PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
23904512-2	2013	Folates are generally taken up into cells by specific transporters, mainly the reduced folate carrier RFC1 (SLC19A1 protein) and the high-affinity folate receptors FOLR1 and FOLR2.	Folic Acid	0-7	replication factor C (activator 1) 1	Mus musculus	102-106
23904512-2	2013	Folates are generally taken up into cells by specific transporters, mainly the reduced folate carrier RFC1 (SLC19A1 protein) and the high-affinity folate receptors FOLR1 and FOLR2.	Folic Acid	87-93	replication factor C (activator 1) 1	Mus musculus	102-106
23904512-7	2013	In COCs, transport of MTX and the reduced folate leucovorin was inhibited by the anion transport inhibitor SITS that blocks RFC1 but was insensitive to dynasore, a specific dynamin inhibitor that instead inhibits folate receptor-receptor mediated endocytosis, whereas the opposite was found in 2-cell embryos and blastocysts.	Methotrexate	22-25	replication factor C (activator 1) 1	Mus musculus	124-128
23904512-7	2013	In COCs, transport of MTX and the reduced folate leucovorin was inhibited by the anion transport inhibitor SITS that blocks RFC1 but was insensitive to dynasore, a specific dynamin inhibitor that instead inhibits folate receptor-receptor mediated endocytosis, whereas the opposite was found in 2-cell embryos and blastocysts.	Leucovorin	49-59	replication factor C (activator 1) 1	Mus musculus	124-128
23904512-8	2013	The inhibitor profile and transport properties of MTX and leucovorin in COCs correspond to established transport characteristics of RFC1 (SLC19A1), whereas those in 2-cell embryos and blastocysts correspond with those of FOLR1, consistent with the mRNA expression patterns.	Methotrexate	50-53	replication factor C (activator 1) 1	Mus musculus	132-136
23904512-8	2013	The inhibitor profile and transport properties of MTX and leucovorin in COCs correspond to established transport characteristics of RFC1 (SLC19A1), whereas those in 2-cell embryos and blastocysts correspond with those of FOLR1, consistent with the mRNA expression patterns.	Leucovorin	58-68	replication factor C (activator 1) 1	Mus musculus	132-136
11997266-1	2002	Although the reduced folate carrier RFC1 and the thiamine transporters THTR-1 and THTR-2 share approximately 40% of their identity in protein sequence, RFC1 does not transport thiamine and THTR-1 and THTR-2 do not transport folates.	Folic Acid	21-27	replication factor C (activator 1) 1	Mus musculus	36-40
18926688-4	2009	Compound heterozygous mice (Folbp1(+/-); RFC1(+/-)) fed an adequate folate diet exhibited a reduction in plasma folate concentrations compared to heterozygous (Folbp1(+/-)) and littermate wild-type mice (P<.05).	Folic Acid	112-118	replication factor C (activator 1) 1	Mus musculus	41-45
18383508-2	2008	In this study, embryonic/fetal development is characterized in an RFC1 knockout mouse model in which pregnant dams receive different levels of folate supplementation.	Folic Acid	143-149	replication factor C (activator 1) 1	Mus musculus	66-70
18383508-7	2008	Maternal folate supplementation with 50 mg/kg/day results in survival of 22% of RFC1 mutants to E18.5, but they develop with multiple malformations of the eyelids, lungs, heart, and skin.	Folic Acid	9-15	replication factor C (activator 1) 1	Mus musculus	80-84
18383508-8	2008	CONCLUSIONS: High doses of daily maternal folate supplementation during embryonic/fetal development are necessary for early postimplantation embryonic viability of RFC1 nullizygous embryos, and play a critical role in chorioallantoic fusion, erythropoiesis, and proper development of the neural tube, limbs, lungs, heart, and skin.	Folic Acid	42-48	replication factor C (activator 1) 1	Mus musculus	164-168
16963246-3	2007	Apc(min/+) mice with heterozygous knockout of the gene for reduced folate carrier 1 (Rfc1(+/-)) developed significantly fewer adenomas compared to Rfc1(+/+)Apc(min/+) mice [30.3+/-4.6 vs. 60.4+/-9.4 on a control diet (CD) and 42.6+/-4.4 vs. 55.8+/-7.6 on a folate-deficient diet, respectively].	Cadmium	218-220	replication factor C (activator 1) 1	Mus musculus	85-89
