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Information on EC 2.7.7.84 - 2'-5' oligoadenylate synthase
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EC Tree
2.7.7.84 2'-5' oligoadenylate synthaseIUBMB Comments
The enzyme is activated by binding to double-stranded RNA. The resulting product binds to and activates RNase L, which subsequently degrades the RNA. Oligoadenylates of chain lengths 2, 4 and 5 are also produced. The dimer does not have any known biological activity .
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Word Map
- 2.7.7.84
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interferon-induced
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ifn-induced
- ifn-alpha
- viruses
- interferon-alpha
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ifn-beta
- ifn-gamma
- synthetases
- dsrna
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ifn-stimulated
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antiproliferative
- stomatitis
- interferon-beta
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interferon-stimulated
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myxovirus
- stat1
- alpha-interferon
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interferon-treated
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encephalomyocarditis
- neopterin
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2-microglobulin
- flavivirus
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daudi
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ifn-treated
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dsrna-dependent
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2'-5'oligoadenylate
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endoribonuclease
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ifn-mediated
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ifn-alpha-induced
- isg15
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2-5a-dependent
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dsrna-activated
- cydonium
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ifn-dependent
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polyi
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rnasel
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polyinosinic-polycytidylic
- geodia
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interferon-mediated
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ifn-resistant
-
anticellular
- analysis
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
2-5a synthetase, 2',5'-oligoadenylate synthetase, 2'-5'-oligoadenylate synthetase, 2'-5' oligoadenylate synthetase, oas1b, oas1a, 2'-5'-oligoadenylate synthetase 1, 2'-5'oas, 2'5' oligoadenylate synthetase, oligoadenylate synthetase-like, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2',5'-oligoadenylate synthetase 1
2'-5' oligoadenylate synthetase
2'-5'-oligoadenylate synthetase
2'5' oligoadenylate synthetase
OAS
OAS-L
OAS1
OAS1A
OAS1b
OAS1c
OAS1d
OAS1e
OAS1f
OAS1g
OAS1h
OAS2
OAS3
OASL
2',5'-oligoadenylate synthetase 1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 ATP = pppA2'p5'A2'p5'A + 2 diphosphate
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SYSTEMATIC NAME
IUBMB Comments
ATP:ATP adenylyltransferase (2'-5' linkages-forming)
The enzyme is activated by binding to double-stranded RNA. The resulting product binds to and activates RNase L, which subsequently degrades the RNA. Oligoadenylates of chain lengths 2, 4 and 5 are also produced. The dimer does not have any known biological activity [2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ATP
pppA2'p5'A + diphosphate
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synthesis of 2-5A dimer, trimer and tetramer with the prevalence of dimer among reaction products
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?
3 ATP
pppA2'p5'A3'p5'A + 2 diphosphate
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enzyme synthesizes triadenylates with the first linkage being a 2',5'-phosphodiester bond and the second one being a 3',5'-bond. The ratio of products containing 2',5'-linkage to the products with 3',5'-linkage is 2.4 in the presence of 100 mg/ml poly(I)poly(C)
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?
NTP + pppA2'p5'A
pppA2'p5'Ap2'p5'N + 2 diphosphate
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reaction of OAS2, broad spectrum of accepted donor substrates, including ATP, GTP, CTP, UTP, ITP, and their deoxy variants, overview
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?
NTP + RpA
RpA2'p5'N + 2 diphosphate
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reaction of OAS3, broad spectrum of accepted donor substrates, including ATP, GTP, CT, UTP, ITP, and their deoxy variants, and of acceptor substrates including tRNA, A5'ppp5''A, A5'pppp5''A, NAD+, and polyA, overview
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?
3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
during the synthesis of 2-5A, one ATP, known as the donor, transfers its AMP moiety to a second ATP, known as the acceptor. For polymerization, the acceptor ATP is replaced by a growing chain of 2-5A
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?
3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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-
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?
additional information
?
