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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 1,N6-ethenoadenosine
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3 2-beta-D-ribofuranosylthiazole-4-carboxamide
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3 2-chloroadenosine
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3 3-ribosyladenine
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3 8-azaadenosine
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3 8-bromoadenosine
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3 adenosine 1-oxide
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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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3 sangivamycin
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3 toyocamycin
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n ATP
pppA(2'p5'A)n + 2 diphosphate
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reaction of OAS1
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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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additional information
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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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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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 ATP
pppA2'p5'A2'p5'A + 2 diphosphate
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3 CTP
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3 dATP
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3 GTP
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3 UTP
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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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viral dsRNA
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2'-5'-oligoadenylate synthases are activated by viral double-stranded RNA in infected cells and initiate a cellular response by synthesizing 2'-5'-oligoadenylates, which in turn activate RNase L. All mammalian OAS proteins require dsRNA for activity ssRNA or DNA does not activate this class of enzymes. The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated. OAS1 RNA activation site structure, overview
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viral RNA VAI
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sequences and secondary structures of adenovirus VAI dsRNAs, overview. Highly structured RNA, VAI, positively regulates the activity of the interferon-induced 2'5'-oligoadenylate synthase, which typically represents a key mechanism whereby host-cell protein translation is attenuated in response to foreign dsRNA. In the contrary, with other cell proteins, RNA VAI, after processing by the RNA silencing machinery, inhibits the innate immune response via a series of interactions with specific protein partners. OAS1:VAI complex stoichiometry and kinetics, overview. The RNA 5'-end phosphorylation state is important in the activation or inhibition of OAS enzymes. While full-length VAI does indeed activate OAS1 in vitro, the Dicer-truncated molecule lacking the terminal stem has the opposite effect, and this is the physiologically important response, overview
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dsRNA
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the catalysis of 2'-5'-oligoadenylate synthesis is strictly dependent on double-stranded RNA and magnesium ions
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dsRNA
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the enzyme is dependent on dsRNA, activation of isozyme OAs3 by 0.001 mg/ml, and of isozymes AS1 and OAS2 by 0.1 mg/ml, at optimals pH values
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dsRNA
OAS1 can be catalytically activated by dsRNA of any length greater than 19 bp. Highly structured viral RNAs are established OAS1 activators, but they are not able to activate OAS2 enzymatic activity based on the lack of extended stretches of dsRNA of greater than 35 bp. In-vitro transcribtion of WNV 5' TR, WNV 3' TR, VAI, VAIDELTATS, HIV-TAR, and EBER-1 from linearized plasmids using T7 polymerase, with the exceptions of HIV-TAR and EBER-1, all viral RNAs can activate OAS1 to some extent. Whereas 5'-TR and 3'-TR achieve potent activation, VAI and VAIDELTATS are only modestly above baseline
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dsRNA
OAS2 shows a marked increase in activity with increasing dsRNA length with a minimum requirement of 35 bp. Activation of OAS2 is also more efficient when the dsRNA contained 3'-overhangs, despite no significant impact on binding affinity. The OAS2 activation potential is dependent on dsRNA length, kinetic analysis, overview. In-vitro transcribtion of WNV 5' TR, WNV 3' TR, VAI, VAIDELTATS, HIV-TAR, and EBER-1 from linearized plasmids using T7 polymerase, none of the RNAs can activate isozyme OAS2