16963246-3	2007	Apc(min/+) mice with heterozygous knockout of the gene for reduced folate carrier 1 (Rfc1(+/-)) developed significantly fewer adenomas compared to Rfc1(+/+)Apc(min/+) mice [30.3+/-4.6 vs. 60.4+/-9.4 on a control diet (CD) and 42.6+/-4.4 vs. 55.8+/-7.6 on a folate-deficient diet, respectively].	Folic Acid	67-73	replication factor C (activator 1) 1	Mus musculus	85-89
11997266-1	2002	Although the reduced folate carrier RFC1 and the thiamine transporters THTR-1 and THTR-2 share approximately 40% of their identity in protein sequence, RFC1 does not transport thiamine and THTR-1 and THTR-2 do not transport folates.	Folic Acid	224-231	replication factor C (activator 1) 1	Mus musculus	36-40
11997266-1	2002	Although the reduced folate carrier RFC1 and the thiamine transporters THTR-1 and THTR-2 share approximately 40% of their identity in protein sequence, RFC1 does not transport thiamine and THTR-1 and THTR-2 do not transport folates.	Folic Acid	224-231	replication factor C (activator 1) 1	Mus musculus	152-156
11997266-2	2002	In the present study, we demonstrate that transport of thiamine monophosphate (TMP), an important thiamine metabolite present in plasma and cerebrospinal fluid, is mediated by RFC1 in L1210 murine leukemia cells.	Thiamine Monophosphate	55-77	replication factor C (activator 1) 1	Mus musculus	176-180
11997266-2	2002	In the present study, we demonstrate that transport of thiamine monophosphate (TMP), an important thiamine metabolite present in plasma and cerebrospinal fluid, is mediated by RFC1 in L1210 murine leukemia cells.	Thiamine Monophosphate	79-82	replication factor C (activator 1) 1	Mus musculus	176-180
11997266-2	2002	In the present study, we demonstrate that transport of thiamine monophosphate (TMP), an important thiamine metabolite present in plasma and cerebrospinal fluid, is mediated by RFC1 in L1210 murine leukemia cells.	Thiamine	55-63	replication factor C (activator 1) 1	Mus musculus	176-180
11997266-3	2002	Transport of TMP was augmented by a factor of five in cells (R16) that overexpress RFC1 and was markedly inhibited by methotrexate, an RFC1 substrate, but not by thiamine.	Thiamine Monophosphate	13-16	replication factor C (activator 1) 1	Mus musculus	83-87
11997266-3	2002	Transport of TMP was augmented by a factor of five in cells (R16) that overexpress RFC1 and was markedly inhibited by methotrexate, an RFC1 substrate, but not by thiamine.	Thiamine Monophosphate	13-16	replication factor C (activator 1) 1	Mus musculus	135-139
11997266-3	2002	Transport of TMP was augmented by a factor of five in cells (R16) that overexpress RFC1 and was markedly inhibited by methotrexate, an RFC1 substrate, but not by thiamine.	Methotrexate	118-130	replication factor C (activator 1) 1	Mus musculus	83-87
11997266-3	2002	Transport of TMP was augmented by a factor of five in cells (R16) that overexpress RFC1 and was markedly inhibited by methotrexate, an RFC1 substrate, but not by thiamine.	Methotrexate	118-130	replication factor C (activator 1) 1	Mus musculus	135-139
11997266-4	2002	At a near-physiological concentration (50 nM), TMP influx mediated by RFC1 in wild-type L1210 cells was approximately 50% of thiamine influx mediated by thiamine transporter(s).	Thiamine Monophosphate	47-50	replication factor C (activator 1) 1	Mus musculus	70-74
11997266-4	2002	At a near-physiological concentration (50 nM), TMP influx mediated by RFC1 in wild-type L1210 cells was approximately 50% of thiamine influx mediated by thiamine transporter(s).	Thiamine	125-133	replication factor C (activator 1) 1	Mus musculus	70-74
11997266-6	2002	These data suggest that RFC1 may be one of the alternative transport routes available for TMP in some tissues when THTR-1 is mutated in the autosomal recessive disorder thiamine-responsive megaloblastic anemia.	Thiamine Monophosphate	90-93	replication factor C (activator 1) 1	Mus musculus	24-28