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enzyme duOASL possesses the enzymatic activity to convert the ATP to 2'-5'-A up to tetramer
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additional information
?
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enzyme duOASL possesses the enzymatic activity to convert the ATP to 2'-5'-A up to tetramer
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additional information
?
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enzyme goOASL possesses the enzymatic activity to convert the ATP to 2'-5'-A up to tetramer
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additional information
?
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the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity
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?
additional information
?
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enzyme chOASL possesses the enzymatic activity to convert the ATP to 2'-5'-A up to tetramer
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additional information
?
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enzyme chOASL possesses the enzymatic activity to convert the ATP to 2'-5'-A up to tetramer
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additional information
?
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the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity
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?
additional information
?
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whereas only two 2',5'-adenylates that inhibit protein synthesis (i.e., trimer and tetramer) are synthesized by normal peripheral blood mononuclear cells, trimer, tetramer, pentamer, and hexamer are synthesized by peripheral blood mononuclear cells from cutaneous T-cell lymphomas
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?
additional information
?
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addition of high concentrations of tRNA (2 mg/ml) does not relieve the absolute dependence on double stranded RNA for 2' adenylation activity and 2'5' oligoadenylate synthetase activity in an extract of human Wish cells
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?
additional information
?
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isozyme OAS1 is specific for ATP, but isozyme OAS2 shows broad substrate specificity accepting diverse nucleotide triphosphates as donor substrates that give several products, overview. Isozymes OAS1 and OAS2 produce 2-5A oligomers, while isozyme OAS3 produces 2-5A dimers. GTP is an alternative substrate for the 2'-5'OAS, as donor as well as acceptor molecule. Nevertheless, competition experiments of GTP versus ATP points out that GTP exhibits a much higher affinity for the donor site of OAS than for the acceptor one. A monomeric OAS-like protein, OASL, is catalytically inactive
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?
additional information
?
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catalytic activity of OAS proteins incubated with polyriboinosinic polyribocytidylic acid [poly (I:C)] in a buffered solution with ATP and MgCl2 at 37°C
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additional information
?
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catalytic activity of OAS proteins incubated with polyriboinosinic polyribocytidylic acid [poly (I:C)] in a buffered solution with ATP and MgCl2 at 37°C
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additional information
?
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catalytic activity of OAS proteins incubated with polyriboinosinic polyribocytidylic acid [poly (I:C)] in a buffered solution with ATP and MgCl2 at 37°C
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additional information
?
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the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity
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?
additional information
?
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besides accepting AMP, the NAD+ molecule can accept UMP, CMP, GMP and dAMP and probably other NMP catalyzed by the rabbit reticulocyte synthetase, UMP, CMP, and dAMP as well as AMP are incorporated into NAD+ at about half the rate of AMP incorporation into 2'5'-oligoadenylates, overview. A natural RNA, tRNA, can also be used as a primer for the 2' adenylation by both the the mouse L-cell enzyme. NADP+ does not serve as substrate
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?
additional information
?
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substrate specificity and possible products, overview. Selected nucleoside 5'-triphosphates are converted to 2',5'-oligonucleotides with the following order of efficiency for the nucleoside: 8-azaadenosine > adenosine = 2-chloroadenosine > sangivamycin > toyocamycin > formycin > 3-ribosyladenine > ribavirin > tubercidin > adenosine 1-oxide > 2-beta-D-ribofuranosylthiazole-4-carboxamide > inosine = 1,N6-ethenoadenosine > guanosine > 8-bromoadenosine = uridine > cytidine. Adenosine 5'-(beta,gamma-imidotriphosphate) is no substrate
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?
additional information
?
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the 2'5' oligoadenylate synthase has a multifunctional 2',5'-nucleotidyl-transferase activity
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?
additional information
?
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besides accepting AMP, the NAD+ molecule can accept UMP, CMP, GMP, and dAMP and probably other NMP catalyzed by the rabbit reticulocyte synthetase, UMP, CMP, and dAMP as well as AMP are incorporated into NAD+ at about half the rate of AMP incorporation into 2'5' oligoadenylates, overview. A natural RNA, tRNA, can also be used as a primer for the 2' adenylation by both the rabbit reticulocyte enzyme. NADP+ does not serve as substrate
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?
additional information
?
