PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2633609-1 1989 Growth of rat hepatoma cells in subtoxic concentrations of the DHFR inhibitor metoprine caused a marked time and concentration dependent reduction in cellular folates. Folic Acid 159-166 dihydrofolate reductase Rattus norvegicus 63-67 3676170-11 1986 The hepatic activity of another key folate-metabolizing enzyme, dihydrofolate reductase (EC 1.5.1.3), was not diminished by riboflavin deficiency in the present study. Folic Acid 36-42 dihydrofolate reductase Rattus norvegicus 64-87 3630970-0 1987 Competitive inhibition of folate absorption by dihydrofolate reductase inhibitors, trimethoprim and pyrimethamine. Folic Acid 26-32 dihydrofolate reductase Rattus norvegicus 47-70 3630970-5 1987 [3H] folic acid absorption from jejunal loops was determined 3-16 h after IV administration of methotrexate; this treatment abolished DHFR activity in the small intestine. Folic Acid 5-15 dihydrofolate reductase Rattus norvegicus 134-138 29390203-9 2019 However, all of the above and hemodynamic index (RI) of femoral artery were resumed via restoration of DHFR protein expression by folic acid treatment or DHFR transfection. Folic Acid 130-140 dihydrofolate reductase Rattus norvegicus 103-107 761221-5 1979 The presence of DHFR in neoplasms of central nervous system origin is relevant to the development of folate antagonists which, unlike methotrexate, can readily cross the blood-brain barrier. Folic Acid 101-107 dihydrofolate reductase Rattus norvegicus 16-20 9701044-1 1997 A stretch of about 150 amino acids located between the heme and the calmodulin recognition sequence of nitric oxide synthase (NOS) has been strongly conserved within isoforms and was proposed to participate in pteridine binding because of sequence similarities to the folate binding site of dihydrofolate reductase (DHFR). Folic Acid 268-274 dihydrofolate reductase Rattus norvegicus 291-314 9701044-1 1997 A stretch of about 150 amino acids located between the heme and the calmodulin recognition sequence of nitric oxide synthase (NOS) has been strongly conserved within isoforms and was proposed to participate in pteridine binding because of sequence similarities to the folate binding site of dihydrofolate reductase (DHFR). Folic Acid 268-274 dihydrofolate reductase Rattus norvegicus 316-320