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LitCovid-PMC-OGER-BB

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T79","span":{"begin":156,"end":163},"obj":"Body_part"},{"id":"T80","span":{"begin":789,"end":796},"obj":"Body_part"},{"id":"T81","span":{"begin":1195,"end":1202},"obj":"Body_part"},{"id":"T82","span":{"begin":1827,"end":1834},"obj":"Body_part"},{"id":"T83","span":{"begin":2678,"end":2685},"obj":"Body_part"}],"attributes":[{"id":"A79","pred":"fma_id","subj":"T79","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A80","pred":"fma_id","subj":"T80","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A81","pred":"fma_id","subj":"T81","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A82","pred":"fma_id","subj":"T82","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A83","pred":"fma_id","subj":"T83","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"2.5 Thermal shift DSF assays for SARS-CoV nsp14\nSARS-CoV nsp14-inhibitor interactions were further investigated by monitoring the thermal stability of the protein using differential scanning fluorimetry (DSF) (Supporting Information, Fig. S3) [34]. The change in thermal stability of SARS-CoV nsp14 was monitored in response to binding of the natural cofactor substrate SAM, sinefungin and the 9 most active and specific compounds 6 and 9–16 with IC50 \u003c 100 μM. As expected, SARS-CoV nsp14 displayed an increased melting temperature (T m) value with SAM (+6.5 °C) and sinefungin (+4.4 °C) whose structure only differs by a C–NH2 in place of S+-CH3 group in SAM (Fig. 2 ). The binding experiments with the bisubstrate inhibitors showed that all dinucleosides stabilized the SARS-CoV nsp14 protein (T m \u003e 40 °C) with a T m shift from +4.6 °C to +10.8 °C (Supporting Information, Table S1). Eight of the 9 examined compounds increased the stability of SARS-CoV nsp14 more efficiently than the well-known inhibitor sinefungin. More interestingly, T m values for SARS-CoV nsp14 were larger in the presence of five compounds 10 and 12–15 than with the natural enzyme substrate SAM, suggesting strong protein-inhibitor interactions. Remarkably, the highest T m was observed with the most efficient inhibitor 13 (IC50 0.6 ± 0.1 μM) that stabilizes SARS-CoV nsp14 against thermal denaturation with a ΔT m +10.8 °C and exhibits notable binding affinity (apparent KD 1.3 ± 0.87 μM), as deduced from TSA performed with increasing concentration of compound 13. This demonstrates a favorable interaction and highlights the inhibitor potential of compound 13. The T m comparison of compounds 16, 15 and 13 showed a respective increase in SARS-CoV nsp14 stability, settling the importance of the sulfone group, the Cl and NO2 substituents in protein binding with 13. Thus the N-(4-Cl-3-NO2-phenylsulfonamide) moiety is notably preferred for optimal SARS-CoV nsp14 interactions. Another highlight is the thermal shift (+5.4 °C) for SARS-CoV nsp14 observed in the presence of compound 10 compared to 11, both only differ by the position of OCH3 and NO2 substituents in the phenyl ring. A higher stability and inhibition of SARS-CoV nsp14 was observed when the OCH3 group is in “para” position in dinucleoside 10.\nFig. 2 Thermal shifts (ΔTm) of SARS-CoV nsp14 in the absence or presence of SAM, sinefungin and 9 dinucleoside inhibitors 6 and 9–16. Thermal stability of SARS-CoV nsp14 upon ligand binding was monitored by differential scanning fluorimetry. Assays were carried out in reaction mixture [20 mM HEPES (pH 7.5), 150 mM NaCl, 1x SYPRO orange dye] in the presence of 5 μM SARS-CoV nsp14 protein and 1 mM compound previously dissolved in 100% DMSO. The bars and error bars correspond to the mean values from three independent measurements and their s.d.’s, respectively."}

