PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12974624-0 2003 Structure of avian AICAR transformylase with a multisubstrate adduct inhibitor beta-DADF identifies the folate binding site. Folic Acid 104-110 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 19-24 12974624-3 2003 Identification of the location of the AICAR transformylase active site was previously elucidated from the crystal structure of the avian ATIC with bound substrate AICAR; however, due to the absence of any bound folate, the folate binding region of the active site could not be identified. Folic Acid 211-217 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 38-43 12974624-3 2003 Identification of the location of the AICAR transformylase active site was previously elucidated from the crystal structure of the avian ATIC with bound substrate AICAR; however, due to the absence of any bound folate, the folate binding region of the active site could not be identified. Folic Acid 223-229 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 38-43 12974624-3 2003 Identification of the location of the AICAR transformylase active site was previously elucidated from the crystal structure of the avian ATIC with bound substrate AICAR; however, due to the absence of any bound folate, the folate binding region of the active site could not be identified. Folic Acid 223-229 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 137-141 12974624-3 2003 Identification of the location of the AICAR transformylase active site was previously elucidated from the crystal structure of the avian ATIC with bound substrate AICAR; however, due to the absence of any bound folate, the folate binding region of the active site could not be identified. Folic Acid 223-229 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 163-168 12974624-5 2003 Beta-DADF encompasses both the AICAR and folate moieties into a single covalently linked entity, thereby allowing for the characterization of the folate binding pocket of the AICAR transformylase active site. Folic Acid 146-152 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 175-180 12501179-2 2002 The formyl transfer reaction catalyzed by the AICAR Tfase domain is substantially more demanding than that catalyzed by the other folate-dependent enzyme of the purine biosynthesis pathway, GAR transformylase. Folic Acid 130-136 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 46-51 3366769-3 1988 Chemically synthesized monoglutamated or pentaglutamated 10-formyl-H2folate was examined for its interaction with three folate-dependent enzymes: AICAR transformylase, glucinamide ribotide (GAR) transformylase, and thymidylatesynthase. Folic Acid 69-75 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 146-151 9598063-10 1998 Cleland-type kinetic inhibition experiments indicate that the AICARFT reaction is of the ordered, sequential type with the reduced folate cofactor binding first. Folic Acid 131-137 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 62-69 9598063-16 1998 A PurH crystal structure is that of a dimer, with a putative single binding site for the reduced folate cofactor formed using elements from each of the monomer subunits. Folic Acid 97-103 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 2-6 30867454-1 2019 In folate-mediated one-carbon metabolism (FOCM), 5-formyltetrahydrofolate (5fTHF), a one-carbon substituted tetrahydrofolate (THF) vitamer, acts as an intracellular storage form of folate and as an inhibitor of the folate-dependent enzymes phosphoribosylaminoimidazolecarboxamide formyltransferase (AICARFT) and serine hydroxymethyltransferase (SHMT). Folic Acid 3-9 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 299-306 30867454-1 2019 In folate-mediated one-carbon metabolism (FOCM), 5-formyltetrahydrofolate (5fTHF), a one-carbon substituted tetrahydrofolate (THF) vitamer, acts as an intracellular storage form of folate and as an inhibitor of the folate-dependent enzymes phosphoribosylaminoimidazolecarboxamide formyltransferase (AICARFT) and serine hydroxymethyltransferase (SHMT). Folic Acid 67-73 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 299-306 30867454-1 2019 In folate-mediated one-carbon metabolism (FOCM), 5-formyltetrahydrofolate (5fTHF), a one-carbon substituted tetrahydrofolate (THF) vitamer, acts as an intracellular storage form of folate and as an inhibitor of the folate-dependent enzymes phosphoribosylaminoimidazolecarboxamide formyltransferase (AICARFT) and serine hydroxymethyltransferase (SHMT). Folic Acid 67-73 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 299-306 32384607-4 2020 We identified six genes (GART, PFAS, PPAT, PAICS, ATIC, and ADSL) whose blocking results in nearly the same effect in the metabolic network as folate depletion. Folic Acid 143-149 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 50-54 29042184-6 2018 The AICARFT site is capable of independently binding both nucleotide and folate substrates with high affinity however no evidence for positive cooperativity in binding could be detected using the model ligands employed in this study. Folic Acid 73-79 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 4-11 30337562-1 2018 AICARFT is a folate dependent catalytic site within the ATIC gene, part of the purine biosynthetic pathway, a pathway frequently upregulated in cancers. Folic Acid 13-19 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 0-7 30337562-1 2018 AICARFT is a folate dependent catalytic site within the ATIC gene, part of the purine biosynthetic pathway, a pathway frequently upregulated in cancers. Folic Acid 13-19 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 56-60 22554803-1 2012 5-Aminoimidazole-4-carboxamide riboside (AICAR), an agent with diverse pharmacological properties, augments transport of folates and antifolates. Folic Acid 121-128 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 41-46 22554803-3 2012 Exposure of HeLa cells to AICAR resulted in augmentation of methotrexate, 5-formyltetrahydrofolate, and 5-methyltetrahydrofolate initial rates and net uptake in cells that express the reduced folate carrier (RFC). Folic Acid 92-98 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 26-31 22554803-6 2012 When ZMP formation was blocked with 5-iodotubercidin, an inhibitor of adenosine kinase, folate transport stimulation by AICAR was absent. Folic Acid 88-94 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 120-125 22554803-7 2012 When cells first accumulated ZMP and were then exposed to 5-iodotubercidin or AICAR-free buffer, the ZMP level markedly decreased and folate transport stimulation was abolished. Folic Acid 134-140 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Homo sapiens 78-83