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dsRNA
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double-stranded RNA, synthetic poly(I:C), an allosteric activator of the latent (2-5)A synthetase
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dsRNA
2'-5'-oligoadenylate synthases are activated by viral double-stranded RNA in infected cells and initiate a cellular response by synthesizing 2'-5'-oligoadenylates, which in turn activate RNase L. All mammalian OAS proteins require dsRNA for activity ssRNA or DNA does not activate this class of enzymes. The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated. OAS1 RNA activation site structure, overview
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additional information
highly structured viral RNAs that are established OAS1 activators are not able to activate OAS2 enzymatic activity based on the lack of extended stretches of dsRNA of greater than 35 bp. Phosphorylation state of the 5' end of dsRNA activators does not affect OAS2 activation
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additional information
highly structured viral RNAs that are established OAS1 activators are not able to activate OAS2 enzymatic activity based on the lack of extended stretches of dsRNA of greater than 35 bp. Phosphorylation state of the 5' end of dsRNA activators does not affect OAS2 activation
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additional information
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highly structured viral RNAs that are established OAS1 activators are not able to activate OAS2 enzymatic activity based on the lack of extended stretches of dsRNA of greater than 35 bp. Phosphorylation state of the 5' end of dsRNA activators does not affect OAS2 activation
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evolution
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conserved catalytic mechanism for the 2'- and 3'-specific nucleotidyl transferases. specific nucleotidyl transferases. Comparison with structures of other superfamily members indicates that the donor substrates are bound by conserved active site features while the acceptor substrates are oriented by nonconserved regions
evolution
conserved catalytic mechanism for the 2'- and 3'-specific nucleotidyl transferases. specific nucleotidyl transferases. Comparison with structures of other superfamily members indicates that the donor substrates are bound by conserved active site features while the acceptor substrates are oriented by nonconserved regions
evolution
in mice, the OAS gene family locates on chromosome 5 and consists of eight genes of Oas1 (Oas1a through Oas1h), Oas2, Oas3, and two OasL genes (OasL1 and OasL2). Oas1a and Oas1g are only active to convert ATP into di- and tri-2,5A, whereas Oas1b, Oas1c, Oas1d, Oas1e, Oas1f, Oas1h and MSM-derived Oas1b are inactive
evolution
isozyme OAS1 belongs to the 2'-5'-oligoadenylate synthetases (OAS) family of interferon-inducible enzymes that act as pattern recognition receptors (PRR) to bind double-stranded RNA (dsRNA) during viral infection. The C-terminal catalytic domain of OAS2 (DII) shares strong sequence homology and catalytic aspartic acids (D408, D410, D481) with OAS1
evolution
isozyme OAS2 belongs to the 2'-5'-oligoadenylate synthetases (OAS) family of interferon-inducible enzymes that act as pattern recognition receptors (PRR) to bind double-stranded RNA (dsRNA) during viral infection. The C-terminal catalytic domain of OAS2 (DII) shares strong sequence homology and catalytic aspartic acids (D408, D410, D481) with OAS1iral infection
evolution
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in mice, the OAS gene family locates on chromosome 5 and consists of eight genes of Oas1 (Oas1a through Oas1h), Oas2, Oas3, and two OasL genes (OasL1 and OasL2). Oas1a and Oas1g are only active to convert ATP into di- and tri-2,5A, whereas Oas1b, Oas1c, Oas1d, Oas1e, Oas1f, Oas1h and MSM-derived Oas1b are inactive
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malfunction
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cells transfected with 25 AS antisense oligonucleotides inhibit the antiviral effect of IFN-gamma
malfunction
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mutation of the conserved Leu3 and Pro7 and of Cys330, Cys331, and Lys332 reduce enzyme activity
malfunction
mutation of the conserved Leu3 and Pro7 and of Cys330, Cys331, and Lys332 reduce enzyme activity. Mutants S62A and S63A display Michaelis-Menten kinetics toward NAD+, the kcat of the Ser62Ala mutant is approximately 3fold lower than the kcat for either the wild-type or the S63A mutant
malfunction
knockdown of endogenous OAS1 increases the PRRSV ORF7 mRNA level to 1.6 and 1.7times of that in control in 24 and 36 hours post-infection of PRRSV, respectively, and leads to approximate 5.5times increase of the frequency of fluorescence positive cells compared to negative control. Overexpression of OAS1 in Marc-145 cells can inhibit the replication of PRRSV
malfunction