11997266-6	2002	These data suggest that RFC1 may be one of the alternative transport routes available for TMP in some tissues when THTR-1 is mutated in the autosomal recessive disorder thiamine-responsive megaloblastic anemia.	Thiamine	169-177	replication factor C (activator 1) 1	Mus musculus	24-28
11427193-9	2001	These data provide insights into the role that RFC1 plays in folate delivery in a variety of tissues.	Folic Acid	61-67	replication factor C (activator 1) 1	Mus musculus	47-51
12007575-1	2002	The reduced folate carrier (RFC1), a member of the major facilitative superfamily, generates uphill transport of folates into cells through an exchange mechanism with intracellular organic anions.	Folic Acid	12-18	replication factor C (activator 1) 1	Mus musculus	28-32
12007575-1	2002	The reduced folate carrier (RFC1), a member of the major facilitative superfamily, generates uphill transport of folates into cells through an exchange mechanism with intracellular organic anions.	Folic Acid	113-120	replication factor C (activator 1) 1	Mus musculus	28-32
11427193-10	2001	In particular, the localization of carrier may elucidate the role of RFC1 in the vectorial transport of folates across epithelia.	Folic Acid	104-111	replication factor C (activator 1) 1	Mus musculus	69-73
11038362-1	2001	The thiamin transporter encoded by SLC19A2 and the reduced folate carrier (RFC1) share 40% homology at the protein level, but the thiamin transporter does not mediate transport of folates.	Folic Acid	59-65	replication factor C (activator 1) 1	Mus musculus	75-79
11306683-3	2001	This article explores the role of these residues in transport function by the development of cell lines in which arginines and lysines in RFC1 were replaced with leucine by site-directed mutagenesis.	Arginine	113-122	replication factor C (activator 1) 1	Mus musculus	138-142
11306683-3	2001	This article explores the role of these residues in transport function by the development of cell lines in which arginines and lysines in RFC1 were replaced with leucine by site-directed mutagenesis.	Lysine	127-134	replication factor C (activator 1) 1	Mus musculus	138-142
11038362-3	2001	However, high level RFC1 expression substantially reduced accumulation of the active thiamin coenzyme, thiamin pyrophosphate (TPP).	Thiamine	85-92	replication factor C (activator 1) 1	Mus musculus	20-24
11038362-3	2001	However, high level RFC1 expression substantially reduced accumulation of the active thiamin coenzyme, thiamin pyrophosphate (TPP).	Thiamine Pyrophosphate	103-124	replication factor C (activator 1) 1	Mus musculus	20-24
11038362-3	2001	However, high level RFC1 expression substantially reduced accumulation of the active thiamin coenzyme, thiamin pyrophosphate (TPP).	Thiamine Pyrophosphate	126-129	replication factor C (activator 1) 1	Mus musculus	20-24
11038362-4	2001	This decreased level of TPP, synthesized intracellularly from imported thiamin, resulted from RFC1-mediated efflux of TPP.	Thiamine Pyrophosphate	24-27	replication factor C (activator 1) 1	Mus musculus	94-98
11038362-4	2001	This decreased level of TPP, synthesized intracellularly from imported thiamin, resulted from RFC1-mediated efflux of TPP.	Thiamine	71-78	replication factor C (activator 1) 1	Mus musculus	94-98
11038362-4	2001	This decreased level of TPP, synthesized intracellularly from imported thiamin, resulted from RFC1-mediated efflux of TPP.	Thiamine Pyrophosphate	118-121	replication factor C (activator 1) 1	Mus musculus	94-98
11038362-6	2001	(i) Efflux of intracellular TPP was increased in cells with high expression of RFC1.	Thiamine Pyrophosphate	28-31	replication factor C (activator 1) 1	Mus musculus	79-83
11038362-10	2001	(v) There was an inverse correlation between thiamin accumulation and RFC1 activity in cells grown at a physiological concentration of thiamin.	Thiamine	45-52	replication factor C (activator 1) 1	Mus musculus	70-74
11038362-10	2001	(v) There was an inverse correlation between thiamin accumulation and RFC1 activity in cells grown at a physiological concentration of thiamin.	Thiamine	135-142	replication factor C (activator 1) 1	Mus musculus	70-74
