PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7651366-1 1995 The metabolism of 5,10-dideazatetrahydrofolate (DDATHF [lometrexol]) to polyglutamate derivatives by folylpoly-gamma-glutamate synthetase (FPGS) plays a central role in the activity of this compound as an antineoplastic agent. Polyglutamic Acid 72-85 folylpolyglutamate synthase Homo sapiens 101-137 9306433-4 1997 The ratio between GGH and FPGS activities was better at predicting the amount of polyglutamate accumulated in the 24-h [3H]MTX assay compared to the determination of either activity alone. Polyglutamic Acid 81-94 folylpolyglutamate synthase Homo sapiens 26-30 9306433-5 1997 The linear regression curve relating the relative levels of long-chain polyglutamates/total polyglutamates with the ratio of GGH/FPGS showed an r value of 0.81 (P < 0.001). Polyglutamic Acid 71-85 folylpolyglutamate synthase Homo sapiens 129-133 9306433-5 1997 The linear regression curve relating the relative levels of long-chain polyglutamates/total polyglutamates with the ratio of GGH/FPGS showed an r value of 0.81 (P < 0.001). Polyglutamic Acid 92-106 folylpolyglutamate synthase Homo sapiens 129-133 7651366-1 1995 The metabolism of 5,10-dideazatetrahydrofolate (DDATHF [lometrexol]) to polyglutamate derivatives by folylpoly-gamma-glutamate synthetase (FPGS) plays a central role in the activity of this compound as an antineoplastic agent. Polyglutamic Acid 72-85 folylpolyglutamate synthase Homo sapiens 139-143 1435744-1 1992 Previous studies have documented the metabolism of a broad range of folate antimetabolites to polyglutamate derivatives by the enzyme folylpoly-gamma-glutamate synthetase (FPGS). Polyglutamic Acid 94-107 folylpolyglutamate synthase Homo sapiens 134-170 7517720-1 1994 Folylpolyglutamate synthetase (FPGS) is responsible for the metabolism of natural folates and a broad range of folate antagonists to polyglutamate derivatives. Polyglutamic Acid 5-18 folylpolyglutamate synthase Homo sapiens 31-35 8144562-1 1994 Chinese hamster ovary (CHO) cells expressing human and Escherichia coli folylpolyglutamate synthetase (FPGS) activities were used as models to study factors regulating the cytotoxicity and metabolism of 5-deazaacyclotetrahydrofolate (DATHF), an anti-purine agent that requires conversion to polyglutamate forms to be a potent inhibitor of its target enzymes. Polyglutamic Acid 77-90 folylpolyglutamate synthase Homo sapiens 103-107 8408019-5 1993 Essentially all transported folate was metabolized to retained polyglutamate derivatives, the chain length of which varied with the level of FPGS activity. Polyglutamic Acid 63-76 folylpolyglutamate synthase Homo sapiens 141-145 8408021-4 1993 CHO cells expressing human FPGS metabolized MTX to polyglutamates characteristic of human cells. Polyglutamic Acid 51-65 folylpolyglutamate synthase Homo sapiens 27-31 8408021-5 1993 Cellular MTX accumulation and metabolism to polyglutamates were dependent on the level of FPGS activity and were unaffected by putative gamma-glutamyl hydrolase inhibitors. Polyglutamic Acid 44-58 folylpolyglutamate synthase Homo sapiens 90-94 1435744-1 1992 Previous studies have documented the metabolism of a broad range of folate antimetabolites to polyglutamate derivatives by the enzyme folylpoly-gamma-glutamate synthetase (FPGS). Polyglutamic Acid 94-107 folylpolyglutamate synthase Homo sapiens 172-176 3431589-7 1987 The ability of compounds to inhibit both DHFR and FPGS makes it possible in principle for such compounds to kill cells via a "self-potentiation" mechanism in which inhibition of tetrahydrofolate synthesis is complemented by interference with the subsequent conversion of tetrahydrofolates to their polyglutamate conjugates. Polyglutamic Acid 298-311 folylpolyglutamate synthase Homo sapiens 50-54 3619447-11 1987 Comparison of MTX with its higher polyglutamates (MTX-Glu2 to MTX-Glu6) as FPGS substrates indicated a significant decrease in Vmax values with increasing glutamate chain length which was partially compensated for by a corresponding decrease in Km. Polyglutamic Acid 34-48 folylpolyglutamate synthase Homo sapiens 75-79 23949282-2 2013 This drug is converted intracellularly into polyglutamate derivates by the enzyme folylpolyglutamate synthase (FPGS). Polyglutamic Acid 44-57 folylpolyglutamate synthase Homo sapiens 