PMC:7094172 / 28510-29811 JSONTXT

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    LitCovid-PMC-OGER-BB

    {"project":"LitCovid-PMC-OGER-BB","denotations":[{"id":"T459","span":{"begin":4,"end":12},"obj":"SP_9"},{"id":"T458","span":{"begin":115,"end":123},"obj":"SP_9"},{"id":"T457","span":{"begin":162,"end":172},"obj":"GO:0010467"},{"id":"T456","span":{"begin":173,"end":179},"obj":"SO:0000440"},{"id":"T455","span":{"begin":391,"end":398},"obj":"SO:0000112"},{"id":"T454","span":{"begin":423,"end":430},"obj":"SO:0000440"},{"id":"T453","span":{"begin":436,"end":447},"obj":"GO:0009294"},{"id":"T452","span":{"begin":453,"end":469},"obj":"NCBITaxon:562"},{"id":"T451","span":{"begin":509,"end":514},"obj":"GO:0040007"},{"id":"T450","span":{"begin":577,"end":584},"obj":"BV_20"},{"id":"T449","span":{"begin":585,"end":595},"obj":"BV_20;GO:0010467"},{"id":"T448","span":{"begin":616,"end":625},"obj":"CHEBI:30353;CHEBI:30353"},{"id":"T447","span":{"begin":626,"end":653},"obj":"CHEBI:75055;CHEBI:75055"},{"id":"T446","span":{"begin":655,"end":659},"obj":"CHEBI:61448;CHEBI:61448"},{"id":"T445","span":{"begin":788,"end":793},"obj":"GO:0019835"},{"id":"T444","span":{"begin":809,"end":813},"obj":"CHEBI:26710;CHEBI:26710"},{"id":"T443","span":{"begin":821,"end":825},"obj":"CHEBI:9754;CHEBI:9754"},{"id":"T442","span":{"begin":826,"end":829},"obj":"CHEBI:17883;CHEBI:17883"},{"id":"T441","span":{"begin":837,"end":846},"obj":"CHEBI:14434;CHEBI:14434"},{"id":"T440","span":{"begin":857,"end":861},"obj":"CHEBI:8102;CHEBI:8102"},{"id":"T439","span":{"begin":887,"end":892},"obj":"GO:0019835"},{"id":"T438","span":{"begin":1016,"end":1019},"obj":"CHEBI:39054;CHEBI:39054"},{"id":"T437","span":{"begin":1089,"end":1098},"obj":"CHEBI:14434;CHEBI:14434"},{"id":"T436","span":{"begin":1190,"end":1194},"obj":"CHEBI:24866;CHEBI:24866"}],"text":"The MERS-CoV N proteins were prepared according to previously described methods.46 In brief, the cDNA fragments of MERS-CoV N proteins were cloned into a pET-28a expression vector (Merck, Darmstadt, Germany) containing a histidine tag-encoding sequence. Vectors encoding the single mutants N39A, N39G, and W43A were generated using the QuikChange site-directed mutagenesis protocol with the primers listed in Table S3. The vectors were transformed into Escherichia coli BL21 (DE3) pLysS cells. The cells were grown to an optical density range of 0.6–0.8 at 600 nm at 37 °C and protein expression induced with 1.0 mM isopropyl β-d-1-thiogalactopyranoside (IPTG), followed by incubation at 10 °C for 24 h. The cells were harvested by centrifugation (6000g, 12 min, 4 °C) and resuspended in lysis buffer (150 mM NaCl, 50 mM Tris-HCl, 15 mM imidazole, and 1 mM PMSF; pH 7.5). The cells were lysed by sonication and centrifuged (10000g, 40 min, 4 °C) to remove debris. The supernatant was purified by injection into a Ni–NTA column (Merck, Darmstadt, Germany) and eluted with buffer containing imidazole at a gradient range of 15–300 mM. Pure protein fractions were collected, dialyzed with low-salt buffer, concentrated, and quantified by the Bradford method (BioShop Canada Inc., Burlington, ON, Canada)."}

