PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
2891354-4	1987	Acetyl coenzyme A carboxylase (EC 6.4.1.2) from corn seedling chloroplasts was inhibited by both sethoxydim and haloxyfop, with I50 values of 2.9 and 0.5 microM, respectively.	sethoxydim	97-107	acetyl-coenzyme A carboxylase	Zea mays	0-29
2891354-4	1987	Acetyl coenzyme A carboxylase (EC 6.4.1.2) from corn seedling chloroplasts was inhibited by both sethoxydim and haloxyfop, with I50 values of 2.9 and 0.5 microM, respectively.	haloxyfop	112-121	acetyl-coenzyme A carboxylase	Zea mays	0-29
12231989-0	1993	Effects of Acetyl-Coenzyme A Carboxylase Inhibitors on Root Cell Transmembrane Electric Potentials in Graminicide-Tolerant and -Susceptible Corn (Zea mays L.).	graminicide	102-113	acetyl-coenzyme A carboxylase	Zea mays	11-40
11234801-0	2001	Polyclonal-based ELISA for the identification of cyclohexanedione analogs that inhibit maize acetyl coenzyme-A carboxylase.	1,2-cyclohexanedione	49-65	acetyl-coenzyme A carboxylase	Zea mays	93-122
11234801-1	2001	Cyclohexanedione herbicides inhibit monocotyledonous acetyl coenzyme-A carboxylase (ACCase; E.C.	1,2-cyclohexanedione	0-16	acetyl-coenzyme A carboxylase	Zea mays	53-82
11234801-1	2001	Cyclohexanedione herbicides inhibit monocotyledonous acetyl coenzyme-A carboxylase (ACCase; E.C.	1,2-cyclohexanedione	0-16	acetyl-coenzyme A carboxylase	Zea mays	84-90
12231989-1	1993	Herbicidal activity of aryloxyphenoxypropionate and cyclohexanedione herbicides (graminicides) has been proposed to involve two mechanisms: inhibition of acetyl-coenzyme A carboxylase (ACCase) and depolarization of cell membrane potential.	aryloxyphenoxypropionate	23-47	acetyl-coenzyme A carboxylase	Zea mays	154-183
12231989-1	1993	Herbicidal activity of aryloxyphenoxypropionate and cyclohexanedione herbicides (graminicides) has been proposed to involve two mechanisms: inhibition of acetyl-coenzyme A carboxylase (ACCase) and depolarization of cell membrane potential.	aryloxyphenoxypropionate	23-47	acetyl-coenzyme A carboxylase	Zea mays	185-191
12231989-1	1993	Herbicidal activity of aryloxyphenoxypropionate and cyclohexanedione herbicides (graminicides) has been proposed to involve two mechanisms: inhibition of acetyl-coenzyme A carboxylase (ACCase) and depolarization of cell membrane potential.	1,2-cyclohexanedione	52-68	acetyl-coenzyme A carboxylase	Zea mays	154-183
12231989-1	1993	Herbicidal activity of aryloxyphenoxypropionate and cyclohexanedione herbicides (graminicides) has been proposed to involve two mechanisms: inhibition of acetyl-coenzyme A carboxylase (ACCase) and depolarization of cell membrane potential.	1,2-cyclohexanedione	52-68	acetyl-coenzyme A carboxylase	Zea mays	185-191
12231989-3	1993	The graminicide-tolerant corn line contained a herbicide-insensitive form of ACCase.	graminicide	4-15	acetyl-coenzyme A carboxylase	Zea mays	77-83
24202589-6	1992	Seedling tolerance to herbicide treatments cosegregated with reduced inhibition of seedling leaf ACCase activity by sethoxydim and haloxyfop demonstrating that alterations of ACCase conferred herbicide tolerance.	sethoxydim	116-126	acetyl-coenzyme A carboxylase	Zea mays	97-103
