PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
1935876-2	1991	EsD polymorphism was also analyzed by one-dimensional isoelectric focusing under reducing and mild denaturing conditions to study the influence of dithiothreitol and low concentrations of urea on the focusing pattern of the EsD dimers.	Urea	188-192	esterase D	Homo sapiens	224-227
10742212-12	2000	We suggest that, in vivo, EstA could be involved in (phospho)lipid metabolism or cellular detoxification or both, as its sequence showed significant similarity to S-formylglutathione hydrolase (FGH) of Paracoccus denitrificans and human EstD (or FGH), which are part of a universal formaldehyde detoxification pathway.	Formaldehyde	282-294	esterase D	Homo sapiens	194-197
8892832-0	1996	S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification?	Formaldehyde	117-129	esterase D	Homo sapiens	0-29
8892832-0	1996	S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification?	Formaldehyde	117-129	esterase D	Homo sapiens	81-91
8892832-5	1996	S-Formylglutathione hydrolase appears to be part of a formaldehyde detoxification pathway that is universal in nature.	Formaldehyde	54-66	esterase D	Homo sapiens	0-29
8690320-11	1996	(3) Two common alleles in Esterase D (EsD) polymorphism, EsD1 and EsD2 were characterized by the substitution of one amino acid (Gly-Glu) caused by the point mutation of one nucleotide (G-A).	N-glycylglutamic acid	129-136	esterase D	Homo sapiens	26-36
8690320-11	1996	(3) Two common alleles in Esterase D (EsD) polymorphism, EsD1 and EsD2 were characterized by the substitution of one amino acid (Gly-Glu) caused by the point mutation of one nucleotide (G-A).	Gallium	186-189	esterase D	Homo sapiens	26-36
8263492-0	1993	Simultaneous subtyping of group specific component and esterase D by isoelectric focusing on agarose gels.	Sepharose	93-100	esterase D	Homo sapiens	55-65
2527190-1	1989	Two rapid and reliable electrophoretic techniques for PGM1 and EsD typing on ultrathin polyacrylamide gels are described.	polyacrylamide	87-101	esterase D	Homo sapiens	63-66
2340827-0	1990	Phenotyping of erythrocyte acid phosphatase and esterase D by high field strength isoelectric focusing on cellulose acetate membrane.	acetylcellulose	106-123	esterase D	Homo sapiens	48-58
2340827-1	1990	Phenotyping of erythrocyte acid phosphatase (EAP) and esterase D (ESD) by cellulose acetate membrane isoelectric focusing (CAM-IEF) under a nonequilibrium condition is described.	acetylcellulose	74-91	esterase D	Homo sapiens	54-64
2584942-5	1989	The polyacrylamide gel can also be used for the subtyping of esterase D.	polyacrylamide	4-18	esterase D	Homo sapiens	61-71
1811491-1	1991	The enzyme systems aldehyde dehydrogenase (ALDH), formaldehyde dehydrogenase (FDH) and S-formylglutation dehydrogenase (FGH/ESD) were investigated in specimen of cadaveric liver and brain by semiquantitative adjusted starch gel electrophoresis.	Starch	217-223	esterase D	Homo sapiens	120-123
2612468-0	1989	Simultaneous phenotyping of erythrocyte acid phosphatase and esterase D by nonequilibrium agarose isoelectric focusing.	Sepharose	90-97	esterase D	Homo sapiens	61-71
2612468-1	1989	Nonequilibrium agarose isoelectric focusing in a pH 4.5-7 gradient with 3-(N-morpholinopropanesulfonic acid (MOPS) and taurine as chemical separators presents a fast, easy and reliable method for the simultaneous determination of the common erythrocyte acid phosphatase and esterase D phenotypes in hemolysates and dried bloodstains.	Sepharose	15-22	esterase D	Homo sapiens	274-284