82-109 3812977-1 1986 The enzyme folylpolyglutamate synthetase (FPGS) catalyzes the conversion of folate (pteroylmonoglutamate) to the polyglutamate forms (pteroylpolyglutamates) that are required for folate retention by mammalian cells. Polyglutamic Acid 16-29 folylpolyglutamate synthase Homo sapiens 42-46 3466358-8 1986 Transformants with FPGS activity that showed a human enzyme preference for dATP also had folate polyglutamate chain lengths characteristic of the human enzyme. Polyglutamic Acid 96-109 folylpolyglutamate synthase Homo sapiens 19-23 3873989-15 1985 In contrast to the formation of long-chain polyglutamates observed when tetrahydrofolate or folinic acid was the substrate, beef liver FPGS, under our reaction conditions, cannot catalyze the formation from MTX monoglutamate of polyglutamates longer than the triglutamate. Polyglutamic Acid 43-57 folylpolyglutamate synthase Homo sapiens 135-139 27620954-10 2016 FPGS catalyzes the addition of a long polyglutamate chain to folates and antifolates, hence rendering them polyanions which are efficiently retained in the cell and are now bound with enhanced affinity by various folate-dependent enzymes. Polyglutamic Acid 38-51 folylpolyglutamate synthase Homo sapiens 0-4 23949282-2 2013 This drug is converted intracellularly into polyglutamate derivates by the enzyme folylpolyglutamate synthase (FPGS). Polyglutamic Acid 44-57 folylpolyglutamate synthase Homo sapiens 111-115 16707018-1 2006 BACKGROUND: Expression of folylpoly-gamma-glutamate synthetase (FPGS) gene is two- to three-fold higher in B-precursor ALL (Bp- ALL) than in T-lineage ALL (T-ALL) and correlates with intracellular accumulation of methotrexate (MTX) polyglutamates and lymphoblast sensitivity to MTX. Polyglutamic Acid 232-246 folylpolyglutamate synthase Homo sapiens 26-62 18025275-1 2007 Folylpolyglutamyl synthase (FPGS) converts intracellular folates and antifolates to polyglutamates. Polyglutamic Acid 84-98 folylpolyglutamate synthase Homo sapiens 0-26 18025275-1 2007 Folylpolyglutamyl synthase (FPGS) converts intracellular folates and antifolates to polyglutamates. Polyglutamic Acid 84-98 folylpolyglutamate synthase Homo sapiens 28-32 16707018-1 2006 BACKGROUND: Expression of folylpoly-gamma-glutamate synthetase (FPGS) gene is two- to three-fold higher in B-precursor ALL (Bp- ALL) than in T-lineage ALL (T-ALL) and correlates with intracellular accumulation of methotrexate (MTX) polyglutamates and lymphoblast sensitivity to MTX. Polyglutamic Acid 232-246 folylpolyglutamate synthase Homo sapiens 64-68 10626793-1 1999 Folates and folate antimetabolites are metabolically trapped in mammalian cells as polyglutamates, a process catalyzed by folylpoly-gamma-glutamate synthetase (FPGS). Polyglutamic Acid 83-97 folylpolyglutamate synthase Homo sapiens 122-158 15542523-1 2004 BACKGROUND: Folylpoly-gamma-glutamate synthetase (FPGS) converts intracellular folates and antifolates (for example, methotrexate (MTX)) to polyglutamates. Polyglutamic Acid 140-154 folylpolyglutamate synthase Homo sapiens 12-48 15542523-1 2004 BACKGROUND: Folylpoly-gamma-glutamate synthetase (FPGS) converts intracellular folates and antifolates (for example, methotrexate (MTX)) to polyglutamates. Polyglutamic Acid 140-154 folylpolyglutamate synthase Homo sapiens 50-54 10626793-1 1999 Folates and folate antimetabolites are metabolically trapped in mammalian cells as polyglutamates, a process catalyzed by folylpoly-gamma-glutamate synthetase (FPGS). Polyglutamic Acid 83-97 folylpolyglutamate synthase Homo sapiens 160-164 10507318-7 1999 These results indicate that FPGS mRNA expression may predict cellular ability to produce polyglutamate metabolites of antifolate drugs in the sensitive cells, but does not necessarily reflect FPGS function at the enzyme level in the antifolate-resistant tumor cells. Polyglutamic Acid 89-102 folylpolyglutamate synthase Homo sapiens 28-32 10413425-2 1999 These drugs are converted intracellularly into polyglutamate derivatives by the enzyme folylpolyglutamyl synthetase (FPGS). Polyglutamic Acid 47-60 folylpolyglutamate synthase Homo sapiens 87-115 10413425-2 1999 These drugs are converted intracellularly into polyglutamate derivatives by the enzyme folylpolyglutamyl synthetase (FPGS). Polyglutamic Acid 47-60 folylpolyglutamate synthase Homo sapiens 117-121