PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
26740819-8	2016	Novel genes determining high acetic acid tolerance, GLO1, DOT5, CUP2, and a previously identified component, VMA7, were identified as causative alleles in the second major F1 QTL and in three newly appearing F7 QTLs, respectively.	Acetic Acid	29-40	Cup2p	Saccharomyces cerevisiae S288C	64-68
29604179-0	2018	Ace1 prevents intracellular copper accumulation by regulating Fet3 expression and thereby restricting Aft1 activity.	Copper	28-34	Cup2p	Saccharomyces cerevisiae S288C	0-4
29604179-4	2018	In this work, we identify Ace1, the regulator of copper detoxification genes, as a regulator of FET3.	Copper	49-55	Cup2p	Saccharomyces cerevisiae S288C	26-30
29604179-5	2018	We suggest that the activation of FET3 by Ace1 prevents the hyper activation of Aft1, possibly by assuring the adequate functioning of mitochondrial iron-sulfur cluster biogenesis.	Iron	149-153	Cup2p	Saccharomyces cerevisiae S288C	42-46
29604179-5	2018	We suggest that the activation of FET3 by Ace1 prevents the hyper activation of Aft1, possibly by assuring the adequate functioning of mitochondrial iron-sulfur cluster biogenesis.	Sulfur	154-160	Cup2p	Saccharomyces cerevisiae S288C	42-46
29604179-6	2018	While reinforcing the link between iron and copper homeostasis, this work unveils a novel protection mechanism against copper toxicity mediated by Ace1, which relies in the activation of FET3 and results in the restriction of Aft1 activity as a means to prevent excessive copper accumulation.	Iron	35-39	Cup2p	Saccharomyces cerevisiae S288C	147-151
29604179-6	2018	While reinforcing the link between iron and copper homeostasis, this work unveils a novel protection mechanism against copper toxicity mediated by Ace1, which relies in the activation of FET3 and results in the restriction of Aft1 activity as a means to prevent excessive copper accumulation.	Copper	119-125	Cup2p	Saccharomyces cerevisiae S288C	147-151
28086780-0	2017	The Zygosaccharomyces bailii transcription factor Haa1 is required for acetic acid and copper stress responses suggesting subfunctionalization of the ancestral bifunctional protein Haa1/Cup2.	Acetic Acid	71-82	Cup2p	Saccharomyces cerevisiae S288C	186-190
28086780-0	2017	The Zygosaccharomyces bailii transcription factor Haa1 is required for acetic acid and copper stress responses suggesting subfunctionalization of the ancestral bifunctional protein Haa1/Cup2.	Copper	87-93	Cup2p	Saccharomyces cerevisiae S288C	186-190
28086780-8	2017	S. cerevisiae Cup2 (alias Ace1) is a transcription factor involved in response and tolerance to copper stress.	Copper	96-102	Cup2p	Saccharomyces cerevisiae S288C	14-18
24471920-1	2014	In yeast, Ace1p-dependent induction of CUP1 is responsible for protecting cells from copper toxicity.	Copper	85-91	Cup2p	Saccharomyces cerevisiae S288C	10-15
23019066-5	2012	Plastically expressed genes included both genes regulated directly by copper-binding transcription factors Mac1 and Ace1 and genes indirectly responding to the downstream metabolic consequences of the copper gradient, particularly genes involved in copper, iron, and sulfur homeostasis.	Copper	201-207	Cup2p	Saccharomyces cerevisiae S288C	116-120
23019066-5	2012	Plastically expressed genes included both genes regulated directly by copper-binding transcription factors Mac1 and Ace1 and genes indirectly responding to the downstream metabolic consequences of the copper gradient, particularly genes involved in copper, iron, and sulfur homeostasis.	Copper	70-76	Cup2p	Saccharomyces cerevisiae S288C	116-120
23332833-5	2013	We cloned the P. brumalis PbAce1 transcription factor, a homologue of Saccharomyces cerevisiae transcription factor Ace1, which regulates metallothionein genes in response to excess copper.	Copper	182-188	Cup2p	Saccharomyces cerevisiae S288C	28-32
23332833-9	2013	PbAce1 has two Cys-rich repeat motifs (PbC1 and PbC2), which are similar to the Cys-rich repeat domain in metallothionein proteins, and are uniquely conserved in the C-terminal domain of basidiomycetous Ace1 sequences.	Cysteine	15-18	Cup2p	Saccharomyces cerevisiae S288C	2-6
23332833-9	2013	PbAce1 has two Cys-rich repeat motifs (PbC1 and PbC2), which are similar to the Cys-rich repeat domain in metallothionein proteins, and are uniquely conserved in the C-terminal domain of basidiomycetous Ace1 sequences.	Cysteine	80-83	Cup2p	Saccharomyces cerevisiae S288C	2-6
23358723-4	2013	The chromosomal rearrangements in EC strains result in segmental duplications in chromosomes 7 and 8, which increase the copy number of genes involved in copper regulation, including the crucial transcriptional activator CUP2 and the metallothionein CUP1.	Copper	154-160	Cup2p	Saccharomyces cerevisiae S288C	221-225
23358723-5	2013	The copy number of CUP2 is correlated with the level of copper tolerance, indicating that increasing dosages of a single transcriptional activator by chromosomal rearrangements has a profound effect on a regulatory pathway.	Copper	56-62	Cup2p	Saccharomyces cerevisiae S288C	19-23
23358723-6	2013	By gene expression analysis and functional assays, we identified three previously unknown downstream targets of CUP2: PHO84, SCM4, and CIN2, all of which contributed to copper tolerance in EC strains.	Copper	169-175	Cup2p	Saccharomyces cerevisiae S288C	112-116
23019066-5	2012	Plastically expressed genes included both genes regulated directly by copper-binding transcription factors Mac1 and Ace1 and genes indirectly responding to the downstream metabolic consequences of the copper gradient, particularly genes involved in copper, iron, and sulfur homeostasis.	Copper	201-207	Cup2p	Saccharomyces cerevisiae S288C	116-120
23019066-5	2012	Plastically expressed genes included both genes regulated directly by copper-binding transcription factors Mac1 and Ace1 and genes indirectly responding to the downstream metabolic consequences of the copper gradient, particularly genes involved in copper, iron, and sulfur homeostasis.	Iron	257-261	Cup2p	Saccharomyces cerevisiae S288C	116-120
23019066-5	2012	Plastically expressed genes included both genes regulated directly by copper-binding transcription factors Mac1 and Ace1 and genes indirectly responding to the downstream metabolic consequences of the copper gradient, particularly genes involved in copper, iron, and sulfur homeostasis.	Sulfur	267-273	Cup2p	Saccharomyces cerevisiae S288C	116-120
22446598-1	2011	Transcription factor Ace1 from Saccharomyces cerevisiae regulates the expression of target genes when the copper concentration reaches 200 iI levels.	Copper	106-112	Cup2p	Saccharomyces cerevisiae S288C	21-25
21180717-1	2011	The two opposing yeast copper regulators, Ace1 and Mac1, were converted into two fluorescent probes, Ace1-FRET and Mac1-FRET, which selectively and sensitively respond to Cu(+).	Copper	23-29	Cup2p	Saccharomyces cerevisiae S288C	42-46
21180717-1	2011	The two opposing yeast copper regulators, Ace1 and Mac1, were converted into two fluorescent probes, Ace1-FRET and Mac1-FRET, which selectively and sensitively respond to Cu(+).	Copper	23-29	Cup2p	Saccharomyces cerevisiae S288C	101-105
21180717-1	2011	The two opposing yeast copper regulators, Ace1 and Mac1, were converted into two fluorescent probes, Ace1-FRET and Mac1-FRET, which selectively and sensitively respond to Cu(+).	Copper	171-176	Cup2p	Saccharomyces cerevisiae S288C	42-46
21180717-1	2011	The two opposing yeast copper regulators, Ace1 and Mac1, were converted into two fluorescent probes, Ace1-FRET and Mac1-FRET, which selectively and sensitively respond to Cu(+).	Copper	171-176	Cup2p	Saccharomyces cerevisiae S288C	101-105
18227253-0	2008	The copper-dependent ACE1 transcription factor activates the transcription of the mco1 gene from the basidiomycete Phanerochaete chrysosporium.	Copper	4-10	Cup2p	Saccharomyces cerevisiae S288C	21-25
19944018-0	2009	Yeast copper-dependent transcription factor ACE1 enhanced copper stress tolerance in Arabidopsis.	Copper	6-12	Cup2p	Saccharomyces cerevisiae S288C	44-48
19944018-2	2009	Yeast transcription factor ACE1 functions as a sensor for copper and an inducer for the transcription of CUP1.	Copper	58-64	Cup2p	Saccharomyces cerevisiae S288C	27-31
19944018-3	2009	In addition, ACE1 can activate the transcription of superoxide dismutase gene (sod1) in response to copper.	Copper	100-106	Cup2p	Saccharomyces cerevisiae S288C	13-17
19944018-5	2009	Under high copper stress, the transgenic plants over-expressing ACE1 showed higher survival rate than the wild-type.	Copper	11-17	Cup2p	Saccharomyces cerevisiae S288C	64-68
19944018-6	2009	We also found that over-expression of ACE1 in Arabidopsis increased the activities of SOD and POD, which were beneficial to the cell in copper buffering.	Copper	136-142	Cup2p	Saccharomyces cerevisiae S288C	38-42