2612468-1	1989	Nonequilibrium agarose isoelectric focusing in a pH 4.5-7 gradient with 3-(N-morpholinopropanesulfonic acid (MOPS) and taurine as chemical separators presents a fast, easy and reliable method for the simultaneous determination of the common erythrocyte acid phosphatase and esterase D phenotypes in hemolysates and dried bloodstains.	morpholinopropane sulfonic acid	109-113	esterase D	Homo sapiens	274-284
2612468-1	1989	Nonequilibrium agarose isoelectric focusing in a pH 4.5-7 gradient with 3-(N-morpholinopropanesulfonic acid (MOPS) and taurine as chemical separators presents a fast, easy and reliable method for the simultaneous determination of the common erythrocyte acid phosphatase and esterase D phenotypes in hemolysates and dried bloodstains.	Taurine	119-126	esterase D	Homo sapiens	274-284
3234387-0	1988	Two new esterase D (ESD) variants revealed by isoelectric focusing in agarose gel.	Sepharose	70-77	esterase D	Homo sapiens	8-18
3234387-0	1988	Two new esterase D (ESD) variants revealed by isoelectric focusing in agarose gel.	Sepharose	70-77	esterase D	Homo sapiens	20-23
3234387-1	1988	Using isoelectric focusing in thin-layer agarose gel (AGIF) with the narrow pH range of 4.5-5.4, a high resolution of esterase D (ESD) isozyme banding patterns has been achieved.	Sepharose	41-48	esterase D	Homo sapiens	118-128
3234387-1	1988	Using isoelectric focusing in thin-layer agarose gel (AGIF) with the narrow pH range of 4.5-5.4, a high resolution of esterase D (ESD) isozyme banding patterns has been achieved.	Sepharose	41-48	esterase D	Homo sapiens	130-133
3591015-2	1987	Human red cell Esterase D (EsD) was analyzed by isoelectric focusing (IEF) on ultrathin-layer polyacrylamide gel with a pH range of 5.0-6.0.	polyacrylamide	94-108	esterase D	Homo sapiens	15-25
3385383-1	1988	An ultrathin-layer polyacrylamide gel isoelectric focusing technique that uses a composite of ampholytes from three commercial sources is described for subtyping esterase D.	polyacrylamide	19-33	esterase D	Homo sapiens	162-172
3587887-3	1987	13 (q12.3-q21.2), was the esterase D activity (type 2) 1.47 Unit/gHb which was approximately 50% of the level in normals.	4-hydroxybutyric acid	65-68	esterase D	Homo sapiens	26-36
3817677-5	1987	In addition, a method for the consecutive determination of esterase D (ESD) and GPT on the same gel using the malic acid buffer system is described.	malic acid	110-120	esterase D	Homo sapiens	59-69
3591015-2	1987	Human red cell Esterase D (EsD) was analyzed by isoelectric focusing (IEF) on ultrathin-layer polyacrylamide gel with a pH range of 5.0-6.0.	polyacrylamide	94-108	esterase D	Homo sapiens	27-30
3462714-2	1986	Since the gene for esterase D (ESD) is known to be tightly linked to the retinoblastoma locus (RB1) in the q14.1 band of chromosome 13, we have cloned the ESD gene from a human cDNA library by using oligonucleotides specific for a partial amino acid sequence of the purified enzyme to provide a genetic marker for further studies on retinoblastoma.	Oligonucleotides	199-215	esterase D	Homo sapiens	19-29
3770744-1	1986	The S-formylglutathione hydrolase (FGH) polymorphism of human red blood cells was studied in unrelated individuals, both by isoelectric focusing and starch gel electrophoresis, and with the substrates S-acetylglutathione and 4-methylumbelliferyl-acetate (the standard substrate for esterase D (ESD].	S-acetylglutathione	201-220	esterase D	Homo sapiens	35-38