11038362-11	2001	The modulation of thiamin accumulation by RFC1 in murine leukemia cells suggests that this carrier may play a role in thiamin homeostasis and could serve as a modifying factor in thiamin nutritional deficiency as well as when the high affinity thiamin transporter is mutated.	Thiamine	18-25	replication factor C (activator 1) 1	Mus musculus	42-46
11038362-11	2001	The modulation of thiamin accumulation by RFC1 in murine leukemia cells suggests that this carrier may play a role in thiamin homeostasis and could serve as a modifying factor in thiamin nutritional deficiency as well as when the high affinity thiamin transporter is mutated.	Thiamine	118-125	replication factor C (activator 1) 1	Mus musculus	42-46
11038362-11	2001	The modulation of thiamin accumulation by RFC1 in murine leukemia cells suggests that this carrier may play a role in thiamin homeostasis and could serve as a modifying factor in thiamin nutritional deficiency as well as when the high affinity thiamin transporter is mutated.	Thiamine	118-125	replication factor C (activator 1) 1	Mus musculus	42-46
10535753-1	1999	A phenylalanine substitution for serine in the reduced folate carrier at residue 309 (RFC1-S309F) was identified in a methotrexate (MTX)-resistant cell line selected with 5-formyltetrahydrofolate (5-CHO-THF) as the sole folate source.	Folic Acid	189-195	replication factor C (activator 1) 1	Mus musculus	86-90
10955817-2	2000	A valine-to-methionine substitution at amino acid 104 in the reduced folate carrier (RFC1) explains this disparity in drug resistance.	Folic Acid	69-75	replication factor C (activator 1) 1	Mus musculus	85-89
10955817-3	2000	Transfection of the V104M cDNA into an RFC1-deficient cell line markedly increased DDATHF influx (32x) but only modestly increased influx of MTX and 5-formyltetrahydrofolate (4- and 6-fold, respectively).	lometrexol	83-89	replication factor C (activator 1) 1	Mus musculus	39-43
10955817-10	2000	Hence, resistance to one antifolate, in this case MTX, because of a loss of RFC1 transport activity need not exclude the subsequent utility of another antifolate that uses the same carrier.	Methotrexate	50-53	replication factor C (activator 1) 1	Mus musculus	76-80
10825425-1	2000	The reduced folate carrier (RFC1) is a major transporter for both natural reduced folates and antifolate chemotherapeutics.	Folic Acid	12-18	replication factor C (activator 1) 1	Mus musculus	28-32
10825425-1	2000	The reduced folate carrier (RFC1) is a major transporter for both natural reduced folates and antifolate chemotherapeutics.	Folic Acid	82-89	replication factor C (activator 1) 1	Mus musculus	28-32
10535753-1	1999	A phenylalanine substitution for serine in the reduced folate carrier at residue 309 (RFC1-S309F) was identified in a methotrexate (MTX)-resistant cell line selected with 5-formyltetrahydrofolate (5-CHO-THF) as the sole folate source.	Phenylalanine	2-15	replication factor C (activator 1) 1	Mus musculus	86-90
10535753-4	1999	Influx of 5-CH3-THF and 5-CHO-THF mediated by RFC1-S309F was 20- and 7-fold greater than that of MTX, respectively.	Methotrexate	97-100	replication factor C (activator 1) 1	Mus musculus	46-50
10535753-1	1999	A phenylalanine substitution for serine in the reduced folate carrier at residue 309 (RFC1-S309F) was identified in a methotrexate (MTX)-resistant cell line selected with 5-formyltetrahydrofolate (5-CHO-THF) as the sole folate source.	Serine	33-39	replication factor C (activator 1) 1	Mus musculus	86-90
10535753-1	1999	A phenylalanine substitution for serine in the reduced folate carrier at residue 309 (RFC1-S309F) was identified in a methotrexate (MTX)-resistant cell line selected with 5-formyltetrahydrofolate (5-CHO-THF) as the sole folate source.	Folic Acid	55-61	replication factor C (activator 1) 1	Mus musculus	86-90
10535753-9	1999	This study represents another example of a single mutation in RFC1 that markedly impairs MTX influx but partially preserves transport of reduced folates when cells are selected with 5-CHO-THF as the available folate substrate.	Methotrexate	89-92	replication factor C (activator 1) 1	Mus musculus	62-66