OAS2 knockdown increases ZIKV replication. Overexpression of OAS2 modestly increases the IFN-induced p-STAT1 both with IFN treatment and without IFN treatment compared to control. OAS2 overexpression also increases ISRE activity and some classical ISGs expression including Myxovirus resistance-A (MxA) and interferon-induced protein 2 (IFIT2)
malfunction
the effects of OASL silencing on cytokine and chemokine (MCP-1) secretion in THP-1 macrophages can be summarised as follows: I. TNF-alpha and IL-1beta secretion is enhanced during mycobacterial infection in the presence of OASL, II. OASL enhances MCP-1 production in response to THP-1 infection by pathogenic mycobacteria only, and III. IL-10 production is unaffected by the presence/absence of OASL. Silencing of OASL promotes intracellular replication of pathogenic and non-pathogenic mycobacteria, OASL exerts a suppressive effect on intracellular mycobacterial replication
metabolism
only Oas1a and Oas1g show enzymatic activity. Although MSM-derived Oas1b shows antiviral activity in BHK-21 cells to both viruses, the two neurotropic flaviviruses, West Nile virus and tick-borne encephalitis virus, but all B6-derived OAS paralogues do not show antiviral activity. Paralogues Oas1a and Oas1g play a role in potentiating viral RNA-induced interferon response in the cell, whereas the paralogue Oas1b works as a specific anti-flavivirus factor unless it is mutated. The role of other paralogues (OAS1c, d, e, f, and h) is unknown to date
metabolism
only Oas1a and Oas1g show enzymatic activity. Although MSM-derived Oas1b shows antiviral activity to both viruses, the two neurotropic flaviviruses, West Nile virus and tick-borne encephalitis virus, but all B6-derived OAS paralogues do not show antiviral activity. Paralogues Oas1a and Oas1g play a role in potentiating viral RNA-induced interferon response in the cell, whereas the paralogue Oas1b works as a specific anti-flavivirus factor unless it is mutated. The role of other paralogues (OAS1c, d, e, f, and h) is unknown to date
metabolism
the human 2',5'-oligoadenylate synthetase (OAS) are IFN-induced genes that play an essential role in the antiviral activity of IFNs. The OAS family is composed of four gene members, including OAS1, OAS2, OAS3, and OAS-like protein (OASL), differing in numbers of OAS domain, type of synthesized 2-5A and oligomerization level
metabolism
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only Oas1a and Oas1g show enzymatic activity. Although MSM-derived Oas1b shows antiviral activity in BHK-21 cells to both viruses, the two neurotropic flaviviruses, West Nile virus and tick-borne encephalitis virus, but all B6-derived OAS paralogues do not show antiviral activity. Paralogues Oas1a and Oas1g play a role in potentiating viral RNA-induced interferon response in the cell, whereas the paralogue Oas1b works as a specific anti-flavivirus factor unless it is mutated. The role of other paralogues (OAS1c, d, e, f, and h) is unknown to date
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metabolism
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only Oas1a and Oas1g show enzymatic activity. Although MSM-derived Oas1b shows antiviral activity to both viruses, the two neurotropic flaviviruses, West Nile virus and tick-borne encephalitis virus, but all B6-derived OAS paralogues do not show antiviral activity. Paralogues Oas1a and Oas1g play a role in potentiating viral RNA-induced interferon response in the cell, whereas the paralogue Oas1b works as a specific anti-flavivirus factor unless it is mutated. The role of other paralogues (OAS1c, d, e, f, and h) is unknown to date
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physiological function
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2'-5' oligoadenylate synthase plays a critical role in interferon-gamma inhibition of respiratory syncytial virus infection of human epithelial cells. Respiratory syncytial virus, RSV, associated with bronchiolitis and asthma, is resistant to the antiviral effects of type-I interferons, but not IFN-gamma, molecular mechanism involving the 2',5'-oligoadenylate synthetase, overview
physiological function
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2'-5'-oligoadenylate synthases are interferon-induced, double-stranded RNA-activated antiviral enzymes which are the only proteins known to catalyze 2'-specific nucleotidyl transfer
physiological function
2'-5'-oligoadenylate synthases are interferon-induced, double-stranded RNA-activated antiviral enzymes which are the only proteins known to catalyze 2'-specific nucleotidyl transfer
physiological function
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2'-5'OASs are initially described as important components of the antiviral action of interferon. But the structural and functional complexity of the human 2'-5'OAS family implying that these proteins may have distinct roles in the cell. 2'-5'OAS forms 2-5A molecules that activate the latent endoribonuclease. The RNAse L. OAS1 and OAS2 mediate resistance to virus infections, OAS3 appears to confer sensitivity to dsRNA-induced apoptosis via a mechanism that does not require the synthesis of 2-5A