3770744-1	1986	The S-formylglutathione hydrolase (FGH) polymorphism of human red blood cells was studied in unrelated individuals, both by isoelectric focusing and starch gel electrophoresis, and with the substrates S-acetylglutathione and 4-methylumbelliferyl-acetate (the standard substrate for esterase D (ESD].	4-methylumbelliferyl acetate	225-253	esterase D	Homo sapiens	4-33
3770744-1	1986	The S-formylglutathione hydrolase (FGH) polymorphism of human red blood cells was studied in unrelated individuals, both by isoelectric focusing and starch gel electrophoresis, and with the substrates S-acetylglutathione and 4-methylumbelliferyl-acetate (the standard substrate for esterase D (ESD].	4-methylumbelliferyl acetate	225-253	esterase D	Homo sapiens	35-38
3770744-1	1986	The S-formylglutathione hydrolase (FGH) polymorphism of human red blood cells was studied in unrelated individuals, both by isoelectric focusing and starch gel electrophoresis, and with the substrates S-acetylglutathione and 4-methylumbelliferyl-acetate (the standard substrate for esterase D (ESD].	Starch	149-155	esterase D	Homo sapiens	35-38
3770744-1	1986	The S-formylglutathione hydrolase (FGH) polymorphism of human red blood cells was studied in unrelated individuals, both by isoelectric focusing and starch gel electrophoresis, and with the substrates S-acetylglutathione and 4-methylumbelliferyl-acetate (the standard substrate for esterase D (ESD].	S-acetylglutathione	201-220	esterase D	Homo sapiens	4-33
3462714-2	1986	Since the gene for esterase D (ESD) is known to be tightly linked to the retinoblastoma locus (RB1) in the q14.1 band of chromosome 13, we have cloned the ESD gene from a human cDNA library by using oligonucleotides specific for a partial amino acid sequence of the purified enzyme to provide a genetic marker for further studies on retinoblastoma.	Oligonucleotides	199-215	esterase D	Homo sapiens	155-158
3462728-3	1986	The Km of esterase D was estimated to be 10 X 10(-6) M using 4-methylumbelliferyl acetate as substrate.	4-methylumbelliferyl acetate	61-89	esterase D	Homo sapiens	10-20
3462728-8	1986	Furthermore, the expression of esterase D was enhanced 3-fold in a promonocytic cell line treated with phenobarbital but not with phorbol myristate acetate, suggesting that esterase D may have a role in detoxification.	Phenobarbital	103-116	esterase D	Homo sapiens	31-41
3462728-8	1986	Furthermore, the expression of esterase D was enhanced 3-fold in a promonocytic cell line treated with phenobarbital but not with phorbol myristate acetate, suggesting that esterase D may have a role in detoxification.	Phenobarbital	103-116	esterase D	Homo sapiens	173-183
3710480-1	1986	Using "new" techniques (malic acid thin layer agarose gel electrophoresis and/or isoelectric focusing), the polymorphism of the human red cell isozyme system esterase D (ESD) was shown to be extended.	malic acid	24-34	esterase D	Homo sapiens	158-168
3710480-1	1986	Using "new" techniques (malic acid thin layer agarose gel electrophoresis and/or isoelectric focusing), the polymorphism of the human red cell isozyme system esterase D (ESD) was shown to be extended.	malic acid	24-34	esterase D	Homo sapiens	170-173
3710480-1	1986	Using "new" techniques (malic acid thin layer agarose gel electrophoresis and/or isoelectric focusing), the polymorphism of the human red cell isozyme system esterase D (ESD) was shown to be extended.	Sepharose	46-53	esterase D	Homo sapiens	158-168