10535753-1	1999	A phenylalanine substitution for serine in the reduced folate carrier at residue 309 (RFC1-S309F) was identified in a methotrexate (MTX)-resistant cell line selected with 5-formyltetrahydrofolate (5-CHO-THF) as the sole folate source.	Methotrexate	118-130	replication factor C (activator 1) 1	Mus musculus	86-90
10535753-9	1999	This study represents another example of a single mutation in RFC1 that markedly impairs MTX influx but partially preserves transport of reduced folates when cells are selected with 5-CHO-THF as the available folate substrate.	Folic Acid	145-152	replication factor C (activator 1) 1	Mus musculus	62-66
10535753-1	1999	A phenylalanine substitution for serine in the reduced folate carrier at residue 309 (RFC1-S309F) was identified in a methotrexate (MTX)-resistant cell line selected with 5-formyltetrahydrofolate (5-CHO-THF) as the sole folate source.	Methotrexate	132-135	replication factor C (activator 1) 1	Mus musculus	86-90
10535753-9	1999	This study represents another example of a single mutation in RFC1 that markedly impairs MTX influx but partially preserves transport of reduced folates when cells are selected with 5-CHO-THF as the available folate substrate.	Folic Acid	145-151	replication factor C (activator 1) 1	Mus musculus	62-66
10535753-1	1999	A phenylalanine substitution for serine in the reduced folate carrier at residue 309 (RFC1-S309F) was identified in a methotrexate (MTX)-resistant cell line selected with 5-formyltetrahydrofolate (5-CHO-THF) as the sole folate source.	Leucovorin	171-195	replication factor C (activator 1) 1	Mus musculus	86-90
10535753-10	1999	The data indicate that residues in the predicted eighth transmembrane domain of RFC1 can play an important role in the selectivity of folate binding and the mobility of the carrier-substrate complex.	Folic Acid	134-140	replication factor C (activator 1) 1	Mus musculus	80-84
10385685-1	1999	Chemical mutagenesis with N-methyl-N-nitrosourea was employed to study the pattern of mutations in the reduced folate carrier (RFC1) that results in transport-related methotrexate resistance and to identify amino acid residues that are critical to carrier structure and/or function.	Methylnitrosourea	26-48	replication factor C (activator 1) 1	Mus musculus	127-131
10385685-1	1999	Chemical mutagenesis with N-methyl-N-nitrosourea was employed to study the pattern of mutations in the reduced folate carrier (RFC1) that results in transport-related methotrexate resistance and to identify amino acid residues that are critical to carrier structure and/or function.	Folic Acid	111-117	replication factor C (activator 1) 1	Mus musculus	127-131
10385685-1	1999	Chemical mutagenesis with N-methyl-N-nitrosourea was employed to study the pattern of mutations in the reduced folate carrier (RFC1) that results in transport-related methotrexate resistance and to identify amino acid residues that are critical to carrier structure and/or function.	Methotrexate	167-179	replication factor C (activator 1) 1	Mus musculus	127-131
9689927-12	1998	These results document the amplification at the site of a putative HSR in an L1210 cell variant of the RFC-1 gene regulating expression of the one-carbon, reduced folate transporter.	Carbon	147-153	replication factor C (activator 1) 1	Mus musculus	103-108
9634005-7	1998	This is different from what was reported when mouse RFC1 was transfected into murine leukemia cells, resulting in large, more symmetrical increases in the MTX bidirectional transport kinetics with a much smaller change in steady-state levels.	Methotrexate	155-158	replication factor C (activator 1) 1	Mus musculus	52-56
9261128-0	1997	Impact of overexpression of the reduced folate carrier (RFC1), an anion exchanger, on concentrative transport in murine L1210 leukemia cells.	Folic Acid	40-46	replication factor C (activator 1) 1	Mus musculus	56-60