19944018-7	2009	Excess copper would suppress the expression of chlorophyll biosynthetic genes in Arabidopsis, RT-PCR analysis revealed that over-expression of ACE1 decrease the suppression.	Copper	7-13	Cup2p	Saccharomyces cerevisiae S288C	143-147
19944018-7	2009	Excess copper would suppress the expression of chlorophyll biosynthetic genes in Arabidopsis, RT-PCR analysis revealed that over-expression of ACE1 decrease the suppression.	Chlorophyll	47-58	Cup2p	Saccharomyces cerevisiae S288C	143-147
19944018-8	2009	Together, our results indicate that ACE1 may play an important role in response to copper stress in Arabidopsis.	Copper	83-89	Cup2p	Saccharomyces cerevisiae S288C	36-40
18227253-2	2008	In Saccharomyces cerevisiae, ACE1 activates the copper-dependent transcription of target genes through a DNA sequence element named ACE.	Copper	48-54	Cup2p	Saccharomyces cerevisiae S288C	29-33
18227253-8	2008	In addition, using a cell-free transcription system, we showed that in the presence of cuprous ion, Pc-ACE1 induces activation of the promoter of mco1, but not that of mco2.	mco1	146-150	Cup2p	Saccharomyces cerevisiae S288C	103-107
12578838-6	2003	Within this region, the first 61 amino acids of Cuf1 exhibit more overall homology to the Saccharomyces cerevisiae Ace1 copper-detoxifying factor (from residues 1 to 63) than to Mac1, its functional ortholog.	Copper	120-126	Cup2p	Saccharomyces cerevisiae S288C	115-119
21783616-0	2005	Evaluation of the role of Ace1 and Yap1 in cadmium absorption using the eukaryotic cell model Saccharomyces cerevisiae.	Cadmium	43-50	Cup2p	Saccharomyces cerevisiae S288C	26-30
21783616-3	2005	Looking a little further into the control mechanism, we have verified that the deficiency in Ace1 impaired cadmium transport significantly.	Cadmium	107-114	Cup2p	Saccharomyces cerevisiae S288C	93-97
21783616-7	2005	However, the mutant strain Ace1 deficient exhibited considerable amounts of glutathione.	Glutathione	76-87	Cup2p	Saccharomyces cerevisiae S288C	27-31
15515160-3	2004	When copper ions are present in the sample, the Ace1 protein activates the cup1 promoter located upstream from the gfpuv gene in plasmid pYEX-GFPuv, thus inducing the production of GFPuv.	Copper	5-11	Cup2p	Saccharomyces cerevisiae S288C	48-52
17657345-2	2006	Pc-ace1 encodes a predicted protein of 633 amino acids containing the copper-fist DNA binding domain typically found in fungal transcription factors such as Ace1, Mac1 and Haa1 from Saccharomyces cerevisiae.	Copper	70-76	Cup2p	Saccharomyces cerevisiae S288C	3-7
17657345-2	2006	Pc-ace1 encodes a predicted protein of 633 amino acids containing the copper-fist DNA binding domain typically found in fungal transcription factors such as Ace1, Mac1 and Haa1 from Saccharomyces cerevisiae.	Copper	70-76	Cup2p	Saccharomyces cerevisiae S288C	157-161
17657345-4	2006	A S. cerevisiae ace1 null mutant strain unable to grow in high-copper medium was fully complemented by transformation with the cDNA of Pc-ace1.	Copper	63-69	Cup2p	Saccharomyces cerevisiae S288C	16-20
17657345-5	2006	Moreover, Northern blot hybridization studies indicated that Pc-ace1 cDNA restores copper inducibility of the yeast cup 1 gene, which encodes the metal-binding protein metallothionein implicated in copper resistance.	Copper	83-89	Cup2p	Saccharomyces cerevisiae S288C	64-68
17657345-5	2006	Moreover, Northern blot hybridization studies indicated that Pc-ace1 cDNA restores copper inducibility of the yeast cup 1 gene, which encodes the metal-binding protein metallothionein implicated in copper resistance.	Metals	146-151	Cup2p	Saccharomyces cerevisiae S288C	64-68
17657345-5	2006	Moreover, Northern blot hybridization studies indicated that Pc-ace1 cDNA restores copper inducibility of the yeast cup 1 gene, which encodes the metal-binding protein metallothionein implicated in copper resistance.	Copper	198-204	Cup2p	Saccharomyces cerevisiae S288C	64-68
16278453-1	2005	Ace1 and Mac1 undergo reciprocal copper metalloregulation in yeast cells.	Copper	33-39	Cup2p	Saccharomyces cerevisiae S288C	0-4
16278453-3	2005	Cells undergoing a transition from copper-deficient to copper-sufficient conditions through a switch in the growth medium show a rapid inactivation of Mac1 and a corresponding rise in Ace1 activation.	Copper	35-41	Cup2p	Saccharomyces cerevisiae S288C	184-188
14511662-7	2003	However, the toxicity of cisplatin in cells with a disrupted gene for ACE1, a factor that regulates transcription of the yeast gene for metallothionein, was also significantly reduced by treatment with copper.	Cisplatin	25-34	Cup2p	Saccharomyces cerevisiae S288C	70-74
14511662-7	2003	However, the toxicity of cisplatin in cells with a disrupted gene for ACE1, a factor that regulates transcription of the yeast gene for metallothionein, was also significantly reduced by treatment with copper.	Copper	202-208	Cup2p	Saccharomyces cerevisiae S288C	70-74
12578838-8	2003	Furthermore, we show that Schizosaccharomyces pombe cuf1Delta mutant cells expressing the full-length S. cerevisiae Ace1 protein are hypersensitive to copper ions, with a concomitant up-regulation of CuSE-mediated gene expression in fission yeast.	Copper	151-157	Cup2p	Saccharomyces cerevisiae S288C	116-120
12578838-9	2003	Taken together, these studies reveal that S. cerevisiae Ace1 1-63 is functionally exchangeable with S. pombe Cuf1 1-61, and the nature of the amino acids located downstream of this amino-terminal conserved region may be crucial in dictating the type of regulatory response required to establish and maintain copper homeostasis.	Copper	308-314	Cup2p	Saccharomyces cerevisiae S288C	56-60
12578363-7	2003	A sequence that is highly homologous to those of the copper-responsive transcription factors ACE1 (Saccharomyces cerevisiae) and AMT1 (Candida glabrata) is present in the promoters of three maize Cu/ZnSod genes.	Copper	53-59	Cup2p	Saccharomyces cerevisiae S288C	93-97
12559980-0	2003	Nitroxyl-mediated disruption of thiol proteins: inhibition of the yeast transcription factor Ace1.	nitroxyl	0-8	Cup2p	Saccharomyces cerevisiae S288C	93-97
12559980-0	2003	Nitroxyl-mediated disruption of thiol proteins: inhibition of the yeast transcription factor Ace1.	Sulfhydryl Compounds	32-37	Cup2p	Saccharomyces cerevisiae S288C	93-97
12559980-5	2003	Herein, we have examined the effect of HNO on the thiol-containing, metal-responsive, yeast transcription factor Ace1 under a variety of cellular conditions as a means of delineating the chemistry of HNO interactions with this representative thiol protein.	Sulfhydryl Compounds	50-55	Cup2p	Saccharomyces cerevisiae S288C	113-117
12559980-5	2003	Herein, we have examined the effect of HNO on the thiol-containing, metal-responsive, yeast transcription factor Ace1 under a variety of cellular conditions as a means of delineating the chemistry of HNO interactions with this representative thiol protein.	Metals	68-73	Cup2p	Saccharomyces cerevisiae S288C	113-117
12559980-5	2003	Herein, we have examined the effect of HNO on the thiol-containing, metal-responsive, yeast transcription factor Ace1 under a variety of cellular conditions as a means of delineating the chemistry of HNO interactions with this representative thiol protein.	Sulfhydryl Compounds	242-247	Cup2p	Saccharomyces cerevisiae S288C	113-117
12559980-6	2003	Using a reporter gene system, we find that HNO efficiently inhibits copper-dependent Ace1 activity.	Copper	68-74	Cup2p	Saccharomyces cerevisiae S288C	85-89
12559980-7	2003	Moreover, this inhibition appears to be a result of a direct interaction between Ace1 thiols and HNO and not a result of any chemistry associated with HNO-derived species.	nitroxyl	97-100	Cup2p	Saccharomyces cerevisiae S288C	81-85
12513977-2	2003	Deletion of ace1 resulted in an increase in the expression of all the main cellulase genes and two xylanase genes in sophorose- and cellulose-induced cultures, indicating that ACEI acts as a repressor of cellulase and xylanase expression.	Cellulose	132-141	Cup2p	Saccharomyces cerevisiae S288C	12-16
12513977-2	2003	Deletion of ace1 resulted in an increase in the expression of all the main cellulase genes and two xylanase genes in sophorose- and cellulose-induced cultures, indicating that ACEI acts as a repressor of cellulase and xylanase expression.	acei	176-180	Cup2p	Saccharomyces cerevisiae S288C	12-16
12513977-3	2003	Growth of the strain with a deletion of the ace1 gene on different carbon sources was analyzed.	Carbon	67-73	Cup2p	Saccharomyces cerevisiae S288C	44-48
12513977-5	2003	On culture media containing sorbitol as the sole carbon source, the growth of the strain with a deletion of the ace1 gene was severely impaired, suggesting that ACEI regulates expression of other genes in addition to cellulase and xylanase genes.	Sorbitol	28-36	Cup2p	Saccharomyces cerevisiae S288C	112-116
11743740-4	2001	Exposure of yeast to various nitrogen oxides, under a variety of conditions, revealed that the oxygen-dependent inhibition of Ace1 is due to the reaction of NO with O(2).	Oxygen	95-101	Cup2p	Saccharomyces cerevisiae S288C	126-130