LitCovid-PubTator

{"project":"LitCovid-PubTator","denotations":[{"id":"439","span":{"begin":2377,"end":2387},"obj":"Chemical"},{"id":"440","span":{"begin":2589,"end":2594},"obj":"Chemical"},{"id":"441","span":{"begin":2612,"end":2616},"obj":"Chemical"},{"id":"442","span":{"begin":2621,"end":2633},"obj":"Chemical"},{"id":"443","span":{"begin":2733,"end":2737},"obj":"Chemical"},{"id":"451","span":{"begin":376,"end":386},"obj":"Chemical"},{"id":"452","span":{"begin":745,"end":758},"obj":"Chemical"},{"id":"453","span":{"begin":1012,"end":1022},"obj":"Chemical"},{"id":"454","span":{"begin":1781,"end":1788},"obj":"Chemical"},{"id":"455","span":{"begin":1807,"end":1810},"obj":"Chemical"},{"id":"456","span":{"begin":1861,"end":1892},"obj":"Chemical"},{"id":"457","span":{"begin":2279,"end":2291},"obj":"Chemical"}],"attributes":[{"id":"A439","pred":"tao:has_database_id","subj":"439","obj":"MESH:C006235"},{"id":"A440","pred":"tao:has_database_id","subj":"440","obj":"MESH:D006531"},{"id":"A441","pred":"tao:has_database_id","subj":"441","obj":"MESH:D012965"},{"id":"A443","pred":"tao:has_database_id","subj":"443","obj":"MESH:D004121"},{"id":"A451","pred":"tao:has_database_id","subj":"451","obj":"MESH:C006235"},{"id":"A453","pred":"tao:has_database_id","subj":"453","obj":"MESH:C006235"},{"id":"A454","pred":"tao:has_database_id","subj":"454","obj":"MESH:D013450"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"2.5 Thermal shift DSF assays for SARS-CoV nsp14\nSARS-CoV nsp14-inhibitor interactions were further investigated by monitoring the thermal stability of the protein using differential scanning fluorimetry (DSF) (Supporting Information, Fig. S3) [34]. The change in thermal stability of SARS-CoV nsp14 was monitored in response to binding of the natural cofactor substrate SAM, sinefungin and the 9 most active and specific compounds 6 and 9–16 with IC50 \u003c 100 μM. As expected, SARS-CoV nsp14 displayed an increased melting temperature (T m) value with SAM (+6.5 °C) and sinefungin (+4.4 °C) whose structure only differs by a C–NH2 in place of S+-CH3 group in SAM (Fig. 2 ). The binding experiments with the bisubstrate inhibitors showed that all dinucleosides stabilized the SARS-CoV nsp14 protein (T m \u003e 40 °C) with a T m shift from +4.6 °C to +10.8 °C (Supporting Information, Table S1). Eight of the 9 examined compounds increased the stability of SARS-CoV nsp14 more efficiently than the well-known inhibitor sinefungin. More interestingly, T m values for SARS-CoV nsp14 were larger in the presence of five compounds 10 and 12–15 than with the natural enzyme substrate SAM, suggesting strong protein-inhibitor interactions. Remarkably, the highest T m was observed with the most efficient inhibitor 13 (IC50 0.6 ± 0.1 μM) that stabilizes SARS-CoV nsp14 against thermal denaturation with a ΔT m +10.8 °C and exhibits notable binding affinity (apparent KD 1.3 ± 0.87 μM), as deduced from TSA performed with increasing concentration of compound 13. This demonstrates a favorable interaction and highlights the inhibitor potential of compound 13. The T m comparison of compounds 16, 15 and 13 showed a respective increase in SARS-CoV nsp14 stability, settling the importance of the sulfone group, the Cl and NO2 substituents in protein binding with 13. Thus the N-(4-Cl-3-NO2-phenylsulfonamide) moiety is notably preferred for optimal SARS-CoV nsp14 interactions. Another highlight is the thermal shift (+5.4 °C) for SARS-CoV nsp14 observed in the presence of compound 10 compared to 11, both only differ by the position of OCH3 and NO2 substituents in the phenyl ring. A higher stability and inhibition of SARS-CoV nsp14 was observed when the OCH3 group is in “para” position in dinucleoside 10.\nFig. 2 Thermal shifts (ΔTm) of SARS-CoV nsp14 in the absence or presence of SAM, sinefungin and 9 dinucleoside inhibitors 6 and 9–16. Thermal stability of SARS-CoV nsp14 upon ligand binding was monitored by differential scanning fluorimetry. Assays were carried out in reaction mixture [20 mM HEPES (pH 7.5), 150 mM NaCl, 1x SYPRO orange dye] in the presence of 5 μM SARS-CoV nsp14 protein and 1 mM compound previously dissolved in 100% DMSO. The bars and error bars correspond to the mean values from three independent measurements and their s.d.’s, respectively."}