9525881-9	1998	The functional expression of the mutated RFC1 reduced the growth requirement for 5-CHO-THF by a factor of 30, compared with only a 3-fold decrease in the MTX IC50.	Methotrexate	154-157	replication factor C (activator 1) 1	Mus musculus	41-45
9525881-10	1998	This represents the first reported RFC1 mutation that confers resistance to MTX due to a markedly impaired influx with relative conservation of reduced folate transport.	Methotrexate	76-79	replication factor C (activator 1) 1	Mus musculus	35-39
9525881-10	1998	This represents the first reported RFC1 mutation that confers resistance to MTX due to a markedly impaired influx with relative conservation of reduced folate transport.	Folic Acid	152-158	replication factor C (activator 1) 1	Mus musculus	35-39
9446553-0	1998	A single amino acid difference within the folate transporter encoded by the murine RFC-1 gene selectively alters its interaction with folate analogues.	Folic Acid	42-48	replication factor C (activator 1) 1	Mus musculus	83-88
9446553-11	1998	In this case, the higher Km for MTX influx associated with S180 cells was duplicated only in the S180 RFC-1 transfectants.	Methotrexate	32-35	replication factor C (activator 1) 1	Mus musculus	102-107
9446553-12	1998	These results appear to document the first example of a nucleotide alteration within the RFC-1 gene, which influences the interaction of MTX with the encoded plasma membrane transporter.	Methotrexate	137-140	replication factor C (activator 1) 1	Mus musculus	89-94
9261128-1	1997	Transport of reduced folates in murine leukemia cells is mediated by the bidirectional reduced folate carrier (RFC1) and independent unidirectional exit pumps.	Folic Acid	21-28	replication factor C (activator 1) 1	Mus musculus	111-115
9261128-1	1997	Transport of reduced folates in murine leukemia cells is mediated by the bidirectional reduced folate carrier (RFC1) and independent unidirectional exit pumps.	Folic Acid	21-27	replication factor C (activator 1) 1	Mus musculus	111-115
9261128-3	1997	This paper defines the role of high level carrier expression, through transfection with RFC1 cDNA, on concentrative transport of the folate analog, methotrexate (MTX) in murine L1210 leukemia cells.	Folic Acid	133-139	replication factor C (activator 1) 1	Mus musculus	88-92
9261128-3	1997	This paper defines the role of high level carrier expression, through transfection with RFC1 cDNA, on concentrative transport of the folate analog, methotrexate (MTX) in murine L1210 leukemia cells.	Methotrexate	148-160	replication factor C (activator 1) 1	Mus musculus	88-92
9261128-3	1997	This paper defines the role of high level carrier expression, through transfection with RFC1 cDNA, on concentrative transport of the folate analog, methotrexate (MTX) in murine L1210 leukemia cells.	Methotrexate	162-165	replication factor C (activator 1) 1	Mus musculus	88-92
9261128-10	1997	The data indicate that RFC1 produces a large and near symmetrical increase in the bidirectional fluxes of MTX resulting in only a small increase in the transmembrane chemical gradient at low extracellular folate levels.	Methotrexate	106-109	replication factor C (activator 1) 1	Mus musculus	23-27
9261128-10	1997	The data indicate that RFC1 produces a large and near symmetrical increase in the bidirectional fluxes of MTX resulting in only a small increase in the transmembrane chemical gradient at low extracellular folate levels.	Folic Acid	205-211	replication factor C (activator 1) 1	Mus musculus	23-27
9111015-0	1997	RFC-1 gene expression regulates folate absorption in mouse small intestine.	Folic Acid	32-38	replication factor C (activator 1) 1	Mus musculus	0-5
9111015-6	1997	The increase in pH-dependent influx during maturation was associated with an increase in RFC-1 gene expression in the form of a 2.5-kilobase RNA transcript and 58-kDa brush-border membrane protein detected by folate-based affinity labeling and with anti-mouse RFC-1 peptide antibodies.	Folic Acid	209-215	replication factor C (activator 1) 1	Mus musculus	89-94