12009910-0	2002	Structures of the cuprous-thiolate clusters of the Mac1 and Ace1 transcriptional activators.	cuprous-thiolate	18-34	Cup2p	Saccharomyces cerevisiae S288C	60-64
12009910-1	2002	X-ray absorption spectroscopy on the minimal copper-regulatory domains of the two copper-regulated transcription factors (Ace1 and Mac1) in Saccharomyces cerevisiae revealed the presence of a remarkably similar polycopper cluster in both proteins.	Copper	45-51	Cup2p	Saccharomyces cerevisiae S288C	122-126
12009910-2	2002	The Cu-regulatory switch motif of Mac1 consisting of the C-terminal first Cys-rich motif, designated the C1 domain, binds four Cu(I) ions as does the Cu-regulatory domain of Ace1.	Cysteine	74-77	Cup2p	Saccharomyces cerevisiae S288C	174-178
12009910-7	2002	The tetracopper clusters bound by Ace1 and Mac1 differ in that the Ace1 cluster is coordinated entirely by cysteinyl thiolate, whereas the cysteine-deficient Mac1 cluster appears to consist of a Cu(4)(S-Cys)(5)(N-His) cluster with a bridging histidyl-derived nitrogen.	cysteinyl thiolate	107-125	Cup2p	Saccharomyces cerevisiae S288C	34-38
12009910-7	2002	The tetracopper clusters bound by Ace1 and Mac1 differ in that the Ace1 cluster is coordinated entirely by cysteinyl thiolate, whereas the cysteine-deficient Mac1 cluster appears to consist of a Cu(4)(S-Cys)(5)(N-His) cluster with a bridging histidyl-derived nitrogen.	cysteinyl thiolate	107-125	Cup2p	Saccharomyces cerevisiae S288C	67-71
12009910-7	2002	The tetracopper clusters bound by Ace1 and Mac1 differ in that the Ace1 cluster is coordinated entirely by cysteinyl thiolate, whereas the cysteine-deficient Mac1 cluster appears to consist of a Cu(4)(S-Cys)(5)(N-His) cluster with a bridging histidyl-derived nitrogen.	Cysteine	139-147	Cup2p	Saccharomyces cerevisiae S288C	34-38
12009910-7	2002	The tetracopper clusters bound by Ace1 and Mac1 differ in that the Ace1 cluster is coordinated entirely by cysteinyl thiolate, whereas the cysteine-deficient Mac1 cluster appears to consist of a Cu(4)(S-Cys)(5)(N-His) cluster with a bridging histidyl-derived nitrogen.	Copper	195-197	Cup2p	Saccharomyces cerevisiae S288C	34-38
12009910-7	2002	The tetracopper clusters bound by Ace1 and Mac1 differ in that the Ace1 cluster is coordinated entirely by cysteinyl thiolate, whereas the cysteine-deficient Mac1 cluster appears to consist of a Cu(4)(S-Cys)(5)(N-His) cluster with a bridging histidyl-derived nitrogen.	Cysteine	201-206	Cup2p	Saccharomyces cerevisiae S288C	34-38
12009910-7	2002	The tetracopper clusters bound by Ace1 and Mac1 differ in that the Ace1 cluster is coordinated entirely by cysteinyl thiolate, whereas the cysteine-deficient Mac1 cluster appears to consist of a Cu(4)(S-Cys)(5)(N-His) cluster with a bridging histidyl-derived nitrogen.	n-his	211-216	Cup2p	Saccharomyces cerevisiae S288C	34-38
12009910-7	2002	The tetracopper clusters bound by Ace1 and Mac1 differ in that the Ace1 cluster is coordinated entirely by cysteinyl thiolate, whereas the cysteine-deficient Mac1 cluster appears to consist of a Cu(4)(S-Cys)(5)(N-His) cluster with a bridging histidyl-derived nitrogen.	histidyl	242-250	Cup2p	Saccharomyces cerevisiae S288C	34-38
12009910-7	2002	The tetracopper clusters bound by Ace1 and Mac1 differ in that the Ace1 cluster is coordinated entirely by cysteinyl thiolate, whereas the cysteine-deficient Mac1 cluster appears to consist of a Cu(4)(S-Cys)(5)(N-His) cluster with a bridging histidyl-derived nitrogen.	Nitrogen	259-267	Cup2p	Saccharomyces cerevisiae S288C	34-38
11743740-0	2001	Mechanisms of nitrogen oxide-mediated disruption of metalloprotein function: an examination of the copper-responsive yeast transcription factor Ace1.	Nitrogen Oxides	14-28	Cup2p	Saccharomyces cerevisiae S288C	144-148
11743740-0	2001	Mechanisms of nitrogen oxide-mediated disruption of metalloprotein function: an examination of the copper-responsive yeast transcription factor Ace1.	Copper	99-105	Cup2p	Saccharomyces cerevisiae S288C	144-148
11743740-1	2001	Nitric oxide (NO) has been found to inhibit the copper-responsive yeast transcription factor Ace1 in an oxygen-dependent manner.	Nitric Oxide	0-12	Cup2p	Saccharomyces cerevisiae S288C	93-97
11743740-1	2001	Nitric oxide (NO) has been found to inhibit the copper-responsive yeast transcription factor Ace1 in an oxygen-dependent manner.	Copper	48-54	Cup2p	Saccharomyces cerevisiae S288C	93-97
11743740-4	2001	Exposure of yeast to various nitrogen oxides, under a variety of conditions, revealed that the oxygen-dependent inhibition of Ace1 is due to the reaction of NO with O(2).	Oxygen	165-169	Cup2p	Saccharomyces cerevisiae S288C	126-130
11743740-1	2001	Nitric oxide (NO) has been found to inhibit the copper-responsive yeast transcription factor Ace1 in an oxygen-dependent manner.	Oxygen	104-110	Cup2p	Saccharomyces cerevisiae S288C	93-97
11743740-3	2001	In the present study, the chemical interaction of nitrogen oxide species with Ace1 was examined using a yeast reporter system.	Nitrogen Oxides	50-64	Cup2p	Saccharomyces cerevisiae S288C	78-82
11743740-5	2001	The nitrosating nitrogen oxide species N(2)O(3) is likely to be the disrupter of Ace1 activity.	Nitrogen Oxides	16-30	Cup2p	Saccharomyces cerevisiae S288C	81-85
11743740-4	2001	Exposure of yeast to various nitrogen oxides, under a variety of conditions, revealed that the oxygen-dependent inhibition of Ace1 is due to the reaction of NO with O(2).	Nitrogen Oxides	29-44	Cup2p	Saccharomyces cerevisiae S288C	126-130
11743740-5	2001	The nitrosating nitrogen oxide species N(2)O(3) is likely to be the disrupter of Ace1 activity.	Nitrogen	39-40	Cup2p	Saccharomyces cerevisiae S288C	81-85
11278870-0	2001	The fission yeast copper-sensing transcription factor Cuf1 regulates the copper transporter gene expression through an Ace1/Amt1-like recognition sequence.	Copper	18-24	Cup2p	Saccharomyces cerevisiae S288C	119-123
11504737-11	2001	The lack of metalloregulation of Haa1 despite the strong sequence similarity to the copper regulatory domain of Ace1 is discussed.	Copper	84-90	Cup2p	Saccharomyces cerevisiae S288C	112-116
11278870-4	2001	Interestingly, the CuSE element bears a strong sequence similarity to the recognition site, denoted MRE (metal regulatory element), which is recognized by a distinct class of copper sensors required for copper detoxification, including Ace1 from Saccharomyces cerevisiae and Amt1 from Candida glabrata.	Metals	105-110	Cup2p	Saccharomyces cerevisiae S288C	236-240
11278870-4	2001	Interestingly, the CuSE element bears a strong sequence similarity to the recognition site, denoted MRE (metal regulatory element), which is recognized by a distinct class of copper sensors required for copper detoxification, including Ace1 from Saccharomyces cerevisiae and Amt1 from Candida glabrata.	Copper	175-181	Cup2p	Saccharomyces cerevisiae S288C	236-240
11278870-4	2001	Interestingly, the CuSE element bears a strong sequence similarity to the recognition site, denoted MRE (metal regulatory element), which is recognized by a distinct class of copper sensors required for copper detoxification, including Ace1 from Saccharomyces cerevisiae and Amt1 from Candida glabrata.	Copper	203-209	Cup2p	Saccharomyces cerevisiae S288C	236-240
11278870-7	2001	These results demonstrate that the Cuf1 nutritional copper-sensing factor possesses a module that functions similarly to domains found in the Ace1/Amt1 class of metalloregulatory factors, which allows the protein to act through a closely related MRE-like sequence to regulate copper transport gene expression in S. pombe.	Copper	52-58	Cup2p	Saccharomyces cerevisiae S288C	142-146
11278870-7	2001	These results demonstrate that the Cuf1 nutritional copper-sensing factor possesses a module that functions similarly to domains found in the Ace1/Amt1 class of metalloregulatory factors, which allows the protein to act through a closely related MRE-like sequence to regulate copper transport gene expression in S. pombe.	Copper	276-282	Cup2p	Saccharomyces cerevisiae S288C	142-146
11297016-4	2001	It has been reported that the induction for the transcription of CUP1 by copper and silver is mediated by the Ace1 transcription factor.	Copper	73-79	Cup2p	Saccharomyces cerevisiae S288C	110-114
11134341-1	2001	The yeast CUP1 gene is activated by the copper-dependent binding of the transcriptional activator, Ace1p.	Copper	40-46	Cup2p	Saccharomyces cerevisiae S288C	99-104
11297016-5	2001	However, the expression of the gene by cobalt occurred in yeast cells lacking the Ace1 factor.	Cobalt	39-45	Cup2p	Saccharomyces cerevisiae S288C	82-86
10845707-0	2000	Effects of nitric oxide on the copper-responsive transcription factor Ace1 in Saccharomyces cerevisiae: cytotoxic and cytoprotective actions of nitric oxide.	Copper	31-37	Cup2p	Saccharomyces cerevisiae S288C	70-74