LitCovid-PD-MONDO

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T213","span":{"begin":245,"end":247},"obj":"http://purl.obolibrary.org/obo/CLO_0001302"},{"id":"T214","span":{"begin":402,"end":408},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T215","span":{"begin":622,"end":623},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T216","span":{"begin":816,"end":817},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T217","span":{"begin":884,"end":886},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T218","span":{"begin":1390,"end":1391},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T219","span":{"begin":1489,"end":1492},"obj":"http://purl.obolibrary.org/obo/CLO_0009405"},{"id":"T220","span":{"begin":1567,"end":1568},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T221","span":{"begin":1699,"end":1700},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T222","span":{"begin":1800,"end":1802},"obj":"http://purl.obolibrary.org/obo/CLO_0052906"},{"id":"T223","span":{"begin":1866,"end":1870},"obj":"http://purl.obolibrary.org/obo/CLO_0002489"},{"id":"T224","span":{"begin":2083,"end":2085},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T225","span":{"begin":2169,"end":2170},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"2.5 Thermal shift DSF assays for SARS-CoV nsp14\nSARS-CoV nsp14-inhibitor interactions were further investigated by monitoring the thermal stability of the protein using differential scanning fluorimetry (DSF) (Supporting Information, Fig. S3) [34]. The change in thermal stability of SARS-CoV nsp14 was monitored in response to binding of the natural cofactor substrate SAM, sinefungin and the 9 most active and specific compounds 6 and 9–16 with IC50 \u003c 100 μM. As expected, SARS-CoV nsp14 displayed an increased melting temperature (T m) value with SAM (+6.5 °C) and sinefungin (+4.4 °C) whose structure only differs by a C–NH2 in place of S+-CH3 group in SAM (Fig. 2 ). The binding experiments with the bisubstrate inhibitors showed that all dinucleosides stabilized the SARS-CoV nsp14 protein (T m \u003e 40 °C) with a T m shift from +4.6 °C to +10.8 °C (Supporting Information, Table S1). Eight of the 9 examined compounds increased the stability of SARS-CoV nsp14 more efficiently than the well-known inhibitor sinefungin. More interestingly, T m values for SARS-CoV nsp14 were larger in the presence of five compounds 10 and 12–15 than with the natural enzyme substrate SAM, suggesting strong protein-inhibitor interactions. Remarkably, the highest T m was observed with the most efficient inhibitor 13 (IC50 0.6 ± 0.1 μM) that stabilizes SARS-CoV nsp14 against thermal denaturation with a ΔT m +10.8 °C and exhibits notable binding affinity (apparent KD 1.3 ± 0.87 μM), as deduced from TSA performed with increasing concentration of compound 13. This demonstrates a favorable interaction and highlights the inhibitor potential of compound 13. The T m comparison of compounds 16, 15 and 13 showed a respective increase in SARS-CoV nsp14 stability, settling the importance of the sulfone group, the Cl and NO2 substituents in protein binding with 13. Thus the N-(4-Cl-3-NO2-phenylsulfonamide) moiety is notably preferred for optimal SARS-CoV nsp14 interactions. Another highlight is the thermal shift (+5.4 °C) for SARS-CoV nsp14 observed in the presence of compound 10 compared to 11, both only differ by the position of OCH3 and NO2 substituents in the phenyl ring. A higher stability and inhibition of SARS-CoV nsp14 was observed when the OCH3 group is in “para” position in dinucleoside 10.\nFig. 2 Thermal shifts (ΔTm) of SARS-CoV nsp14 in the absence or presence of SAM, sinefungin and 9 dinucleoside inhibitors 6 and 9–16. Thermal stability of SARS-CoV nsp14 upon ligand binding was monitored by differential scanning fluorimetry. Assays were carried out in reaction mixture [20 mM HEPES (pH 7.5), 150 mM NaCl, 1x SYPRO orange dye] in the presence of 5 μM SARS-CoV nsp14 protein and 1 mM compound previously dissolved in 100% DMSO. The bars and error bars correspond to the mean values from three independent measurements and their s.d.’s, respectively."}