12231761-1	1993	A mutation (Acc1-S2) in the structural gene for maize (Zea mays L.) acetyl-coenzyme A carboxylase (ACCase) that significantly reduces sethoxydim inhibition of leaf ACCase activity was used to investigate the gene-enzyme relationship regulating ACCase activity during oil deposition in developing kernels.	Oils	267-270	acetyl-coenzyme A carboxylase	Zea mays	12-16
12231761-1	1993	A mutation (Acc1-S2) in the structural gene for maize (Zea mays L.) acetyl-coenzyme A carboxylase (ACCase) that significantly reduces sethoxydim inhibition of leaf ACCase activity was used to investigate the gene-enzyme relationship regulating ACCase activity during oil deposition in developing kernels.	Oils	267-270	acetyl-coenzyme A carboxylase	Zea mays	68-97
12231761-1	1993	A mutation (Acc1-S2) in the structural gene for maize (Zea mays L.) acetyl-coenzyme A carboxylase (ACCase) that significantly reduces sethoxydim inhibition of leaf ACCase activity was used to investigate the gene-enzyme relationship regulating ACCase activity during oil deposition in developing kernels.	Oils	267-270	acetyl-coenzyme A carboxylase	Zea mays	99-105
24202589-6	1992	Seedling tolerance to herbicide treatments cosegregated with reduced inhibition of seedling leaf ACCase activity by sethoxydim and haloxyfop demonstrating that alterations of ACCase conferred herbicide tolerance.	sethoxydim	116-126	acetyl-coenzyme A carboxylase	Zea mays	175-181
24202589-6	1992	Seedling tolerance to herbicide treatments cosegregated with reduced inhibition of seedling leaf ACCase activity by sethoxydim and haloxyfop demonstrating that alterations of ACCase conferred herbicide tolerance.	haloxyfop	131-140	acetyl-coenzyme A carboxylase	Zea mays	97-103
24202589-6	1992	Seedling tolerance to herbicide treatments cosegregated with reduced inhibition of seedling leaf ACCase activity by sethoxydim and haloxyfop demonstrating that alterations of ACCase conferred herbicide tolerance.	haloxyfop	131-140	acetyl-coenzyme A carboxylase	Zea mays	175-181
24202589-7	1992	Therefore, we propose that at least three, and possible five, new alleles of the maize ACCase structural gene (Acc1) were identified based on their differential response to sethoxydim and haloxyfop.	sethoxydim	173-183	acetyl-coenzyme A carboxylase	Zea mays	87-93
24202589-7	1992	Therefore, we propose that at least three, and possible five, new alleles of the maize ACCase structural gene (Acc1) were identified based on their differential response to sethoxydim and haloxyfop.	sethoxydim	173-183	acetyl-coenzyme A carboxylase	Zea mays	111-115
24202589-7	1992	Therefore, we propose that at least three, and possible five, new alleles of the maize ACCase structural gene (Acc1) were identified based on their differential response to sethoxydim and haloxyfop.	haloxyfop	188-197	acetyl-coenzyme A carboxylase	Zea mays	87-93
24202589-7	1992	Therefore, we propose that at least three, and possible five, new alleles of the maize ACCase structural gene (Acc1) were identified based on their differential response to sethoxydim and haloxyfop.	haloxyfop	188-197	acetyl-coenzyme A carboxylase	Zea mays	111-115
24202589-8	1992	The group represented by Acc1-S1, Acc1-S2 and Acc1-S3 alleles, which had similar phenotypes, exhibited tolerance to high rates of sethoxydim and haloxyfop.	sethoxydim	130-140	acetyl-coenzyme A carboxylase	Zea mays	25-29
24202589-8	1992	The group represented by Acc1-S1, Acc1-S2 and Acc1-S3 alleles, which had similar phenotypes, exhibited tolerance to high rates of sethoxydim and haloxyfop.	sethoxydim	130-140	acetyl-coenzyme A carboxylase	Zea mays	34-38