10922376-1	2000	In Saccharomyces cerevisiae, copper ions regulate gene expression through the two transcriptional activators, Ace1 and Mac1.	Copper	29-35	Cup2p	Saccharomyces cerevisiae S288C	110-114
10922376-2	2000	Ace1 mediates copper-induced gene expression in cells exposed to stressful levels of copper salts, whereas Mac1 activates a subset of genes under copper-deficient conditions.	Copper	14-20	Cup2p	Saccharomyces cerevisiae S288C	0-4
10922376-2	2000	Ace1 mediates copper-induced gene expression in cells exposed to stressful levels of copper salts, whereas Mac1 activates a subset of genes under copper-deficient conditions.	Copper	85-91	Cup2p	Saccharomyces cerevisiae S288C	0-4
10845707-0	2000	Effects of nitric oxide on the copper-responsive transcription factor Ace1 in Saccharomyces cerevisiae: cytotoxic and cytoprotective actions of nitric oxide.	Nitric Oxide	144-156	Cup2p	Saccharomyces cerevisiae S288C	70-74
9599102-2	1998	In Saccharomyces cerevisiae, the nutritional copper sensor Mac1p regulates the copper-dependent expression of the high affinity Cu(I) uptake genes CTR1, CTR3, and FRE1, while the toxic copper sensor Ace1p regulates the transcriptional activation of the detoxification genes CUP1, CRS5, and SOD1 in response to copper.	Copper	79-85	Cup2p	Saccharomyces cerevisiae S288C	199-204
10694579-0	2000	The interaction of nitric oxide (NO) with the yeast transcription factor Ace1: A model system for NO-protein thiol interactions with implications to metal metabolism.	Nitric Oxide	19-31	Cup2p	Saccharomyces cerevisiae S288C	73-77
10694579-0	2000	The interaction of nitric oxide (NO) with the yeast transcription factor Ace1: A model system for NO-protein thiol interactions with implications to metal metabolism.	Sulfhydryl Compounds	109-114	Cup2p	Saccharomyces cerevisiae S288C	73-77
10694579-0	2000	The interaction of nitric oxide (NO) with the yeast transcription factor Ace1: A model system for NO-protein thiol interactions with implications to metal metabolism.	Metals	149-154	Cup2p	Saccharomyces cerevisiae S288C	73-77
10694579-2	2000	This effect is attributable to an inhibition of the copper-responsive CUP1 transcriptional activator Ace1.	Copper	52-58	Cup2p	Saccharomyces cerevisiae S288C	101-105
10694579-3	2000	A mechanism is proposed whereby the metal binding thiols of Ace1 are chemically modified via NO- and O(2)-dependent chemistry, thereby diminishing the ability of Ace1 to bind and respond to copper.	Metals	36-41	Cup2p	Saccharomyces cerevisiae S288C	60-64
10694579-3	2000	A mechanism is proposed whereby the metal binding thiols of Ace1 are chemically modified via NO- and O(2)-dependent chemistry, thereby diminishing the ability of Ace1 to bind and respond to copper.	Metals	36-41	Cup2p	Saccharomyces cerevisiae S288C	162-166
10694579-3	2000	A mechanism is proposed whereby the metal binding thiols of Ace1 are chemically modified via NO- and O(2)-dependent chemistry, thereby diminishing the ability of Ace1 to bind and respond to copper.	Sulfhydryl Compounds	50-56	Cup2p	Saccharomyces cerevisiae S288C	60-64
10694579-3	2000	A mechanism is proposed whereby the metal binding thiols of Ace1 are chemically modified via NO- and O(2)-dependent chemistry, thereby diminishing the ability of Ace1 to bind and respond to copper.	Sulfhydryl Compounds	50-56	Cup2p	Saccharomyces cerevisiae S288C	162-166
10694579-3	2000	A mechanism is proposed whereby the metal binding thiols of Ace1 are chemically modified via NO- and O(2)-dependent chemistry, thereby diminishing the ability of Ace1 to bind and respond to copper.	o(2)	101-105	Cup2p	Saccharomyces cerevisiae S288C	60-64
10694579-3	2000	A mechanism is proposed whereby the metal binding thiols of Ace1 are chemically modified via NO- and O(2)-dependent chemistry, thereby diminishing the ability of Ace1 to bind and respond to copper.	o(2)	101-105	Cup2p	Saccharomyces cerevisiae S288C	162-166
10694579-3	2000	A mechanism is proposed whereby the metal binding thiols of Ace1 are chemically modified via NO- and O(2)-dependent chemistry, thereby diminishing the ability of Ace1 to bind and respond to copper.	Copper	190-196	Cup2p	Saccharomyces cerevisiae S288C	60-64
10694579-3	2000	A mechanism is proposed whereby the metal binding thiols of Ace1 are chemically modified via NO- and O(2)-dependent chemistry, thereby diminishing the ability of Ace1 to bind and respond to copper.	Copper	190-196	Cup2p	Saccharomyces cerevisiae S288C	162-166
10694579-4	2000	Moreover, it is proposed that demetallated Ace1 is proteolytically degraded in the cell, resulting in a prolonged inhibition of copper-dependent CUP1 induction.	Copper	128-134	Cup2p	Saccharomyces cerevisiae S288C	43-47
9599102-2	1998	In Saccharomyces cerevisiae, the nutritional copper sensor Mac1p regulates the copper-dependent expression of the high affinity Cu(I) uptake genes CTR1, CTR3, and FRE1, while the toxic copper sensor Ace1p regulates the transcriptional activation of the detoxification genes CUP1, CRS5, and SOD1 in response to copper.	Copper	45-51	Cup2p	Saccharomyces cerevisiae S288C	199-204
9599102-2	1998	In Saccharomyces cerevisiae, the nutritional copper sensor Mac1p regulates the copper-dependent expression of the high affinity Cu(I) uptake genes CTR1, CTR3, and FRE1, while the toxic copper sensor Ace1p regulates the transcriptional activation of the detoxification genes CUP1, CRS5, and SOD1 in response to copper.	Copper	79-85	Cup2p	Saccharomyces cerevisiae S288C	199-204
9599102-2	1998	In Saccharomyces cerevisiae, the nutritional copper sensor Mac1p regulates the copper-dependent expression of the high affinity Cu(I) uptake genes CTR1, CTR3, and FRE1, while the toxic copper sensor Ace1p regulates the transcriptional activation of the detoxification genes CUP1, CRS5, and SOD1 in response to copper.	Copper	79-85	Cup2p	Saccharomyces cerevisiae S288C	199-204
9599102-2	1998	In Saccharomyces cerevisiae, the nutritional copper sensor Mac1p regulates the copper-dependent expression of the high affinity Cu(I) uptake genes CTR1, CTR3, and FRE1, while the toxic copper sensor Ace1p regulates the transcriptional activation of the detoxification genes CUP1, CRS5, and SOD1 in response to copper.	cuprous ion	128-133	Cup2p	Saccharomyces cerevisiae S288C	199-204
9599102-4	1998	Upon addition of CuSO4, mRNA levels of CTR3 were rapidly reduced to eightfold the original basal level whereas the Ace1p-mediated transcriptional activation of CUP1 was rapid and potent but transient.	Copper Sulfate	17-22	Cup2p	Saccharomyces cerevisiae S288C	115-120
9599102-6	1998	In vivo dimethyl sulfate footprinting analysis of the CUP1 promoter demonstrated transient occupation of the metal response elements by Ace1p which paralleled CUP1 mRNA expression.	dimethyl sulfate	8-24	Cup2p	Saccharomyces cerevisiae S288C	136-141
9599102-6	1998	In vivo dimethyl sulfate footprinting analysis of the CUP1 promoter demonstrated transient occupation of the metal response elements by Ace1p which paralleled CUP1 mRNA expression.	Metals	109-114	Cup2p	Saccharomyces cerevisiae S288C	136-141
9599102-8	1998	These studies (i) demonstrate that the nutritional and toxic copper metalloregulatory transcription factors Mac1p and Ace1p must sense and respond to copper ions in a dynamic fashion to appropriately regulate copper ion homeostasis and (ii) establish the requirement for a wild-type Mac1p for survival in the presence of toxic copper levels.	Copper	61-67	Cup2p	Saccharomyces cerevisiae S288C	118-123
9599102-8	1998	These studies (i) demonstrate that the nutritional and toxic copper metalloregulatory transcription factors Mac1p and Ace1p must sense and respond to copper ions in a dynamic fashion to appropriately regulate copper ion homeostasis and (ii) establish the requirement for a wild-type Mac1p for survival in the presence of toxic copper levels.	Copper	150-156	Cup2p	Saccharomyces cerevisiae S288C	118-123
9599102-8	1998	These studies (i) demonstrate that the nutritional and toxic copper metalloregulatory transcription factors Mac1p and Ace1p must sense and respond to copper ions in a dynamic fashion to appropriately regulate copper ion homeostasis and (ii) establish the requirement for a wild-type Mac1p for survival in the presence of toxic copper levels.	Copper	150-156	Cup2p	Saccharomyces cerevisiae S288C	118-123
9599102-8	1998	These studies (i) demonstrate that the nutritional and toxic copper metalloregulatory transcription factors Mac1p and Ace1p must sense and respond to copper ions in a dynamic fashion to appropriately regulate copper ion homeostasis and (ii) establish the requirement for a wild-type Mac1p for survival in the presence of toxic copper levels.	Copper	150-156	Cup2p	Saccharomyces cerevisiae S288C	118-123
8634288-1	1996	The N-terminal metal-binding domains of the copper-activated yeast transcription factors, ACE1 and AMT1, bind to specific DNA sequences in a Cu-dependent fashion.	Metals	15-20	Cup2p	Saccharomyces cerevisiae S288C	90-94