LitCovid-PD-CHEBI

2_test

{"project":"2_test","denotations":[{"id":"32563813-17853878-29105589","span":{"begin":245,"end":247},"obj":"17853878"}],"text":"2.5 Thermal shift DSF assays for SARS-CoV nsp14\nSARS-CoV nsp14-inhibitor interactions were further investigated by monitoring the thermal stability of the protein using differential scanning fluorimetry (DSF) (Supporting Information, Fig. S3) [34]. The change in thermal stability of SARS-CoV nsp14 was monitored in response to binding of the natural cofactor substrate SAM, sinefungin and the 9 most active and specific compounds 6 and 9–16 with IC50 \u003c 100 μM. As expected, SARS-CoV nsp14 displayed an increased melting temperature (T m) value with SAM (+6.5 °C) and sinefungin (+4.4 °C) whose structure only differs by a C–NH2 in place of S+-CH3 group in SAM (Fig. 2 ). The binding experiments with the bisubstrate inhibitors showed that all dinucleosides stabilized the SARS-CoV nsp14 protein (T m \u003e 40 °C) with a T m shift from +4.6 °C to +10.8 °C (Supporting Information, Table S1). Eight of the 9 examined compounds increased the stability of SARS-CoV nsp14 more efficiently than the well-known inhibitor sinefungin. More interestingly, T m values for SARS-CoV nsp14 were larger in the presence of five compounds 10 and 12–15 than with the natural enzyme substrate SAM, suggesting strong protein-inhibitor interactions. Remarkably, the highest T m was observed with the most efficient inhibitor 13 (IC50 0.6 ± 0.1 μM) that stabilizes SARS-CoV nsp14 against thermal denaturation with a ΔT m +10.8 °C and exhibits notable binding affinity (apparent KD 1.3 ± 0.87 μM), as deduced from TSA performed with increasing concentration of compound 13. This demonstrates a favorable interaction and highlights the inhibitor potential of compound 13. The T m comparison of compounds 16, 15 and 13 showed a respective increase in SARS-CoV nsp14 stability, settling the importance of the sulfone group, the Cl and NO2 substituents in protein binding with 13. Thus the N-(4-Cl-3-NO2-phenylsulfonamide) moiety is notably preferred for optimal SARS-CoV nsp14 interactions. Another highlight is the thermal shift (+5.4 °C) for SARS-CoV nsp14 observed in the presence of compound 10 compared to 11, both only differ by the position of OCH3 and NO2 substituents in the phenyl ring. A higher stability and inhibition of SARS-CoV nsp14 was observed when the OCH3 group is in “para” position in dinucleoside 10.\nFig. 2 Thermal shifts (ΔTm) of SARS-CoV nsp14 in the absence or presence of SAM, sinefungin and 9 dinucleoside inhibitors 6 and 9–16. Thermal stability of SARS-CoV nsp14 upon ligand binding was monitored by differential scanning fluorimetry. Assays were carried out in reaction mixture [20 mM HEPES (pH 7.5), 150 mM NaCl, 1x SYPRO orange dye] in the presence of 5 μM SARS-CoV nsp14 protein and 1 mM compound previously dissolved in 100% DMSO. The bars and error bars correspond to the mean values from three independent measurements and their s.d.’s, respectively."