3710480-1	1986	Using "new" techniques (malic acid thin layer agarose gel electrophoresis and/or isoelectric focusing), the polymorphism of the human red cell isozyme system esterase D (ESD) was shown to be extended.	Sepharose	46-53	esterase D	Homo sapiens	170-173
6868831-0	1983	[Detection of esterase D and glyoxalase I in human hair roots using agarose gel thin-layer electrophoresis].	Sepharose	68-75	esterase D	Homo sapiens	14-24
4007717-1	1985	The simultaneous isoelectric focusing (IEF) in polyacrylamide gels (PAG) of erythrocyte acid phosphatase (EAP) and esterase D (EsD) allows the poor discriminating power (DP) of EsD to be usefully combined with a highly discriminating system EAP, such that a joint DP of 0.766 was achieved compared with PGM IEF DP 0.756.	polyacrylamide	47-61	esterase D	Homo sapiens	127-130
4007717-1	1985	The simultaneous isoelectric focusing (IEF) in polyacrylamide gels (PAG) of erythrocyte acid phosphatase (EAP) and esterase D (EsD) allows the poor discriminating power (DP) of EsD to be usefully combined with a highly discriminating system EAP, such that a joint DP of 0.766 was achieved compared with PGM IEF DP 0.756.	polyacrylamide gels	68-71	esterase D	Homo sapiens	115-125
4007717-1	1985	The simultaneous isoelectric focusing (IEF) in polyacrylamide gels (PAG) of erythrocyte acid phosphatase (EAP) and esterase D (EsD) allows the poor discriminating power (DP) of EsD to be usefully combined with a highly discriminating system EAP, such that a joint DP of 0.766 was achieved compared with PGM IEF DP 0.756.	polyacrylamide gels	68-71	esterase D	Homo sapiens	127-130
4007717-1	1985	The simultaneous isoelectric focusing (IEF) in polyacrylamide gels (PAG) of erythrocyte acid phosphatase (EAP) and esterase D (EsD) allows the poor discriminating power (DP) of EsD to be usefully combined with a highly discriminating system EAP, such that a joint DP of 0.766 was achieved compared with PGM IEF DP 0.756.	polyacrylamide gels	68-71	esterase D	Homo sapiens	177-180
3456572-0	1986	A sialic acid-specific O-acetylesterase in human erythrocytes: possible identity with esterase D, the genetic marker of retinoblastomas and Wilson disease.	N-Acetylneuraminic Acid	2-13	esterase D	Homo sapiens	86-96
3456572-3	1986	Esterase D is characterized by its reactivity with 4-methylumbelliferyl acetate.	4-methylumbelliferyl acetate	51-79	esterase D	Homo sapiens	0-10
3456572-6	1986	We next present evidence that suggests that esterase D is identical to this sialic acid-specific O-acetylesterase.	N-Acetylneuraminic Acid	76-87	esterase D	Homo sapiens	44-54
3776354-1	1986	The distribution of the human red cell esterase D (EsD) "extended" polymorphism in a population sample from Tuscany (Italy) was studied using agarose gel isoelectric focusing.	Sepharose	142-149	esterase D	Homo sapiens	39-49
3776354-1	1986	The distribution of the human red cell esterase D (EsD) "extended" polymorphism in a population sample from Tuscany (Italy) was studied using agarose gel isoelectric focusing.	Sepharose	142-149	esterase D	Homo sapiens	51-54
2933484-0	1985	An agarose gel electrophoretic method for typing phosphoglucomutase-1, esterase D, or glyoxalase I.	Sepharose	3-10	esterase D	Homo sapiens	71-81
2933484-1	1985	A conventional agarose gel electrophoretic method was described for typing phosphoglucomutase-1, esterase D, or glyoxalase I as single systems.	Sepharose	15-22	esterase D	Homo sapiens	97-107
4065784-1	1985	Non-equilibrium focusing in a pH 4-6 gradient in ultra-thin polyacrylamide gels has been shown to be a reliable and reproducible method for detecting the six common esterase D phenotypes (EsD 1,2-1,2,5-1,5-2 and 5) in dried bloodstains.	polyacrylamide	60-74	esterase D	Homo sapiens	165-175