24202589-8	1992	The group represented by Acc1-S1, Acc1-S2 and Acc1-S3 alleles, which had similar phenotypes, exhibited tolerance to high rates of sethoxydim and haloxyfop.	sethoxydim	130-140	acetyl-coenzyme A carboxylase	Zea mays	34-38
24202589-8	1992	The group represented by Acc1-S1, Acc1-S2 and Acc1-S3 alleles, which had similar phenotypes, exhibited tolerance to high rates of sethoxydim and haloxyfop.	haloxyfop	145-154	acetyl-coenzyme A carboxylase	Zea mays	25-29
24202589-8	1992	The group represented by Acc1-S1, Acc1-S2 and Acc1-S3 alleles, which had similar phenotypes, exhibited tolerance to high rates of sethoxydim and haloxyfop.	haloxyfop	145-154	acetyl-coenzyme A carboxylase	Zea mays	34-38
24202589-8	1992	The group represented by Acc1-S1, Acc1-S2 and Acc1-S3 alleles, which had similar phenotypes, exhibited tolerance to high rates of sethoxydim and haloxyfop.	haloxyfop	145-154	acetyl-coenzyme A carboxylase	Zea mays	34-38
24202589-9	1992	The Acc1-H1 allele lacked sethoxydim tolerance but was tolerant to haloxyfop, whereas the Acc1-H2 allele had intermediate tolerance to sethoxydim but was tolerant to haloxyfop.	haloxyfop	67-76	acetyl-coenzyme A carboxylase	Zea mays	4-8
24202589-9	1992	The Acc1-H1 allele lacked sethoxydim tolerance but was tolerant to haloxyfop, whereas the Acc1-H2 allele had intermediate tolerance to sethoxydim but was tolerant to haloxyfop.	sethoxydim	26-36	acetyl-coenzyme A carboxylase	Zea mays	4-8
24202589-9	1992	The Acc1-H1 allele lacked sethoxydim tolerance but was tolerant to haloxyfop, whereas the Acc1-H2 allele had intermediate tolerance to sethoxydim but was tolerant to haloxyfop.	haloxyfop	166-175	acetyl-coenzyme A carboxylase	Zea mays	90-94
24202589-11	1992	These mutations in maize ACCase should prove useful in characterization of the regulatory role of ACCase in fatty acid biosynthesis and in development of herbicide-tolerant maize germplasm.	Fatty Acids	108-118	acetyl-coenzyme A carboxylase	Zea mays	25-31
24202589-11	1992	These mutations in maize ACCase should prove useful in characterization of the regulatory role of ACCase in fatty acid biosynthesis and in development of herbicide-tolerant maize germplasm.	Fatty Acids	108-118	acetyl-coenzyme A carboxylase	Zea mays	98-104
1976254-0	1990	Dominant mutations causing alterations in acetyl-coenzyme A carboxylase confer tolerance to cyclohexanedione and aryloxyphenoxypropionate herbicides in maize.	1,2-cyclohexanedione	92-108	acetyl-coenzyme A carboxylase	Zea mays	42-71
1976254-0	1990	Dominant mutations causing alterations in acetyl-coenzyme A carboxylase confer tolerance to cyclohexanedione and aryloxyphenoxypropionate herbicides in maize.	aryloxyphenoxypropionate	113-137	acetyl-coenzyme A carboxylase	Zea mays	42-71
1976254-5	1990	Acetyl-coenzyme A carboxylase (ACCase; EC 6.4.1.2) is the target enzyme of cyclohexanedione and aryloxyphenoxypropionate herbicides.	1,2-cyclohexanedione	75-91	acetyl-coenzyme A carboxylase	Zea mays	0-29
1976254-5	1990	Acetyl-coenzyme A carboxylase (ACCase; EC 6.4.1.2) is the target enzyme of cyclohexanedione and aryloxyphenoxypropionate herbicides.	1,2-cyclohexanedione	75-91	acetyl-coenzyme A carboxylase	Zea mays	31-37