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T184","span":{"begin":0,"end":48},"obj":"Sentence"},{"id":"T185","span":{"begin":49,"end":249},"obj":"Sentence"},{"id":"T186","span":{"begin":250,"end":462},"obj":"Sentence"},{"id":"T187","span":{"begin":463,"end":672},"obj":"Sentence"},{"id":"T188","span":{"begin":673,"end":888},"obj":"Sentence"},{"id":"T189","span":{"begin":889,"end":1023},"obj":"Sentence"},{"id":"T190","span":{"begin":1024,"end":1226},"obj":"Sentence"},{"id":"T191","span":{"begin":1227,"end":1548},"obj":"Sentence"},{"id":"T192","span":{"begin":1549,"end":1645},"obj":"Sentence"},{"id":"T193","span":{"begin":1646,"end":1851},"obj":"Sentence"},{"id":"T194","span":{"begin":1852,"end":1962},"obj":"Sentence"},{"id":"T195","span":{"begin":1963,"end":2168},"obj":"Sentence"},{"id":"T196","span":{"begin":2169,"end":2295},"obj":"Sentence"},{"id":"T197","span":{"begin":2296,"end":2429},"obj":"Sentence"},{"id":"T198","span":{"begin":2430,"end":2537},"obj":"Sentence"},{"id":"T199","span":{"begin":2538,"end":2738},"obj":"Sentence"},{"id":"T200","span":{"begin":2739,"end":2860},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"2.5 Thermal shift DSF assays for SARS-CoV nsp14\nSARS-CoV nsp14-inhibitor interactions were further investigated by monitoring the thermal stability of the protein using differential scanning fluorimetry (DSF) (Supporting Information, Fig. S3) [34]. The change in thermal stability of SARS-CoV nsp14 was monitored in response to binding of the natural cofactor substrate SAM, sinefungin and the 9 most active and specific compounds 6 and 9–16 with IC50 \u003c 100 μM. As expected, SARS-CoV nsp14 displayed an increased melting temperature (T m) value with SAM (+6.5 °C) and sinefungin (+4.4 °C) whose structure only differs by a C–NH2 in place of S+-CH3 group in SAM (Fig. 2 ). The binding experiments with the bisubstrate inhibitors showed that all dinucleosides stabilized the SARS-CoV nsp14 protein (T m \u003e 40 °C) with a T m shift from +4.6 °C to +10.8 °C (Supporting Information, Table S1). Eight of the 9 examined compounds increased the stability of SARS-CoV nsp14 more efficiently than the well-known inhibitor sinefungin. More interestingly, T m values for SARS-CoV nsp14 were larger in the presence of five compounds 10 and 12–15 than with the natural enzyme substrate SAM, suggesting strong protein-inhibitor interactions. Remarkably, the highest T m was observed with the most efficient inhibitor 13 (IC50 0.6 ± 0.1 μM) that stabilizes SARS-CoV nsp14 against thermal denaturation with a ΔT m +10.8 °C and exhibits notable binding affinity (apparent KD 1.3 ± 0.87 μM), as deduced from TSA performed with increasing concentration of compound 13. This demonstrates a favorable interaction and highlights the inhibitor potential of compound 13. The T m comparison of compounds 16, 15 and 13 showed a respective increase in SARS-CoV nsp14 stability, settling the importance of the sulfone group, the Cl and NO2 substituents in protein binding with 13. Thus the N-(4-Cl-3-NO2-phenylsulfonamide) moiety is notably preferred for optimal SARS-CoV nsp14 interactions. Another highlight is the thermal shift (+5.4 °C) for SARS-CoV nsp14 observed in the presence of compound 10 compared to 11, both only differ by the position of OCH3 and NO2 substituents in the phenyl ring. A higher stability and inhibition of SARS-CoV nsp14 was observed when the OCH3 group is in “para” position in dinucleoside 10.\nFig. 2 Thermal shifts (ΔTm) of SARS-CoV nsp14 in the absence or presence of SAM, sinefungin and 9 dinucleoside inhibitors 6 and 9–16. Thermal stability of SARS-CoV nsp14 upon ligand binding was monitored by differential scanning fluorimetry. Assays were carried out in reaction mixture [20 mM HEPES (pH 7.5), 150 mM NaCl, 1x SYPRO orange dye] in the presence of 5 μM SARS-CoV nsp14 protein and 1 mM compound previously dissolved in 100% DMSO. The bars and error bars correspond to the mean values from three independent measurements and their s.d.’s, respectively."}