physiological function
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2'5' oligoadenylate synthase catalyzes the synthesis of a series of 2'5' heteronucleotides with the general structure of pppA(pA)nPN and NAD-NMP. NAD+ acts as an acceptor for 2'-adenylation by the enzyme isolated from interferon treated chicken cell. The requirement for the acceptor site is an AMP group linked in a RpA configuration where R stands for pyrophosphate, NAD+, oligomeric or polymeric primers. NAD+ tRNA may play a regulatory role in 2'5'-oligoadenylates synthesis in the cell
physiological function
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2'5' oligoadenylate synthase catalyzes the synthesis of a series of 2'5' heteronucleotides with the general structure of pppA(pA)nPN and NAD-NMP. The enzyme also catalyzes the 2' adenylation of tRNA. The requirement for the acceptor site is an AMP group linked in a RpA configuration where R stands for pyrophosphate, NAD+, oligomeric or polymeric primers. NAD+ tRNA may play a regulatory role in 2'5'-oligoadenylates synthesis in the cell
physiological function
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2'5' oligoadenylate synthase catalyzes the synthesis of a series of 2'5' heteronucleotides with the general structure of pppA(pA)nPN and NAD-NMP. The enzyme also catalyzes the 2' adenylation of tRNA. The requirement for the acceptor site is an AMP group linked in a RpA configuration where R stands for pyrophosphate, NAD+, oligomeric or polymeric primers. NAD+ tRNA may play a regulatory role in 2'5'-oligoadenylates synthesis in the cell
physiological function
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2'5'-oligoadenylate synthase catalyzes the synthesis of a series of 2'5'-heteronucleotides with the general structure of pppA(pA)nPN and NAD-NMP. NAD+ acts as an acceptor for 2'-adenylation by the enzyme isolated from interferon treated chicken cell. The requirement for the acceptor site is an AMP group linked in a RpA configuration where R stands for pyrophosphate, NAD+, oligomeric or polymeric primers. NAD+ tRNA may play a regulatory role in 2'5'-oligoadenylates synthesis in the cell
physiological function
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highly structured RNA, VAI, is able to positively regulate the activity of the interferon-induced 2'5'-oligoadenylate synthase, a processed version of VAI lacking the terminal stem behaves as a pseudo-inhibitor of OAS1. The RNA 5'-end phosphorylation state is important in the activation or inhibition of OAS enzymes. While full-length VAI activates OAS1 in vitro, the Dicer-truncated molecule lacking the terminal stem has the opposite effect, and this is the physiologically important response
physiological function
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synthesis of higher molecular weight 2',5'-adenylates is that in vitro protein synthesis is inhibited 30% by a 2500fold dilution of the 2',5'-oligoadenylates synthesized by 2',5'-oligoadenylate synthetase in peripheral blood mononuclear cells cell-free extracts from cutaneous T-cell lymphoma, whereas a 2500fold dilution of the 2',5'-oligoadenylates from normal peripheral blood mononuclear cells is not inhibitory. No appreciable difference in 2',5'-oligoadenylate synthetase activity occurs between T-cells and non-T-cells from cutaneous T-cell lymphomas
physiological function
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The 2,5'-oligoadenylate synthetase proteins associated with endoribonuclease RNase L are components of the interferon-regulated OAS/RNase L system, which is an RNA decay pathway known to play an important role in the innate antiviral immunity. Critical role for the 1b isoform of the mouse Oas1b gene in resistance to West Nile virus, WNV, infection in vivo, molecular basis for the sensitivity of WNVto the Oas1b antiviral pathway, overview. Antiviral action of Oas1b is essentially restricted to the early stages in virus life cycle. Inability of WNV to productively infect the Oas1b-expressing cells is attributable to a dramatic reduction in positive-stranded viral RNA level
physiological function
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the enzyme is part of the (2-5)A synthetase antiviral protection system of the sponge
physiological function
2',5'-oligoadenylate synthetase 1 (OAS1) inhibits PRRSV replication in monkey Marc-145 cells. Antiviral activity of OAS1 has been demonstrated in mice and humans with infections of numerous RNA and DNA viruses, such as coxsackie virus, West Nile virus, Hepatitis C virus, cowpox virus, and SARS virus
physiological function
2',5'-oligoadenylate synthetase 2 (OAS2) inhibits Zika virus replication through activation of type I IFN signaling pathway. ZIKV infection induces OAS2 expression through a RIG-I-dependent pathway. OAS2 overexpression inhibits ZIKV replication, while OAS2 knockdown increases ZIKV replication. OAS2 inhibits ZIKV replication through enhanced IFNbeta expression, leading to the activation of the Jak/STAT signaling pathway