2979304-0	1985	Phenotyping of esterase D in the Polish population by cellulose acetate gel isoelectrofocusing.	acetylcellulose	54-71	esterase D	Homo sapiens	15-25
6519615-0	1984	The esterase D polymorphism as revealed by isoelectric focusing in ultra-thin polyacrylamide gels.	polyacrylamide	78-92	esterase D	Homo sapiens	4-14
6519615-1	1984	The polymorphism of human red cell esterase D (EsD) was studied using isoelectric focusing (pH 4-6) in ultra-thin polyacrylamide gels.	polyacrylamide	114-128	esterase D	Homo sapiens	35-45
6519615-1	1984	The polymorphism of human red cell esterase D (EsD) was studied using isoelectric focusing (pH 4-6) in ultra-thin polyacrylamide gels.	polyacrylamide	114-128	esterase D	Homo sapiens	47-50
6698561-1	1984	The isoelectric focusing study of esterase D in Japanese revealed evidence of a new polymorphic allele (EsD7) which is difficult to find by conventional starch gel electrophoresis only.	Starch	153-159	esterase D	Homo sapiens	34-44
595780-0	1977	[Preparation of esterase D phenotypes of erythrocytes using 4-methylumbelliferone heptanoate after electrophoresis in agar-agarose gel].	4-methylumbelliferyl heptanoate	60-92	esterase D	Homo sapiens	16-26
744972-0	1978	Electrophoresis of esterase D in fresh blood and in bloodstains on cellulose acetate.	acetylcellulose	67-84	esterase D	Homo sapiens	19-29
7184301-0	1982	[Acid phosphatase activity and non-specific esterase D of alpha-naphthyl acetate in the lymphocytes of patients with digestive system neoplasms after surgical treatment].	alpha-naphthyl acetate	58-80	esterase D	Homo sapiens	44-54
623100-1	1978	Esterase D (EsD), purified from human erythrocytes and tested with a variety of substrates, hydrolyzed only triacetin, tributyrin, and certain soluble aryl esters of aliphatic acids.	Triacetin	108-117	esterase D	Homo sapiens	0-10
623100-1	1978	Esterase D (EsD), purified from human erythrocytes and tested with a variety of substrates, hydrolyzed only triacetin, tributyrin, and certain soluble aryl esters of aliphatic acids.	Triacetin	108-117	esterase D	Homo sapiens	12-15
623100-1	1978	Esterase D (EsD), purified from human erythrocytes and tested with a variety of substrates, hydrolyzed only triacetin, tributyrin, and certain soluble aryl esters of aliphatic acids.	tributyrin	119-129	esterase D	Homo sapiens	0-10
623100-1	1978	Esterase D (EsD), purified from human erythrocytes and tested with a variety of substrates, hydrolyzed only triacetin, tributyrin, and certain soluble aryl esters of aliphatic acids.	tributyrin	119-129	esterase D	Homo sapiens	12-15
623100-1	1978	Esterase D (EsD), purified from human erythrocytes and tested with a variety of substrates, hydrolyzed only triacetin, tributyrin, and certain soluble aryl esters of aliphatic acids.	aryl esters	151-162	esterase D	Homo sapiens	0-10
623100-1	1978	Esterase D (EsD), purified from human erythrocytes and tested with a variety of substrates, hydrolyzed only triacetin, tributyrin, and certain soluble aryl esters of aliphatic acids.	aryl esters	151-162	esterase D	Homo sapiens	12-15
623100-1	1978	Esterase D (EsD), purified from human erythrocytes and tested with a variety of substrates, hydrolyzed only triacetin, tributyrin, and certain soluble aryl esters of aliphatic acids.	Fatty Acids	166-181	esterase D	Homo sapiens	0-10