8866892-4	1996	After addition of copper ions to the plant nutrient solution, beta-glucuronidase (GUS) expression was visualized either specifically in nodules or in both roots and nodules when the ace1 gene was placed under control of the nod45 promoter or the CaMV 35S RNA promoter, respectively.	Copper	18-24	Cup2p	Saccharomyces cerevisiae S288C	182-186
8634288-12	1996	The sequence homology between AMT1, ACE1, and MAC1 in the N-terminal 42 residues suggests that ACE1 and MAC1 will, likewise, contain N-terminal Zn modules.	Zinc	144-146	Cup2p	Saccharomyces cerevisiae S288C	95-99
9308366-9	1998	Cu(I) triggering may involve a metal exchange reaction converting Ace1 from a Zn(II)-specific conformer to a clustered Cu(I) conformer.	Copper	0-2	Cup2p	Saccharomyces cerevisiae S288C	66-70
9308366-9	1998	Cu(I) triggering may involve a metal exchange reaction converting Ace1 from a Zn(II)-specific conformer to a clustered Cu(I) conformer.	Metals	31-36	Cup2p	Saccharomyces cerevisiae S288C	66-70
9308366-9	1998	Cu(I) triggering may involve a metal exchange reaction converting Ace1 from a Zn(II)-specific conformer to a clustered Cu(I) conformer.	Zinc	78-84	Cup2p	Saccharomyces cerevisiae S288C	66-70
9308366-9	1998	Cu(I) triggering may involve a metal exchange reaction converting Ace1 from a Zn(II)-specific conformer to a clustered Cu(I) conformer.	cuprous ion	0-5	Cup2p	Saccharomyces cerevisiae S288C	66-70
8634288-13	1996	A 42-residue ACE1 synthetic peptide gives identical metal binding properties to the corresponding AMT1 synthetic peptide.	Metals	52-57	Cup2p	Saccharomyces cerevisiae S288C	13-17
8634288-1	1996	The N-terminal metal-binding domains of the copper-activated yeast transcription factors, ACE1 and AMT1, bind to specific DNA sequences in a Cu-dependent fashion.	Copper	44-50	Cup2p	Saccharomyces cerevisiae S288C	90-94
8634288-1	1996	The N-terminal metal-binding domains of the copper-activated yeast transcription factors, ACE1 and AMT1, bind to specific DNA sequences in a Cu-dependent fashion.	Copper	141-143	Cup2p	Saccharomyces cerevisiae S288C	90-94
8634288-2	1996	Recombinant AMT1 and ACE1 metal-binding domains are isolated as Cu4Zn1-protein complexes.	Metals	26-31	Cup2p	Saccharomyces cerevisiae S288C	21-25
8634288-4	1996	The results are consistent with the N-terminal halves of AMT1 and ACE1 consisting of two independent submodules, one binding a single Zn(II) ion and the second binding the tetracopper cluster.	Zinc	134-140	Cup2p	Saccharomyces cerevisiae S288C	66-70
8634288-12	1996	The sequence homology between AMT1, ACE1, and MAC1 in the N-terminal 42 residues suggests that ACE1 and MAC1 will, likewise, contain N-terminal Zn modules.	Zinc	144-146	Cup2p	Saccharomyces cerevisiae S288C	36-40
7929283-2	1994	In Saccharomyces cerevisiae Cu,Zn-superoxide dismutase is coregulated with copper-thionein by copper via the transcription factor ACE 1.	Copper	75-81	Cup2p	Saccharomyces cerevisiae S288C	130-135
8585324-4	1995	G1810 is identical to the ACE1 gene sequenced by Szczypka and Thiele (1989), required for copper-inducible transcription of the CUP1 gene.	Copper	90-96	Cup2p	Saccharomyces cerevisiae S288C	26-30
27405549-7	1995	The identification of a number of transcription factors (Yap1, Mac1, Ace1) which are important in the regulation of metal metabolism and homeostasis that are also involved in mediating resistance towards oxidants suggests a link between metal metabolism and oxidative stress.	Metals	116-121	Cup2p	Saccharomyces cerevisiae S288C	69-73
27405549-7	1995	The identification of a number of transcription factors (Yap1, Mac1, Ace1) which are important in the regulation of metal metabolism and homeostasis that are also involved in mediating resistance towards oxidants suggests a link between metal metabolism and oxidative stress.	Metals	237-242	Cup2p	Saccharomyces cerevisiae S288C	69-73
7969120-1	1994	Yeast metallothionein, encoded by the CUP1 gene, and its copper-dependent transcriptional activator ACE1 play a key role in mediating copper resistance in Saccharomyces cerevisiae.	Copper	57-63	Cup2p	Saccharomyces cerevisiae S288C	100-104
7969120-1	1994	Yeast metallothionein, encoded by the CUP1 gene, and its copper-dependent transcriptional activator ACE1 play a key role in mediating copper resistance in Saccharomyces cerevisiae.	Copper	134-140	Cup2p	Saccharomyces cerevisiae S288C	100-104
7969120-2	1994	Using an ethyl methanesulfonate mutant of a yeast strain in which CUP1 and ACE1 were deleted, we isolated a gene, designated CUP9, which permits yeast cells to grow at high concentrations of environmental copper, most notably when lactate is the sole carbon source.	Ethyl Methanesulfonate	9-31	Cup2p	Saccharomyces cerevisiae S288C	75-79
7969120-2	1994	Using an ethyl methanesulfonate mutant of a yeast strain in which CUP1 and ACE1 were deleted, we isolated a gene, designated CUP9, which permits yeast cells to grow at high concentrations of environmental copper, most notably when lactate is the sole carbon source.	Copper	205-211	Cup2p	Saccharomyces cerevisiae S288C	75-79
7969120-2	1994	Using an ethyl methanesulfonate mutant of a yeast strain in which CUP1 and ACE1 were deleted, we isolated a gene, designated CUP9, which permits yeast cells to grow at high concentrations of environmental copper, most notably when lactate is the sole carbon source.	Lactic Acid	231-238	Cup2p	Saccharomyces cerevisiae S288C	75-79
7969120-2	1994	Using an ethyl methanesulfonate mutant of a yeast strain in which CUP1 and ACE1 were deleted, we isolated a gene, designated CUP9, which permits yeast cells to grow at high concentrations of environmental copper, most notably when lactate is the sole carbon source.	Carbon	251-257	Cup2p	Saccharomyces cerevisiae S288C	75-79
7969120-3	1994	Disruption of CUP9, which is located on chromosome XVI, caused a loss of copper resistance in strains which possessed CUP1 and ACE1, as well as in the cup1 ace1 deletion strain.	Copper	73-79	Cup2p	Saccharomyces cerevisiae S288C	127-131
8530401-6	1995	The Saccharomyces cerevisiae SOD1 gene is transcriptionally induced by copper and the ACE1 transactivator, and we demonstrate here that this induction of SOD1 promotes protection against copper toxicity but is not needed for the SOD1-protection against oxygen free radicals.	Copper	187-193	Cup2p	Saccharomyces cerevisiae S288C	86-90
7766204-6	1995	Although transcription of CUP1 is inducible by metals, the ACE1 protein serves a dual function as a sensor for copper and an inducer for CUP1 transcription in the copper-resistant strain.	Copper	111-117	Cup2p	Saccharomyces cerevisiae S288C	59-63
7766204-6	1995	Although transcription of CUP1 is inducible by metals, the ACE1 protein serves a dual function as a sensor for copper and an inducer for CUP1 transcription in the copper-resistant strain.	Copper	163-169	Cup2p	Saccharomyces cerevisiae S288C	59-63
8017099-11	1994	In contrast, at high copper doses, elevated levels of the ACE1 protein resulted in inferior hirudin production.	Copper	21-27	Cup2p	Saccharomyces cerevisiae S288C	58-62
8343519-0	1993	Distinct metal binding configurations in ACE1.	Metals	9-14	Cup2p	Saccharomyces cerevisiae S288C	41-45
8262047-1	1993	The related transcription factors ACE1 of Saccharomyces cerevisiae and AMT1 of Candida glabrata are involved in copper metabolism by activating the transcription of copper metallothionein genes.	Copper	112-118	Cup2p	Saccharomyces cerevisiae S288C	34-38
8262047-2	1993	ACE1 and AMT1 are "copper-fist" transcription factors which possess a conserved cysteine-rich copper binding domain required for DNA binding.	Cysteine	80-88	Cup2p	Saccharomyces cerevisiae S288C	0-4
8262047-2	1993	ACE1 and AMT1 are "copper-fist" transcription factors which possess a conserved cysteine-rich copper binding domain required for DNA binding.	Copper	19-25	Cup2p	Saccharomyces cerevisiae S288C	0-4
8262047-3	1993	Here we report the identification of a nuclear protein from S. cerevisiae, MAC1, whose N-terminal region is highly similar to the copper and DNA binding domains of ACE1 and AMT1.	Copper	130-136	Cup2p	Saccharomyces cerevisiae S288C	164-168
8370529-3	1993	AMT1 shares several structural and functional features with the Saccharomyces cerevisiae copper metalloregulatory transcription factor ACE1, which is constitutively expressed and poised for rapid transcriptional responses to the toxic metal copper.	Metals	96-101	Cup2p	Saccharomyces cerevisiae S288C	135-139
8370529-3	1993	AMT1 shares several structural and functional features with the Saccharomyces cerevisiae copper metalloregulatory transcription factor ACE1, which is constitutively expressed and poised for rapid transcriptional responses to the toxic metal copper.	Copper	89-95	Cup2p	Saccharomyces cerevisiae S288C	135-139
8343519-1	1993	The ACE1 protein of Saccharomyces cerevisiae mediates the metal-induced expression of the CUP1 metallothionein (MT) genes.	Metals	58-63	Cup2p	Saccharomyces cerevisiae S288C	4-8