physiological function
as part of the type I IFN signaling, the 2'-5'-oligoadenylate synthetase (OAS) proteins are involved in the progression of several non-viral diseases. OAS is correlated with immune-modulatory functions that promote chronic inflammatory conditions, autoimmune disorders, cancer, and infectious diseases
physiological function
different dsRNA length requirement of OAS2 suggests non-overlapping biological functions
physiological function
enzyme ChOAS-L possesses enzymatic activity to convert ATP into 2'-5'-linked oligoadenylates and antiviral activity against West Nile virus (WNV) replicon, relationship between enzymatic and antiviral activities of the chicken oligoadenylate synthetase-like, overview. The ChOAS-L antiviral activity is independent of enzymatic activity. Analysis of the mechanism of antiviral activity against the flavivirus replication of ChOAS-L
physiological function
human 2'-5'-oligoadenylate synthetase-like protein inhibits intracellular Mycobacterium tuberculosis replication and promotes proinflammatory cytokine secretion
physiological function
mouse Oas1b provides resistance to flavivirus infection, and Oas1b is enzymatically inactive and independent of RNase L
physiological function
Oas1a, Oas1b, and Oas1g genes play a general role in various tissues in the stimulation of virus or interferon, whereas other paralogues work as somewhat specific factors in the respective tissues
physiological function
the enzyme shows inhibitory activity on WNV replicon replication
physiological function
the enzyme shows inhibitory activity on WNV replicon replication
physiological function
the enzyme shows inhibitory activity on WNV replicon replication
physiological function
the enzyme shows inhibitory activity on WNV replicon replication
physiological function
the observed differences in anti-viral activity between the human OAS1 p46 and p42 isoforms are not fully understood. The protein expression of these isoforms is determined by the SNP rs10774671, either being an A or a G allele resulting in expression of either the p42 or the p46 isoform. The rs10774671 SNP and in extension the discrepancy between the p42 and p46 isoforms have been directly associated with several viral diseases includingWest Nile Virus infections, susceptibility to hepatitis B virus (HBV) infections and Sjögren's syndrome development, liver fibrosis progression and response to interferon therapy during hepatitis C virus (HCV) infections as well as in tuberculosis. In all of these instances, it is the G allele (i.e. the OAS1 p46 isoform) that confers resistance, while the p42 variant is associated with a higher risk in these infectious diseases. It has also been shown that the p46 isoform, but not the p42 isoform, facilitate RNase L-dependent anti-viral activity against HCV in cultured Huh7 cells
physiological function
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Oas1a, Oas1b, and Oas1g genes play a general role in various tissues in the stimulation of virus or interferon, whereas other paralogues work as somewhat specific factors in the respective tissues
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physiological function
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mouse Oas1b provides resistance to flavivirus infection, and Oas1b is enzymatically inactive and independent of RNase L
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additional information
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mechanism responsible for the inhibition of virus replication in interferon treated cells, overview
additional information
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mechanism responsible for the inhibition of virus replication in interferon treated cells, overview
additional information
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OAS active site structure with three conserved active site aspartic acid residues, overview
additional information
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OAS active site structure with three conserved active site aspartic acid residues, overview
additional information
OAS active site structure with three conserved active site aspartic acid residues, overview
additional information
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OAS1 is the small form and OAS2 is the medium form of the human interferon-induced 2'-5'-oligoadenylate synthases
additional information
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the active site is composed of three aspartic acids, Asp76, Asp78, and Asp148, and two domains found right after the dsRNA binding regions constituting a catalytic groove on the opposite face of the protein, which has the form of an erythrocyte, where the two ends are close
additional information
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the different isozymes may require different conditionss for catalytic reaction and are located in different subcelular locations