1976254-5	1990	Acetyl-coenzyme A carboxylase (ACCase; EC 6.4.1.2) is the target enzyme of cyclohexanedione and aryloxyphenoxypropionate herbicides.	aryloxyphenoxypropionate	96-120	acetyl-coenzyme A carboxylase	Zea mays	0-29
1976254-5	1990	Acetyl-coenzyme A carboxylase (ACCase; EC 6.4.1.2) is the target enzyme of cyclohexanedione and aryloxyphenoxypropionate herbicides.	aryloxyphenoxypropionate	96-120	acetyl-coenzyme A carboxylase	Zea mays	31-37
1976254-7	1990	ACCase activity from homozygous tolerant plants required greater than 100-fold more sethoxydim and 16-fold more haloxyfop for 50% inhibition than ACCase from wild-type plants.	sethoxydim	84-94	acetyl-coenzyme A carboxylase	Zea mays	0-6
1976254-7	1990	ACCase activity from homozygous tolerant plants required greater than 100-fold more sethoxydim and 16-fold more haloxyfop for 50% inhibition than ACCase from wild-type plants.	haloxyfop	112-121	acetyl-coenzyme A carboxylase	Zea mays	0-6
1976254-8	1990	These results indicate that tolerance to sethoxydim and haloxyfop is controlled by a partially dominant nuclear mutation encoding a herbicide-insensitive alteration in maize ACCase.	sethoxydim	41-51	acetyl-coenzyme A carboxylase	Zea mays	174-180
1976254-8	1990	These results indicate that tolerance to sethoxydim and haloxyfop is controlled by a partially dominant nuclear mutation encoding a herbicide-insensitive alteration in maize ACCase.	haloxyfop	56-65	acetyl-coenzyme A carboxylase	Zea mays	174-180
16667393-6	1990	Sethoxydim and haloxyfop concentrations that inhibited ACCase by 50% were similar for BMS, B10S, B50S, and B100S.	sethoxydim	0-10	acetyl-coenzyme A carboxylase	Zea mays	55-61
16667393-6	1990	Sethoxydim and haloxyfop concentrations that inhibited ACCase by 50% were similar for BMS, B10S, B50S, and B100S.	haloxyfop	15-24	acetyl-coenzyme A carboxylase	Zea mays	55-61
16667393-7	1990	However, ACCase activities were 6.01, 10.7, 16.1, and 11.4 nmol HCO(3) (-) incorporated per milligram of protein per minute in extracts of BMS, B10S, B50S, and B100S, respectively, suggesting that increased wild-type ACCase activity conferred herbicide tolerance.	Bicarbonates	64-70	acetyl-coenzyme A carboxylase	Zea mays	9-15
16667393-8	1990	Incorporation of [(14)C]acetate into the nonpolar lipid fraction was higher for B50S than for BMS in the absence of sethoxydim providing further evidence for an increase in ACCase activity in the selected line.	[(14)c]acetate	17-31	acetyl-coenzyme A carboxylase	Zea mays	173-179
16667393-10	1990	The levels of a biotin-containing polypeptide (about 220,000 molecular weight), presumably the ACCase subunit, were increased in the tissue cultures that exhibited elevated ACCase activity indicating overproduction of the ACCase enzyme.	Biotin	16-22	acetyl-coenzyme A carboxylase	Zea mays	95-101
16667393-10	1990	The levels of a biotin-containing polypeptide (about 220,000 molecular weight), presumably the ACCase subunit, were increased in the tissue cultures that exhibited elevated ACCase activity indicating overproduction of the ACCase enzyme.	Biotin	16-22	acetyl-coenzyme A carboxylase	Zea mays	173-179
16667393-10	1990	The levels of a biotin-containing polypeptide (about 220,000 molecular weight), presumably the ACCase subunit, were increased in the tissue cultures that exhibited elevated ACCase activity indicating overproduction of the ACCase enzyme.	Biotin	16-22	acetyl-coenzyme A carboxylase	Zea mays	173-179