623100-1	1978	Esterase D (EsD), purified from human erythrocytes and tested with a variety of substrates, hydrolyzed only triacetin, tributyrin, and certain soluble aryl esters of aliphatic acids.	Fatty Acids	166-181	esterase D	Homo sapiens	12-15
595780-0	1977	[Preparation of esterase D phenotypes of erythrocytes using 4-methylumbelliferone heptanoate after electrophoresis in agar-agarose gel].	Agar	118-122	esterase D	Homo sapiens	16-26
595780-0	1977	[Preparation of esterase D phenotypes of erythrocytes using 4-methylumbelliferone heptanoate after electrophoresis in agar-agarose gel].	Sepharose	123-130	esterase D	Homo sapiens	16-26
1150255-1	1975	With the help of a simplified and quick method, cellulose acetate electrophoresis, the phenotypes of esterase D were determined in an Assamese population.	acetylcellulose	48-65	esterase D	Homo sapiens	101-111
983351-1	1976	Esterase D phenotypes were determined in a population sample of Northern Germany (Schleswig-Holstein) by starch gel electrophoresis.	Starch	105-111	esterase D	Homo sapiens	0-10
1150262-0	1975	Esterase D polymorphism: high-voltage agarose-gel electrophoresis and distribution of phenotypes in different European populations.	Sepharose	38-45	esterase D	Homo sapiens	0-10
1150262-1	1975	Esterase D phenotypes were determined in 1082 non-related individuals from the western region of Germany by agarose-gel electrophoresis.	Sepharose	108-115	esterase D	Homo sapiens	0-10
1148398-2	1975	Esterase D phenotypes were determined in a population sample of Berlin (West) by means of high voltage agarosegel electrophoresis.	agarosegel	103-113	esterase D	Homo sapiens	0-10
4420151-0	1974	[Esterase D polymorphism: demonstration by high-voltage, starch-gel electrophoresis and presentation of allele frequencies (author"s transl)].	Starch	57-63	esterase D	Homo sapiens	1-11
32757998-6	2021	The extract was cytotoxic to both cell lines by inducing apoptotic cell death and acted in synergy with cisplatin; such effect was stronger in HepG2 cells than in FGH cells, demonstrating some selectivity to tumor cells.	Cisplatin	104-113	esterase D	Homo sapiens	163-166
4450806-0	1974	[Investigations on the polymorphism of red cell esterase D by high voltage agarose gel electrophoresis (author"s transl)].	Sepharose	75-82	esterase D	Homo sapiens	48-58
28276689-0	2017	Synthesis of the KLMN Fragment of Gymnocin-A from the FGH Fragment.	gymnocin A	34-44	esterase D	Homo sapiens	54-57
31397637-1	2020	Background: The aim of this study was to evaluate the cytotoxicity of cyanoacrylate adhesives in an indirect contact assay in human gingival fibroblast (FGH) and oral osteoblasts (GO) lineages.	Cyanoacrylates	70-83	esterase D	Homo sapiens	153-156
32247735-3	2020	To address the question, we identified that 4-chloro-2-(5-phenyl-1-(pyridin-2-yl)-4, 5-dihydro-1H-pyrazol-3-yl) phenol (FPD5) could be a good candidate activator for ESD activity.	4-chloro-2-(5-phenyl-1-(pyridin-2-yl)-4, 5-dihydro-1h-pyrazol-3-yl) phenol	44-118	esterase D	Homo sapiens	166-169
29179433-4	2017	We found physical and functional interactions between Skl and S-formylglutathione hydrolase (FGH), a key enzyme in the generation of the major cellular anti-oxidant GSH, using co-immunoprecipitation-coupled mass spectrometry.	Glutathione Disulfide	165-168	esterase D	Homo sapiens	62-91
29179433-4	2017	We found physical and functional interactions between Skl and S-formylglutathione hydrolase (FGH), a key enzyme in the generation of the major cellular anti-oxidant GSH, using co-immunoprecipitation-coupled mass spectrometry.	Glutathione Disulfide	165-168	esterase D	Homo sapiens	93-96