additional information
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three major forms of OAS proteins in human cells: 40/46-kDa small isoforms, OAS1, 69/71-kDa medium isoforms, OAS2, and a 100-kDa large isoform, OAS3
additional information
enzyme structure homology modeling. The active site is formed by residues Asp408, Asp410, Asp481
additional information
enzyme structure homology modeling. The active site is formed by residues Asp408, Asp410, Asp481
additional information
enzyme structure homology modeling. The active site is formed by residues Asp408, Asp410, Asp481
additional information
enzyme structure homology modeling. The active site is formed by residues Asp75, Asp77, Asp148
additional information
enzyme structure homology modeling. The active site is formed by residues Asp75, Asp77, Asp148
additional information
enzyme structure homology modeling. The active site is formed by residues Asp75, Asp77, Asp148
additional information
enzyme structure homology modeling. The active site is formed by residues Asp816, Asp818, Asp888
additional information
enzyme structure homology modeling. The active site is formed by residues Asp816, Asp818, Asp888
additional information
enzyme structure homology modeling. The active site is formed by residues Asp816, Asp818, Asp888
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induction by interferon
K203E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K212A
the mutant has strongly impaired catalytic activity, KM for ATP is increased by almost 4fold relative to that of the wild-type protein, and kcat is decreased by roughly 8fold
K41E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K59E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R194E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R194E/R198E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R198E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R198M
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R245E/K246E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R38E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R38E/K41E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R38E/K41E/K59E/R194E/R198E
site-directed mutagenesis, the mutant is almost inactive
S62A
the mutant displays a strong substrate inhibition at higher ATP concentrations, more dramatic than that observed for wild-type OAS1
S63A
the mutant displays a strong substrate inhibition at higher ATP concentrations, more dramatic than that observed for wild-type OAS1
additional information
enzyme OAS1 knockdown by siRNA, or overexpression in Marc-145 cells. Three siRNAs are designed according to the published Macaque OAS1 mRNA sequence (Macaca mulatta, UniProt ID A4LAA0). Knockdown of OAS1 by siRNA significantly increases the frequency of CPE of PRRSV in Marc-145 cells
additional information
construction of enzyme mutants, ChOAS-L-A-FL, which is ChOAS-L-A conjugated with the Flag-Tag DYKDDDDK sequence, is used for generation of eight mutations: The DELTALxxxP domain, DELTAP-LooP domain, DELTAD-D box domain, 5 KR-RR-K193H (one AA substitution), DELTAKR-RR, and ChOAS-L-B (the other allele) are generated by site-directed mutagenesis. The other two mutations, DELTAUbL2 domain and DELTAUbL1/UbL2 domains, are generated in addition. All mutated variants are enzymatically inactive except for ChOAS-L-ADELTAUbL2, but all mutants shows antiviral activity to inhibit the replication of the WNV replicon except for the ChOAS-L-ADELTAUbL1/UbL2, which shows a partial inhibition compared to the wild-type ChOAS-L-A or the other mutant enzyme variants
additional information
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construction of enzyme mutants, ChOAS-L-A-FL, which is ChOAS-L-A conjugated with the Flag-Tag DYKDDDDK sequence, is used for generation of eight mutations: The DELTALxxxP domain, DELTAP-LooP domain, DELTAD-D box domain, 5 KR-RR-K193H (one AA substitution), DELTAKR-RR, and ChOAS-L-B (the other allele) are generated by site-directed mutagenesis. The other two mutations, DELTAUbL2 domain and DELTAUbL1/UbL2 domains, are generated in addition. All mutated variants are enzymatically inactive except for ChOAS-L-ADELTAUbL2, but all mutants shows antiviral activity to inhibit the replication of the WNV replicon except for the ChOAS-L-ADELTAUbL1/UbL2, which shows a partial inhibition compared to the wild-type ChOAS-L-A or the other mutant enzyme variants
additional information
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substitutions of amino acids in front of the P-loop of Lys42 and Lys60 as well as that of Arg195 reduce the 2'-5'OAS activity at least 50fold. Furthermore substitutions in the Lys199 and Lys204 reduce the activity more than a 1000fold
additional information
OAS2 knockdown increases ZIKV replication. Overexpression of OAS2 modestly increases the IFN-induced p-STAT1 both with IFN treatment and without IFN treatment compared to control. OAS2 overexpression also increases ISRE activity and some classical ISGs expression including Myxovirus resistance-A (MxA) and interferon-induced protein 2 (IFIT2)
