2012 IDH1 and IDH2 with cancer-associated mutations at the active site arginines were unable to carry out the reductive carboxylation of alphaKG. Arginine 66-75 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 0-4 20142433-2 2010 IDH1/2 mutations are heterozygous, and affect a single arginine residue. Arginine 55-63 isocitrate dehydrogenase (NADP(+)) 1 Homo sapiens 0-6