MyTest

{"project":"MyTest","denotations":[{"id":"32563813-17853878-29105589","span":{"begin":245,"end":247},"obj":"17853878"}],"namespaces":[{"prefix":"_base","uri":"https://www.uniprot.org/uniprot/testbase"},{"prefix":"UniProtKB","uri":"https://www.uniprot.org/uniprot/"},{"prefix":"uniprot","uri":"https://www.uniprot.org/uniprotkb/"}],"text":"2.5 Thermal shift DSF assays for SARS-CoV nsp14\nSARS-CoV nsp14-inhibitor interactions were further investigated by monitoring the thermal stability of the protein using differential scanning fluorimetry (DSF) (Supporting Information, Fig. S3) [34]. The change in thermal stability of SARS-CoV nsp14 was monitored in response to binding of the natural cofactor substrate SAM, sinefungin and the 9 most active and specific compounds 6 and 9–16 with IC50 \u003c 100 μM. As expected, SARS-CoV nsp14 displayed an increased melting temperature (T m) value with SAM (+6.5 °C) and sinefungin (+4.4 °C) whose structure only differs by a C–NH2 in place of S+-CH3 group in SAM (Fig. 2 ). The binding experiments with the bisubstrate inhibitors showed that all dinucleosides stabilized the SARS-CoV nsp14 protein (T m \u003e 40 °C) with a T m shift from +4.6 °C to +10.8 °C (Supporting Information, Table S1). Eight of the 9 examined compounds increased the stability of SARS-CoV nsp14 more efficiently than the well-known inhibitor sinefungin. More interestingly, T m values for SARS-CoV nsp14 were larger in the presence of five compounds 10 and 12–15 than with the natural enzyme substrate SAM, suggesting strong protein-inhibitor interactions. Remarkably, the highest T m was observed with the most efficient inhibitor 13 (IC50 0.6 ± 0.1 μM) that stabilizes SARS-CoV nsp14 against thermal denaturation with a ΔT m +10.8 °C and exhibits notable binding affinity (apparent KD 1.3 ± 0.87 μM), as deduced from TSA performed with increasing concentration of compound 13. This demonstrates a favorable interaction and highlights the inhibitor potential of compound 13. The T m comparison of compounds 16, 15 and 13 showed a respective increase in SARS-CoV nsp14 stability, settling the importance of the sulfone group, the Cl and NO2 substituents in protein binding with 13. Thus the N-(4-Cl-3-NO2-phenylsulfonamide) moiety is notably preferred for optimal SARS-CoV nsp14 interactions. Another highlight is the thermal shift (+5.4 °C) for SARS-CoV nsp14 observed in the presence of compound 10 compared to 11, both only differ by the position of OCH3 and NO2 substituents in the phenyl ring. A higher stability and inhibition of SARS-CoV nsp14 was observed when the OCH3 group is in “para” position in dinucleoside 10.\nFig. 2 Thermal shifts (ΔTm) of SARS-CoV nsp14 in the absence or presence of SAM, sinefungin and 9 dinucleoside inhibitors 6 and 9–16. Thermal stability of SARS-CoV nsp14 upon ligand binding was monitored by differential scanning fluorimetry. Assays were carried out in reaction mixture [20 mM HEPES (pH 7.5), 150 mM NaCl, 1x SYPRO orange dye] in the presence of 5 μM SARS-CoV nsp14 protein and 1 mM compound previously dissolved in 100% DMSO. The bars and error bars correspond to the mean values from three independent measurements and their s.d.’s, respectively."}

PMC:7291971 / 25171-28031 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7291971 / 25171-28031 JSON TXT