additional information
OASL knockdown via siRNA
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expression in transgenic Solanum tuberosum plants using the Agrobacterium tumefaciens transfection system, the transformed plants show increased resistance against potato virus X, virus concentration is much lower in leaves and tubers compared to wild-type plants, the virus concentrations are almost that low in transgenic plants expressing the potato virus X coat protein
expression of tagged isozyme OAS1 in Escherichia coli
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functional expression of p42 isoform of OAS1 and the p69 isoform of OAS2 in insect cells
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gene LB2-5OAS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of myc- and His-tagged enzyme in Escherichhia coli
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gene N308_13623, DNA and amino acid sequence determination and analysis, sequence comparisons of avian OASL enzymes, phylogenetic analysis, recombinant expression of EGFP-tagged enzyme in HEK-293FT and BHK-21 cells
gene OAS-L, DNA and amino acid sequence determination and analysis, sequence comparisons of avian OASL enzymes, phylogenetic analysis, recombinant expression of EGFP-tagged enzyme in HEK-293FT and BHK-21 cells
gene OAS1, cloning of paralogues OAS1a-OAS1h, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of EGFP-tagged isozyme paralogue in HEK-293T cell
gene OAS1, recombinant expression of His-tagged OAS1 p42 isoform in Escherichia coli strain BL21(DE3)RIL
gene OAS1, sequence comparisons
gene OAS1, the gene is 25414 base pairs long and consists of eight exons. Of these exons, the first five exons from the 5' end are translated into the core protein while the latter three exons enable alternative splicing into the six known protein isoforms of OAS1. Two of these isoforms are the p42 and p46 variants named due to their theoretical size of about 42 and about 46 kDa, the expression pattern between these two variants is related to one single nucleotide polymorphism (SNP), the SNP rs10774671. The SNP is an A/G variation locates in the splice acceptor site of exon 7 which results in either the A allele expressing the p42 isoform or the G allele expressing the p46 isoform. Recombinant expression of C-terminally EGFP-tagged isozymes in HeLa cells, where the C-terminus of OAS1 p46 and its CaaX motif is in itself not enough for membrane translocation
gene OAS2, DNA and amino acid sequencing, RNA sequence library production, and complete transcriptome analysis of A549 cells with and without Zika virus (ZIKV) infection, quantitative real-time PCR expression analysis
gene OAS2, recombinant expression of N-terminally FLAG-tagged OAS1 p69 isoform in Escherichia coli, and of N-terminally FLAG-tagged OAS2 domain I (DI1-331) or domain II (DII332-687), recombinant expression of N-terminally FLAG-tagged OAS2 in HEK-293T cells
gene OAS2, sequence comparisons
gene OAS3, sequence comparisons
gene OASL, DNA and amino acid sequence determination and analysis, sequence comparisons of avian OASL enzymes, phylogenetic analysis, recombinant expression of EGFP-tagged enzyme in HEK-293FT and BHK-21 cells
gene OASL, wild-type and mutant enzymes are ectopically expressed in HEK 293FT cells to analyze the enzymatic activity, and in BHK-21 and BALB/3T3 cells to analyze the antiviral activity using WNV replicon
OAS1, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
stable Oas1b protein overexpression under the control of the Tet-Off expression system in a mouse fibroblastic cell line, MEF/3T3.Tet-Off. The murine cells respond to Oas1b expression by efficiently inhibiting WNV viral replication
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three distinct forms of 2'-5'OAS exist in human cells, small, medium, and large, which contain one, two, and three OAS units, respectively, and are encoded by distinct genes, clustering of the genes encoding OAS1, OAS2, OAS3 and OASL on human chromosome 12q24.2, genetic organization, expression of isozyme OAS3 and the two forms of OAS2 in HeLa cells, expression of recombinant OAS2 in insect cells
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gene OAS-L, DNA and amino acid sequence determination and analysis, sequence comparisons of avian OASL enzymes, phylogenetic analysis, recombinant expression of EGFP-tagged enzyme in HEK-293FT and BHK-21 cells
gene OAS-L, DNA and amino acid sequence determination and analysis, sequence comparisons of avian OASL enzymes, phylogenetic analysis, recombinant expression of EGFP-tagged enzyme in HEK-293FT and BHK-21 cells
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Homo sapiens (P00973), Homo sapiens
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12
418
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Homo sapiens (P29728)
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