29179433-10	2017	The antioxidant activity of Skl was eliminated by silencing of FGH, indicating that Skl increased GSH via FGH.	Glutathione Disulfide	98-101	esterase D	Homo sapiens	106-109
29179433-12	2017	Site-directed mutagenesis of the N-glycan-modified residues in Skl abolished its antioxidant activity, suggesting that these N-glycan moieties are important features that interact with FGH.	n-glycan	33-41	esterase D	Homo sapiens	185-188
29179433-12	2017	Site-directed mutagenesis of the N-glycan-modified residues in Skl abolished its antioxidant activity, suggesting that these N-glycan moieties are important features that interact with FGH.	n-glycan	125-133	esterase D	Homo sapiens	185-188
29179433-14	2017	Therefore, this study demonstrates, for the first time, that Skl regulates anti-oxidant GSH generation via interaction with FGH through N-glycosylation.	Glutathione Disulfide	88-91	esterase D	Homo sapiens	124-127
29179433-14	2017	Therefore, this study demonstrates, for the first time, that Skl regulates anti-oxidant GSH generation via interaction with FGH through N-glycosylation.	Nitrogen	136-137	esterase D	Homo sapiens	124-127
28276689-1	2017	An improved route for the synthesis of the KLMN fragment of gymnocin-A was developed through the oxiranyl anion coupling of the FGH fragment with a chiral C3 epoxy sulfone, followed by 6-endo cyclization.	gymnocin A	60-70	esterase D	Homo sapiens	128-131
28276689-1	2017	An improved route for the synthesis of the KLMN fragment of gymnocin-A was developed through the oxiranyl anion coupling of the FGH fragment with a chiral C3 epoxy sulfone, followed by 6-endo cyclization.	oxiranyl anion	97-111	esterase D	Homo sapiens	128-131
28276689-1	2017	An improved route for the synthesis of the KLMN fragment of gymnocin-A was developed through the oxiranyl anion coupling of the FGH fragment with a chiral C3 epoxy sulfone, followed by 6-endo cyclization.	c3 epoxy sulfone	155-171	esterase D	Homo sapiens	128-131
26521846-2	2015	The synthesis features three iterations of an oxiranyl anion strategy, involving base-mediated cycloetherification, ring expansion, and reductive etherification, for the construction of the FGH fragment and for its coupling with the ABC and KLMN fragments.	oxiranyl anion	46-60	esterase D	Homo sapiens	190-193
25221997-3	2014	This study showed that A398, a novel podophyllotoxin analogue, was cytotoxic to the HT-29, MCF-7, MOLT-4 and HL-60 tumor cell lines, being less active in human peripheral blood mononuclear cells and normal cell lines FGH and IEC-6.	a398	23-27	esterase D	Homo sapiens	217-220
22405967-2	2012	The aim of this study was to investigate the effect of Eudragit E/HCl (E-SD) on the reprecipitation of a poorly water-soluble drug, tacrolimus.	Tacrolimus	132-142	esterase D	Homo sapiens	71-75
22906720-2	2012	Under oxidizing conditions, inhibition of Saccharomyces cerevisiae S-formylglutathione hydrolase (SFGH, homologous to human esterase D) activity is attributable to a cysteine (Cys-60) adjacent to its catalytic triad and approximately 8.0 A away from the Ogamma of the nucleophilic serine.	Cysteine	166-174	esterase D	Homo sapiens	124-134
22906720-2	2012	Under oxidizing conditions, inhibition of Saccharomyces cerevisiae S-formylglutathione hydrolase (SFGH, homologous to human esterase D) activity is attributable to a cysteine (Cys-60) adjacent to its catalytic triad and approximately 8.0 A away from the Ogamma of the nucleophilic serine.	Cysteine	176-179	esterase D	Homo sapiens	124-134