8343519-2	1993	Curiously, ACE1 resembles the MT protein in the types of metal complexes that form.	Metals	57-62	Cup2p	Saccharomyces cerevisiae S288C	11-15
8343519-3	1993	ACE1 binds Cd(II) and Cu(I) ions in distinct configurations, but only the Cu(I) conformer of ACE1 forms a high-affinity and specific complex with DNA.	cd(ii)	11-17	Cup2p	Saccharomyces cerevisiae S288C	0-4
8343519-3	1993	ACE1 binds Cd(II) and Cu(I) ions in distinct configurations, but only the Cu(I) conformer of ACE1 forms a high-affinity and specific complex with DNA.	cuprous ion	22-27	Cup2p	Saccharomyces cerevisiae S288C	0-4
8343519-3	1993	ACE1 binds Cd(II) and Cu(I) ions in distinct configurations, but only the Cu(I) conformer of ACE1 forms a high-affinity and specific complex with DNA.	cuprous ion	74-79	Cup2p	Saccharomyces cerevisiae S288C	93-97
8343519-4	1993	Cu(I) ions associated with ACE1 are known to assemble in a polymetallic CuI-thiolate cluster that resembles Cu-metallothionein in metal coordination properties [Dameron, C. T., Winge, D. R., George, G. N., Sansone, M., Hu, S., & Hamer, D. (1991) Proc.	Copper	0-2	Cup2p	Saccharomyces cerevisiae S288C	27-31
8343519-4	1993	Cu(I) ions associated with ACE1 are known to assemble in a polymetallic CuI-thiolate cluster that resembles Cu-metallothionein in metal coordination properties [Dameron, C. T., Winge, D. R., George, G. N., Sansone, M., Hu, S., & Hamer, D. (1991) Proc.	cui-thiolate	72-84	Cup2p	Saccharomyces cerevisiae S288C	27-31
8343519-4	1993	Cu(I) ions associated with ACE1 are known to assemble in a polymetallic CuI-thiolate cluster that resembles Cu-metallothionein in metal coordination properties [Dameron, C. T., Winge, D. R., George, G. N., Sansone, M., Hu, S., & Hamer, D. (1991) Proc.	cu-metallothionein	108-126	Cup2p	Saccharomyces cerevisiae S288C	27-31
8343519-4	1993	Cu(I) ions associated with ACE1 are known to assemble in a polymetallic CuI-thiolate cluster that resembles Cu-metallothionein in metal coordination properties [Dameron, C. T., Winge, D. R., George, G. N., Sansone, M., Hu, S., & Hamer, D. (1991) Proc.	Metals	63-68	Cup2p	Saccharomyces cerevisiae S288C	27-31
8343519-9	1993	In contrast to the Cu(I) nuclearity of 6-7 mol equiv in ACE1 and 7 mol equiv in yeast MT, divalent ions, including Cd(II), Zn(II) and Co(II), bind with a maximal stoichiometry of near 4 mol equiv in ACE1 and 4 mol equiv in yeast MT.	cd(ii)	115-121	Cup2p	Saccharomyces cerevisiae S288C	199-209
8343519-13	1993	Metal binding in ACE1 is clearly similar to that in MT, and therefore the MT-metal clusters appear to be a good structural model of the metal center of ACE1.	Metals	0-5	Cup2p	Saccharomyces cerevisiae S288C	17-21
8343519-13	1993	Metal binding in ACE1 is clearly similar to that in MT, and therefore the MT-metal clusters appear to be a good structural model of the metal center of ACE1.	Metals	0-5	Cup2p	Saccharomyces cerevisiae S288C	152-156
8343519-13	1993	Metal binding in ACE1 is clearly similar to that in MT, and therefore the MT-metal clusters appear to be a good structural model of the metal center of ACE1.	Metals	77-82	Cup2p	Saccharomyces cerevisiae S288C	17-21
8343519-13	1993	Metal binding in ACE1 is clearly similar to that in MT, and therefore the MT-metal clusters appear to be a good structural model of the metal center of ACE1.	Metals	77-82	Cup2p	Saccharomyces cerevisiae S288C	152-156
8343519-13	1993	Metal binding in ACE1 is clearly similar to that in MT, and therefore the MT-metal clusters appear to be a good structural model of the metal center of ACE1.	Metals	136-141	Cup2p	Saccharomyces cerevisiae S288C	17-21
8343519-13	1993	Metal binding in ACE1 is clearly similar to that in MT, and therefore the MT-metal clusters appear to be a good structural model of the metal center of ACE1.	Metals	136-141	Cup2p	Saccharomyces cerevisiae S288C	152-156
8509391-1	1993	The AMT1 metalloregulatory trans-acting factor from Candida glabrata was found to functionally mimic the ACE1 metalloregulatory trans-acting factor from Saccharomyces cerevisiae in the copper-induced expression of the chromosomal S. cerevisiae metallothionein gene.	Copper	185-191	Cup2p	Saccharomyces cerevisiae S288C	105-109
8509391-6	1993	The regulation mediated by both ACE1 and AMT1 was copper-dependent and copper-specific.	Copper	50-56	Cup2p	Saccharomyces cerevisiae S288C	32-36
8509391-6	1993	The regulation mediated by both ACE1 and AMT1 was copper-dependent and copper-specific.	Copper	71-77	Cup2p	Saccharomyces cerevisiae S288C	32-36
8509391-9	1993	In conclusion, AMT1 and ACE1 are functionally homologous in metal-specific regulation, AMT1 appears to be more promiscuous than ACE1 in this function.	Metals	60-65	Cup2p	Saccharomyces cerevisiae S288C	24-28
8509391-9	1993	In conclusion, AMT1 and ACE1 are functionally homologous in metal-specific regulation, AMT1 appears to be more promiscuous than ACE1 in this function.	Metals	60-65	Cup2p	Saccharomyces cerevisiae S288C	128-132
8347274-5	1993	The copper MRTFs, ACE1 from S.cerevisiae and AMT1 from C.glabrata, directly interact with specific copper-responsive cis-acting elements in the promotor regions of their respective target genes.	Copper	4-10	Cup2p	Saccharomyces cerevisiae S288C	18-22
8347274-5	1993	The copper MRTFs, ACE1 from S.cerevisiae and AMT1 from C.glabrata, directly interact with specific copper-responsive cis-acting elements in the promotor regions of their respective target genes.	Copper	99-105	Cup2p	Saccharomyces cerevisiae S288C	18-22
2674688-3	1989	The CUP2 protein contains a cysteine-rich DNA-binding domain dependent on Cu+ and Ag+ ions which bind the cysteine residues and direct the refolding of the metal-free apoprotein.	Cysteine	28-36	Cup2p	Saccharomyces cerevisiae S288C	4-8
1633174-0	1992	Characterization of the copper- and silver-thiolate clusters in N-terminal fragments of the yeast ACE1 transcription factor capable of binding to its specific DNA recognition sequence.	Copper	24-30	Cup2p	Saccharomyces cerevisiae S288C	98-102
1633174-0	1992	Characterization of the copper- and silver-thiolate clusters in N-terminal fragments of the yeast ACE1 transcription factor capable of binding to its specific DNA recognition sequence.	silver-thiolate	36-51	Cup2p	Saccharomyces cerevisiae S288C	98-102
1633174-2	1992	Band mobility shift assays showed that binding to a specific oligonucleotide (termed UASc), containing two ACE1(122*) binding sites, requires the presence of Cu(I) or Ag(I) but does not occur in the presence of divalent metal ions.	Oligonucleotides	61-76	Cup2p	Saccharomyces cerevisiae S288C	107-111
1633174-2	1992	Band mobility shift assays showed that binding to a specific oligonucleotide (termed UASc), containing two ACE1(122*) binding sites, requires the presence of Cu(I) or Ag(I) but does not occur in the presence of divalent metal ions.	uasc	85-89	Cup2p	Saccharomyces cerevisiae S288C	107-111
1633174-2	1992	Band mobility shift assays showed that binding to a specific oligonucleotide (termed UASc), containing two ACE1(122*) binding sites, requires the presence of Cu(I) or Ag(I) but does not occur in the presence of divalent metal ions.	Copper	158-160	Cup2p	Saccharomyces cerevisiae S288C	107-111
1633174-2	1992	Band mobility shift assays showed that binding to a specific oligonucleotide (termed UASc), containing two ACE1(122*) binding sites, requires the presence of Cu(I) or Ag(I) but does not occur in the presence of divalent metal ions.	Metals	220-225	Cup2p	Saccharomyces cerevisiae S288C	107-111
1633174-4	1992	The Tyr and metal cluster luminescence emission of Cu-ACE1(122*) was specifically quenched by the oligonucleotide UAScL, but not by an oligonucleotide of the same length and base composition but scrambled sequence.	Tyrosine	4-7	Cup2p	Saccharomyces cerevisiae S288C	54-58
1633174-4	1992	The Tyr and metal cluster luminescence emission of Cu-ACE1(122*) was specifically quenched by the oligonucleotide UAScL, but not by an oligonucleotide of the same length and base composition but scrambled sequence.	Oligonucleotides	98-113	Cup2p	Saccharomyces cerevisiae S288C	54-58
1633174-4	1992	The Tyr and metal cluster luminescence emission of Cu-ACE1(122*) was specifically quenched by the oligonucleotide UAScL, but not by an oligonucleotide of the same length and base composition but scrambled sequence.	Oligonucleotides	135-150	Cup2p	Saccharomyces cerevisiae S288C	54-58
1633174-6	1992	We report the first observation of a Ag(I) metal cluster in solution for Ag(I)-ACE1(122*), which was found to exhibit a quantum yield and average luminescence lifetime that are ca.	Metals	43-48	Cup2p	Saccharomyces cerevisiae S288C	79-83
1924315-3	1991	We show that the ACE1 transcriptional activator protein, which is responsible for the induction of yeast metallothionein (CUP1) in response to copper, also controls the SOD1 response to copper.	Copper	186-192	Cup2p	Saccharomyces cerevisiae S288C	17-21