9111015-8	1997	The treatment of mature absorptive cells with either the affinity label or the anti-RFC-1 peptide antibodies inhibited influx of l, L-[3H]-5-CH3-H4folate in a concentration-dependent manner.	l, l-[3h]-5-ch3-h4folate	129-153	replication factor C (activator 1) 1	Mus musculus	84-89
9111015-9	1997	These results strongly suggest that pH-dependent folate absorption in this tissue is regulated by RFC-1 gene expression.	Folic Acid	49-55	replication factor C (activator 1) 1	Mus musculus	98-103
7659092-3	1995	We report here the cloning of 3T3-L1 adipocyte cDNA encoding a 150 kilodalton protein designated Differentiation Specific Element Binding Protein (DSEB) that exhibits sequence-specific binding to a DSE oligonucleotide.	Oligonucleotides	202-217	replication factor C (activator 1) 1	Mus musculus	97-145
8664315-6	1996	An 11-fold increase in 5-methyltetrahydrofolate (5-MTHF) uptake was observed in oocytes injected with 10 ng IFC1(RFC1) cRNA compared to water-injected controls.	5-methyltetrahydrofolate	23-47	replication factor C (activator 1) 1	Mus musculus	113-117
8664315-6	1996	An 11-fold increase in 5-methyltetrahydrofolate (5-MTHF) uptake was observed in oocytes injected with 10 ng IFC1(RFC1) cRNA compared to water-injected controls.	5-methyltetrahydrofolate	49-55	replication factor C (activator 1) 1	Mus musculus	113-117
8664315-6	1996	An 11-fold increase in 5-methyltetrahydrofolate (5-MTHF) uptake was observed in oocytes injected with 10 ng IFC1(RFC1) cRNA compared to water-injected controls.	Water	136-141	replication factor C (activator 1) 1	Mus musculus	113-117
8664315-7	1996	The expressed folate uptake in the cRNA injected oocyte was (1) 4,4"-diisothiocyanatosilbene-2,2"-disulfonic acid (DIDS)-sensitive; and (2) saturable with an apparent Km of 1.99 +/- 0.32 micrometers and a V(max) of 3782 +/- 188 fmol/oocyte per h. The distribution of mRNA species complementary to IFC1(RFC1) in different mouse tissues was examined by Northern blot analysis.	Folic Acid	14-20	replication factor C (activator 1) 1	Mus musculus	302-306
8664315-7	1996	The expressed folate uptake in the cRNA injected oocyte was (1) 4,4"-diisothiocyanatosilbene-2,2"-disulfonic acid (DIDS)-sensitive; and (2) saturable with an apparent Km of 1.99 +/- 0.32 micrometers and a V(max) of 3782 +/- 188 fmol/oocyte per h. The distribution of mRNA species complementary to IFC1(RFC1) in different mouse tissues was examined by Northern blot analysis.	4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid	115-119	replication factor C (activator 1) 1	Mus musculus	302-306
8941343-0	1996	Antisense oligonucleotides to differentiation-specific element binding protein (DSEB) mRNA inhibit adipocyte differentiation.	Oligonucleotides	10-26	replication factor C (activator 1) 1	Mus musculus	30-78
8941343-0	1996	Antisense oligonucleotides to differentiation-specific element binding protein (DSEB) mRNA inhibit adipocyte differentiation.	Oligonucleotides	10-26	replication factor C (activator 1) 1	Mus musculus	80-84
8941343-4	1996	Here we describe loss of function studies in 3T3-L1 cells performed with antisense phosphorothioate oligonucleotides that hybridize to DSEB mRNA.	Phosphorothioate Oligonucleotides	83-116	replication factor C (activator 1) 1	Mus musculus	135-139
8941343-8	1996	Control experiments using the DSEB sense oligonucleotide had no effect on hormonal-stimulated adipocyte differentiation.	Oligonucleotides	41-56	replication factor C (activator 1) 1	Mus musculus	30-34
8664315-2	1996	In this investigation, we screened a mouse intestinal cDNA library using as probe the cDNA clone of a reduced folate carrier (RFC1) of mouse leukemia L1210 cells, and identified a positive clone, IFC1(RFC1).	Folic Acid	110-116	replication factor C (activator 1) 1	Mus musculus	126-130
7659092-3	1995	We report here the cloning of 3T3-L1 adipocyte cDNA encoding a 150 kilodalton protein designated Differentiation Specific Element Binding Protein (DSEB) that exhibits sequence-specific binding to a DSE oligonucleotide.	Oligonucleotides	202-217	replication factor C (activator 1) 1	Mus musculus	147-151