22405967-2	2012	The aim of this study was to investigate the effect of Eudragit E/HCl (E-SD) on the reprecipitation of a poorly water-soluble drug, tacrolimus.	Water	112-117	esterase D	Homo sapiens	71-75
22906720-2	2012	Under oxidizing conditions, inhibition of Saccharomyces cerevisiae S-formylglutathione hydrolase (SFGH, homologous to human esterase D) activity is attributable to a cysteine (Cys-60) adjacent to its catalytic triad and approximately 8.0 A away from the Ogamma of the nucleophilic serine.	Serine	281-287	esterase D	Homo sapiens	124-134
22405967-5	2012	Supersaturation profiles of tacrolimus were observed, and were maintained for 24h only with E-SD.	Tacrolimus	28-38	esterase D	Homo sapiens	92-96
22405967-7	2012	Solid dispersions prepared with E-SD showed higher solubility of tacrolimus compared with that of HPMC.	Tacrolimus	65-75	esterase D	Homo sapiens	32-36
22405967-11	2012	Further, by mixing E-SD the solid dispersion prepared with HPMC showed enhanced drug solubility.	Hypromellose Derivatives	59-63	esterase D	Homo sapiens	19-23
20136065-0	2010	Conformational analysis of a model for the trans-fused FGH ether rings in brevetoxin A.	Ether	59-64	esterase D	Homo sapiens	55-58
20136065-0	2010	Conformational analysis of a model for the trans-fused FGH ether rings in brevetoxin A.	Brevetoxin A	74-86	esterase D	Homo sapiens	55-58
20136065-1	2010	We have applied the Low Mode:Monte Carlo (LM:MC) conformational search method to an investigation of the low energy structures for 3R,4aS,7aR,11aS,12aR)-11a-methyl-3-phenyldecahydro-1H-[1,3]dioxino[5,4-b]pyrano[2,3-g]oxocine, 3, a model for the FGH rings in brevetoxin A, a potent marine toxin.	7ar,11as,12ar)-11a-methyl-3-phenyldecahydro-1h-[1,3]dioxino[5,4-b]pyrano[2,3-g]oxocine	138-224	esterase D	Homo sapiens	245-248
18164690-4	2008	Molecular docking with site-directed mutagenesis analyses indicated that ESD functioned as a partial agonist of PPARgamma by adopting a distinct binding mode to PPARgamma compared with rosiglitazone.	Rosiglitazone	185-198	esterase D	Homo sapiens	73-76
21868245-12	2011	EGCs were treated with ESD in two cases, partial resection of stomach in one, and oesophagocolojejunostomy in three, including one patient who underwent the operation after ESD.	gallocatechol	0-4	esterase D	Homo sapiens	23-26
21868245-12	2011	EGCs were treated with ESD in two cases, partial resection of stomach in one, and oesophagocolojejunostomy in three, including one patient who underwent the operation after ESD.	gallocatechol	0-4	esterase D	Homo sapiens	173-176
15727466-0	2005	A highly efficient synthesis of the FGH ring of micrandilactone A.	micrandilactone	48-63	esterase D	Homo sapiens	36-39
15727466-2	2005	The functionalized FGH ring system of micrandilactone A was successfully constructed in high selectivity and good yields.	micrandilactone A	38-55	esterase D	Homo sapiens	19-22
12688794-0	2003	Convergent synthesis of the E"FGH ring fragment of ciguatoxin 1B via an acetylene cobalt complex strategy.	Acetylene	72-81	esterase D	Homo sapiens	30-33
12688794-0	2003	Convergent synthesis of the E"FGH ring fragment of ciguatoxin 1B via an acetylene cobalt complex strategy.	Cobalt	82-88	esterase D	Homo sapiens	30-33
11720582-3	2001	In this, the second of two Letters, we describe an effective assembly of (+)-4, an eastern hemisphere subtarget comprising the FGH rings of (+)-nodulisporic acid A (1) (17 steps, 9% overall yield).	nodulisporic acid A	140-163	esterase D	Homo sapiens	127-130