1924315-5	1991	The functional importance of this DNA-protein interaction is demonstrated by the facts that (i) copper induction of SOD1 mRNA does not occur in a strain lacking ACE1 and (ii) it does not occur in a strain containing a genetically engineered SOD1 promoter that lacks a functional ACE1 binding site.	Copper	96-102	Cup2p	Saccharomyces cerevisiae S288C	279-283
1996089-2	1991	Strains with a complete deletion of the ACE1 gene, the copper-dependent activator of CUP1 transcription, are hypersensitive to copper.	Copper	55-61	Cup2p	Saccharomyces cerevisiae S288C	40-44
1996089-2	1991	Strains with a complete deletion of the ACE1 gene, the copper-dependent activator of CUP1 transcription, are hypersensitive to copper.	Copper	127-133	Cup2p	Saccharomyces cerevisiae S288C	40-44
2251259-2	1990	We have studied the role of TFIID in the transcription of the yeast metallothionein gene, which is regulated by the copper-dependent activator protein ACE1.	Copper	116-122	Cup2p	Saccharomyces cerevisiae S288C	151-155
2088504-0	1990	The DNA and Cu binding functions of ACE1 are interdigitated within a single domain.	Copper	12-14	Cup2p	Saccharomyces cerevisiae S288C	36-40
2088504-5	1990	Systematic mutagenesis of the 12 cysteine residues in ACE1 showed that all 11 cysteines within the minimal DNA-binding domain are required for ACE1 to undergo a Cu-induced conformational switch into an active DNA-binding protein.	Cysteine	33-41	Cup2p	Saccharomyces cerevisiae S288C	54-58
2088504-5	1990	Systematic mutagenesis of the 12 cysteine residues in ACE1 showed that all 11 cysteines within the minimal DNA-binding domain are required for ACE1 to undergo a Cu-induced conformational switch into an active DNA-binding protein.	Cysteine	33-41	Cup2p	Saccharomyces cerevisiae S288C	143-147
2088504-5	1990	Systematic mutagenesis of the 12 cysteine residues in ACE1 showed that all 11 cysteines within the minimal DNA-binding domain are required for ACE1 to undergo a Cu-induced conformational switch into an active DNA-binding protein.	Cysteine	78-87	Cup2p	Saccharomyces cerevisiae S288C	54-58
2088504-5	1990	Systematic mutagenesis of the 12 cysteine residues in ACE1 showed that all 11 cysteines within the minimal DNA-binding domain are required for ACE1 to undergo a Cu-induced conformational switch into an active DNA-binding protein.	Cysteine	78-87	Cup2p	Saccharomyces cerevisiae S288C	143-147
2088504-5	1990	Systematic mutagenesis of the 12 cysteine residues in ACE1 showed that all 11 cysteines within the minimal DNA-binding domain are required for ACE1 to undergo a Cu-induced conformational switch into an active DNA-binding protein.	Copper	161-163	Cup2p	Saccharomyces cerevisiae S288C	54-58
2088504-5	1990	Systematic mutagenesis of the 12 cysteine residues in ACE1 showed that all 11 cysteines within the minimal DNA-binding domain are required for ACE1 to undergo a Cu-induced conformational switch into an active DNA-binding protein.	Copper	161-163	Cup2p	Saccharomyces cerevisiae S288C	143-147
2088504-7	1990	The critical basic and cysteine residues of ACE1 are interdigitated, thereby providing an unusual example of overlapping small molecule and DNA binding functions within a directly regulated transcription factor.	Cysteine	23-31	Cup2p	Saccharomyces cerevisiae S288C	44-48
1924315-0	1991	ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene.	Copper	8-14	Cup2p	Saccharomyces cerevisiae S288C	0-4
1924315-3	1991	We show that the ACE1 transcriptional activator protein, which is responsible for the induction of yeast metallothionein (CUP1) in response to copper, also controls the SOD1 response to copper.	Copper	143-149	Cup2p	Saccharomyces cerevisiae S288C	17-21
2068090-5	1991	Sequence comparison of AMT1 protein to the S. cerevisiae copper- or silver-activated DNA-binding protein, ACE1, indicates that AMT1 contains the 11 amino terminal cysteine residues known to be critical for the metal-activated DNA-binding activity of ACE1.	Copper	57-63	Cup2p	Saccharomyces cerevisiae S288C	106-110
2068090-5	1991	Sequence comparison of AMT1 protein to the S. cerevisiae copper- or silver-activated DNA-binding protein, ACE1, indicates that AMT1 contains the 11 amino terminal cysteine residues known to be critical for the metal-activated DNA-binding activity of ACE1.	Copper	57-63	Cup2p	Saccharomyces cerevisiae S288C	250-254
2068090-5	1991	Sequence comparison of AMT1 protein to the S. cerevisiae copper- or silver-activated DNA-binding protein, ACE1, indicates that AMT1 contains the 11 amino terminal cysteine residues known to be critical for the metal-activated DNA-binding activity of ACE1.	Cysteine	163-171	Cup2p	Saccharomyces cerevisiae S288C	106-110
2068090-5	1991	Sequence comparison of AMT1 protein to the S. cerevisiae copper- or silver-activated DNA-binding protein, ACE1, indicates that AMT1 contains the 11 amino terminal cysteine residues known to be critical for the metal-activated DNA-binding activity of ACE1.	Cysteine	163-171	Cup2p	Saccharomyces cerevisiae S288C	250-254
2068090-5	1991	Sequence comparison of AMT1 protein to the S. cerevisiae copper- or silver-activated DNA-binding protein, ACE1, indicates that AMT1 contains the 11 amino terminal cysteine residues known to be critical for the metal-activated DNA-binding activity of ACE1.	Metals	210-215	Cup2p	Saccharomyces cerevisiae S288C	106-110
2068090-5	1991	Sequence comparison of AMT1 protein to the S. cerevisiae copper- or silver-activated DNA-binding protein, ACE1, indicates that AMT1 contains the 11 amino terminal cysteine residues known to be critical for the metal-activated DNA-binding activity of ACE1.	Metals	210-215	Cup2p	Saccharomyces cerevisiae S288C	250-254
2068090-7	1991	These results suggest that the amino-terminal cysteines, and other conserved residues, play an important role in the ability of AMT1 and ACE1 to sense intracellular copper levels and assume a metal-activated DNA-binding structure.	Cysteine	46-55	Cup2p	Saccharomyces cerevisiae S288C	137-141
2068090-7	1991	These results suggest that the amino-terminal cysteines, and other conserved residues, play an important role in the ability of AMT1 and ACE1 to sense intracellular copper levels and assume a metal-activated DNA-binding structure.	Copper	165-171	Cup2p	Saccharomyces cerevisiae S288C	137-141
2068090-7	1991	These results suggest that the amino-terminal cysteines, and other conserved residues, play an important role in the ability of AMT1 and ACE1 to sense intracellular copper levels and assume a metal-activated DNA-binding structure.	Metals	192-197	Cup2p	Saccharomyces cerevisiae S288C	137-141
2068093-0	1991	A copper-thiolate polynuclear cluster in the ACE1 transcription factor.	Copper	2-8	Cup2p	Saccharomyces cerevisiae S288C	45-49
2068093-4	1991	Here we report the purification and characterization of the Cu-ACE1 truncated molecule.	Copper	60-62	Cup2p	Saccharomyces cerevisiae S288C	63-67
2068093-5	1991	Spectroscopic techniques showed that ACE1 contains an unusual type of DNA binding structure that is based on a polynuclear Cu(I)-cysteinyl thiolate cluster.	cu(i)-cysteinyl thiolate	123-147	Cup2p	Saccharomyces cerevisiae S288C	37-41
2068093-7	1991	The Cu(I)-cysteine cluster of Cu-ACE1 exhibits structural properties analogous to the Cu(I)-thiolate polynuclear cluster in yeast Cu-metallothionein itself, suggesting an unusual mechanism for the evolution of this regulatory factor.	cu(i)-cysteine	4-18	Cup2p	Saccharomyces cerevisiae S288C	33-37
2068093-7	1991	The Cu(I)-cysteine cluster of Cu-ACE1 exhibits structural properties analogous to the Cu(I)-thiolate polynuclear cluster in yeast Cu-metallothionein itself, suggesting an unusual mechanism for the evolution of this regulatory factor.	copper(I)-thiolate	86-100	Cup2p	Saccharomyces cerevisiae S288C	33-37
2068093-7	1991	The Cu(I)-cysteine cluster of Cu-ACE1 exhibits structural properties analogous to the Cu(I)-thiolate polynuclear cluster in yeast Cu-metallothionein itself, suggesting an unusual mechanism for the evolution of this regulatory factor.	cu-metallothionein	130-148	Cup2p	Saccharomyces cerevisiae S288C	33-37
2068093-8	1991	The Cu cluster organizes and stabilizes the conformation of the N-terminal domain of ACE1 for specific DNA binding.	Copper	4-6	Cup2p	Saccharomyces cerevisiae S288C	85-89
2015895-0	1991	Spectroscopic characterization of the copper(I)-thiolate cluster in the DNA-binding domain of yeast ACE1 transcription factor.	copper(I)-thiolate	38-56	Cup2p	Saccharomyces cerevisiae S288C	100-104
2015895-1	1991	A polypeptide containing the amino-terminal region of ACE1 (residues 1-122; 122*), the activator of yeast Cu-metallothionein gene transcription, shows charge-transfer and metal-centered UV absorption bands, and orange luminescence which are characteristic of Cu-cysteinyl thiolate cluster structures.	cu-cysteinyl thiolate	259-280	Cup2p	Saccharomyces cerevisiae S288C	54-58