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enzyme osOASL possesses the enzymatic activity to convert the ATP to 2'-5'-A up to tetramer, very low activity
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additional information
?
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enzyme polymerizes ATP into 2',5'-linked and 3'-5'-linked oligoadenylates in the presence of synthetic dsRNA poly(I)poly(C). The presence of dsRNA is required
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
-
-
-
?
additional information
?
-
-
the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity
-
-
?
additional information
?
-
-
the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity
-
-
?
additional information
?
-
-
whereas only two 2',5'-adenylates that inhibit protein synthesis (i.e., trimer and tetramer) are synthesized by normal peripheral blood mononuclear cells, trimer, tetramer, pentamer, and hexamer are synthesized by peripheral blood mononuclear cells from cutaneous T-cell lymphomas
-
-
?
additional information
?
-
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the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity
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-
?
additional information
?
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the 2'5' oligoadenylate synthase has a multifunctional 2',5'-nucleotidyl-transferase activity
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
activates, after stimulation with dsRNA, OAS requires two Mg2+ ions and two molecules of ATP to perform its enzymatic activity. Residues Ser396, Gln528, Lys547, Lys566, and Tyr567 are involved in positioning of the donor ATP, while residues Val412, Arg463, Leu483, Ser 521, Thr522, Thr525, and Gln528 are involved in positioning of the acceptor ATP
ATP
activates, after stimulation with dsRNA, OAS requires two Mg2+ ions and two molecules of ATP to perform its enzymatic activity. Residues Ser63, Gln194, Lys213, Gln229, and Tyr230 are involved in positioning of the donor ATP, while residues Val79, Arg130, Leu150, Ser 187, Thr188, Thr191, and Gln194 are involved in positioning of the acceptor ATP
ATP
activates, after stimulation with dsRNA, OAS requires two Mg2+ ions and two molecules of ATP to perform its enzymatic activity. Residues Ser804, Gln931, Lys950, Gln969, and His970 are involved in positioning of the donor ATP, while residues Val820, Arg869, Leu890, Ser924, Thr925, Thr928, and Gln931 are involved in positioning of the acceptor ATP
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
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the catalysis of 2'-5'-oligoadenylate synthesis is strictly dependent on double-stranded RNA and magnesium ions
Mg2+
activates, after stimulation with dsRNA, OAS requires two Mg2+ ions and two molecules of ATP to perform its enzymatic activity. The Mg2+ ions play a critical role in positioning the substrates in an ideal geometry for the reaction, binding structure modeling, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Zn2+
-
strong inhibition, zinc ions can control the oligomerisation by enhancing the formation of tetrameric forms of OAS1p42
additional information
inhibitor screening and identification of 12 compounds exerting competitive inhibition in the ATP binding site1 of OAS1 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors; inhibitor screening and identification of 18 compounds exerting competitive inhibition in the ATP binding site of OAS2 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors; inhibitor screening and identification of 7 compounds exerting competitive inhibition in the ATP binding site of OAS3 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors
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additional information
inhibitor screening and identification of 12 compounds exerting competitive inhibition in the ATP binding site1 of OAS1 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors; inhibitor screening and identification of 18 compounds exerting competitive inhibition in the ATP binding site of OAS2 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors; inhibitor screening and identification of 7 compounds exerting competitive inhibition in the ATP binding site of OAS3 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors
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additional information
inhibitor screening and identification of 12 compounds exerting competitive inhibition in the ATP binding site1 of OAS1 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors; inhibitor screening and identification of 18 compounds exerting competitive inhibition in the ATP binding site of OAS2 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors; inhibitor screening and identification of 7 compounds exerting competitive inhibition in the ATP binding site of OAS3 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors
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