1991520-2	1991	In the wild-type strain DTY22 transcription of both Cu,Zn superoxide dismutase and metallothionein genes is induced by copper and silver, as expected on the basis of previous results indicating that ACE1 binds only Ag(I) besides Cu(I).	Copper	119-125	Cup2p	Saccharomyces cerevisiae S288C	199-203
1991520-2	1991	In the wild-type strain DTY22 transcription of both Cu,Zn superoxide dismutase and metallothionein genes is induced by copper and silver, as expected on the basis of previous results indicating that ACE1 binds only Ag(I) besides Cu(I).	Silver	130-136	Cup2p	Saccharomyces cerevisiae S288C	199-203
1986241-3	1991	In this study, we found that deleting the entire coding sequence of the ACE1 gene resulted in a decrease in basal-level transcription of CUP1 to low but detectable levels and conferred a copper-sensitive phenotype to the cells.	Copper	187-193	Cup2p	Saccharomyces cerevisiae S288C	72-76
1986241-4	1991	We have isolated a gene, designated ACE2, which when present on a high-copy-number plasmid suppresses the copper-sensitive phenotype of an ace1-deletion strain.	Copper	106-112	Cup2p	Saccharomyces cerevisiae S288C	139-143
2167439-1	1990	CUP2 is a copper-dependent transcriptional activator of the yeast CUP1 metallothionein gene.	Copper	10-16	Cup2p	Saccharomyces cerevisiae S288C	0-4
2167439-4	1990	Our results suggest that CUP2 has a complex Cu-coordinated DNA-binding domain containing different parts that function as DNA-binding elements recognizing distinct sequence motifs embedded within the UASc.	Copper	44-46	Cup2p	Saccharomyces cerevisiae S288C	25-29
2674688-5	1989	These results establish CUP2 as the primary sensor of intracellular Cu+ in the yeast Saccharomyces cerevisiae, functioning as a Cu+-regulated transcriptional activator.	Copper	68-71	Cup2p	Saccharomyces cerevisiae S288C	24-28
2653812-10	1989	Mutant cup2 cells produced extremely low levels of CUP1-specific mRNA, with or without added copper ions and lacked a factor which binds to the CUP1 promoter.	Copper	93-99	Cup2p	Saccharomyces cerevisiae S288C	7-11
2664778-1	1989	Cu ions activate yeast metallothionein gene transcription by altering the conformation and DNA-binding activity of the ACE1 transcription factor.	Copper	0-2	Cup2p	Saccharomyces cerevisiae S288C	119-123
2664778-3	1989	Analysis of the subunit composition of ACE1 bound to DNA indicates that cooperativity results from the binding of multiple Cu(I) ions to the cysteine-rich DNA-binding domain.	cuprous ion	123-128	Cup2p	Saccharomyces cerevisiae S288C	39-43
2664778-3	1989	Analysis of the subunit composition of ACE1 bound to DNA indicates that cooperativity results from the binding of multiple Cu(I) ions to the cysteine-rich DNA-binding domain.	Cysteine	141-149	Cup2p	Saccharomyces cerevisiae S288C	39-43
2664778-6	1989	The cooperative interaction between Cu and ACE1 allows the cell to respond to a small change in metal concentration by a large change in gene expression.	Metals	96-101	Cup2p	Saccharomyces cerevisiae S288C	43-47
2651899-1	1989	The ACE1 gene of the yeast Saccharomyces cerevisiae is required for copper-inducible transcription of the metallothionein gene (CUP1).	Copper	68-74	Cup2p	Saccharomyces cerevisiae S288C	4-8
2651899-4	1989	The arrangement of many of the 12 cysteines in the configuration Cys-X-Cys or Cys-X-X-Cys suggested that the ACE1 protein may bind metal ions.	Cysteine	34-43	Cup2p	Saccharomyces cerevisiae S288C	109-113
2651899-4	1989	The arrangement of many of the 12 cysteines in the configuration Cys-X-Cys or Cys-X-X-Cys suggested that the ACE1 protein may bind metal ions.	cys-x-cys	65-74	Cup2p	Saccharomyces cerevisiae S288C	109-113
2651899-4	1989	The arrangement of many of the 12 cysteines in the configuration Cys-X-Cys or Cys-X-X-Cys suggested that the ACE1 protein may bind metal ions.	cys-x-x-cys	78-89	Cup2p	Saccharomyces cerevisiae S288C	109-113
2651899-4	1989	The arrangement of many of the 12 cysteines in the configuration Cys-X-Cys or Cys-X-X-Cys suggested that the ACE1 protein may bind metal ions.	Metals	131-136	Cup2p	Saccharomyces cerevisiae S288C	109-113
2651899-5	1989	The carboxyl-terminal half of the ACE1 protein was devoid of cysteines but was highly acidic in nature.	Cysteine	61-70	Cup2p	Saccharomyces cerevisiae S288C	34-38
2643107-4	1989	This copper-inducible binding is enhanced in a yeast strain that harbors several copies of the positive regulatory gene ACE1 and is not detectable in yeast cells that contain a nonfunctional (ace1-delta 1) locus.	Copper	5-11	Cup2p	Saccharomyces cerevisiae S288C	120-124
2643107-4	1989	This copper-inducible binding is enhanced in a yeast strain that harbors several copies of the positive regulatory gene ACE1 and is not detectable in yeast cells that contain a nonfunctional (ace1-delta 1) locus.	Copper	5-11	Cup2p	Saccharomyces cerevisiae S288C	192-204
33128172-10	2021	Copper-sensing transcription factors Ace1 and Mac1 regulate the expression of genes involved in copper detoxification and uptake/mobilization in response to changes in intracellular copper levels.	Copper	0-6	Cup2p	Saccharomyces cerevisiae S288C	37-41
33128172-10	2021	Copper-sensing transcription factors Ace1 and Mac1 regulate the expression of genes involved in copper detoxification and uptake/mobilization in response to changes in intracellular copper levels.	Copper	96-102	Cup2p	Saccharomyces cerevisiae S288C	37-41
33128172-10	2021	Copper-sensing transcription factors Ace1 and Mac1 regulate the expression of genes involved in copper detoxification and uptake/mobilization in response to changes in intracellular copper levels.	Copper	182-188	Cup2p	Saccharomyces cerevisiae S288C	37-41
3043194-3	1988	This report describes the isolation of a yeast mutant, ace1-1, which is defective in the activation of CUP1 expression upon exposure to exogenous copper.	Copper	146-152	Cup2p	Saccharomyces cerevisiae S288C	55-61
3043194-5	1988	The wild-type ACE1 gene was isolated by in vivo complementation and restores copper inducibility of CUP1 expression and copper resistance to the otherwise copper-sensitive ace1-1 mutant.	Copper	77-83	Cup2p	Saccharomyces cerevisiae S288C	14-18
3043194-5	1988	The wild-type ACE1 gene was isolated by in vivo complementation and restores copper inducibility of CUP1 expression and copper resistance to the otherwise copper-sensitive ace1-1 mutant.	Copper	120-126	Cup2p	Saccharomyces cerevisiae S288C	14-18
3043194-5	1988	The wild-type ACE1 gene was isolated by in vivo complementation and restores copper inducibility of CUP1 expression and copper resistance to the otherwise copper-sensitive ace1-1 mutant.	Copper	120-126	Cup2p	Saccharomyces cerevisiae S288C	14-18
3043194-8	1988	The ACE1 gene appears to play a direct or indirect positive role in activation of CUP1 expression in response to elevated copper concentrations.	Copper	122-128	Cup2p	Saccharomyces cerevisiae S288C	4-8
33498600-6	2021	Reverse engineering of target genes was performed and carotenoid yield could be increased 6.4-fold in YPD media through overexpression of ACE1.	Carotenoids	54-64	Cup2p	Saccharomyces cerevisiae S288C	138-142
33498600-7	2021	The present study revealed for the first time the prominent promotion of carotenoid yield by copper ions in engineered S. cerevisiae and provided a new target ACE1 for genetic engineering of S. cerevisiae for the bioproduction of carotenoids.	Carotenoids	73-83	Cup2p	Saccharomyces cerevisiae S288C	159-163
33498600-7	2021	The present study revealed for the first time the prominent promotion of carotenoid yield by copper ions in engineered S. cerevisiae and provided a new target ACE1 for genetic engineering of S. cerevisiae for the bioproduction of carotenoids.	Carotenoids	230-241	Cup2p	Saccharomyces cerevisiae S288C	159-163
31519745-3	2019	In a previously described non-complementation screen, we found an allele difference of CUP2, a copper-binding transcription factor, underlies divergence in copper resistance between Saccharomyces cerevisiae and S. uvarum Here, we tested whether the allele effect of CUP2 was caused by multiple nucleotide changes.	Copper	95-101	Cup2p	Saccharomyces cerevisiae S288C	87-91
31519745-3	2019	In a previously described non-complementation screen, we found an allele difference of CUP2, a copper-binding transcription factor, underlies divergence in copper resistance between Saccharomyces cerevisiae and S. uvarum Here, we tested whether the allele effect of CUP2 was caused by multiple nucleotide changes.	Copper	156-162	Cup2p	Saccharomyces cerevisiae S288C	87-91
31519745-4	2019	By analyzing chimeric constructs containing four separate regions in the CUP2 gene, including its distal promoter, proximal promoter, DNA binding domain and transcriptional activation domain, we found that all four regions of the S. cerevisiae allele conferred copper resistance, with the proximal promoter showing the largest effect, and that both additive and epistatic effects are likely involved.	Copper	261-267	Cup2p	Saccharomyces cerevisiae S288C	73-77