    LitCovid-PD-FMA-UBERON

    {"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T135","span":{"begin":15,"end":23},"obj":"Body_part"},{"id":"T136","span":{"begin":126,"end":134},"obj":"Body_part"},{"id":"T137","span":{"begin":221,"end":230},"obj":"Body_part"},{"id":"T138","span":{"begin":487,"end":492},"obj":"Body_part"},{"id":"T139","span":{"begin":498,"end":503},"obj":"Body_part"},{"id":"T140","span":{"begin":577,"end":584},"obj":"Body_part"},{"id":"T141","span":{"begin":708,"end":713},"obj":"Body_part"},{"id":"T142","span":{"begin":876,"end":881},"obj":"Body_part"},{"id":"T143","span":{"begin":1138,"end":1145},"obj":"Body_part"}],"attributes":[{"id":"A135","pred":"fma_id","subj":"T135","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A136","pred":"fma_id","subj":"T136","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A137","pred":"fma_id","subj":"T137","obj":"http://purl.org/sig/ont/fma/fma82755"},{"id":"A138","pred":"fma_id","subj":"T138","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A139","pred":"fma_id","subj":"T139","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A140","pred":"fma_id","subj":"T140","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A141","pred":"fma_id","subj":"T141","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A142","pred":"fma_id","subj":"T142","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A143","pred":"fma_id","subj":"T143","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"The MERS-CoV N proteins were prepared according to previously described methods.46 In brief, the cDNA fragments of MERS-CoV N proteins were cloned into a pET-28a expression vector (Merck, Darmstadt, Germany) containing a histidine tag-encoding sequence. Vectors encoding the single mutants N39A, N39G, and W43A were generated using the QuikChange site-directed mutagenesis protocol with the primers listed in Table S3. The vectors were transformed into Escherichia coli BL21 (DE3) pLysS cells. The cells were grown to an optical density range of 0.6–0.8 at 600 nm at 37 °C and protein expression induced with 1.0 mM isopropyl β-d-1-thiogalactopyranoside (IPTG), followed by incubation at 10 °C for 24 h. The cells were harvested by centrifugation (6000g, 12 min, 4 °C) and resuspended in lysis buffer (150 mM NaCl, 50 mM Tris-HCl, 15 mM imidazole, and 1 mM PMSF; pH 7.5). The cells were lysed by sonication and centrifuged (10000g, 40 min, 4 °C) to remove debris. The supernatant was purified by injection into a Ni–NTA column (Merck, Darmstadt, Germany) and eluted with buffer containing imidazole at a gradient range of 15–300 mM. Pure protein fractions were collected, dialyzed with low-salt buffer, concentrated, and quantified by the Bradford method (BioShop Canada Inc., Burlington, ON, Canada)."}

    LitCovid-PD-CLO

    {"project":"LitCovid-PD-CLO","denotations":[{"id":"T212","span":{"begin":152,"end":153},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T213","span":{"begin":219,"end":220},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T214","span":{"begin":487,"end":492},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T215","span":{"begin":498,"end":503},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T216","span":{"begin":708,"end":713},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T217","span":{"begin":763,"end":767},"obj":"http://purl.obolibrary.org/obo/CLO_0001387"},{"id":"T218","span":{"begin":876,"end":881},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T219","span":{"begin":940,"end":944},"obj":"http://purl.obolibrary.org/obo/CLO_0001387"},{"id":"T220","span":{"begin":1011,"end":1012},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T221","span":{"begin":1102,"end":1103},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"The MERS-CoV N proteins were prepared according to previously described methods.46 In brief, the cDNA fragments of MERS-CoV N proteins were cloned into a pET-28a expression vector (Merck, Darmstadt, Germany) containing a histidine tag-encoding sequence. Vectors encoding the single mutants N39A, N39G, and W43A were generated using the QuikChange site-directed mutagenesis protocol with the primers listed in Table S3. The vectors were transformed into Escherichia coli BL21 (DE3) pLysS cells. The cells were grown to an optical density range of 0.6–0.8 at 600 nm at 37 °C and protein expression induced with 1.0 mM isopropyl β-d-1-thiogalactopyranoside (IPTG), followed by incubation at 10 °C for 24 h. The cells were harvested by centrifugation (6000g, 12 min, 4 °C) and resuspended in lysis buffer (150 mM NaCl, 50 mM Tris-HCl, 15 mM imidazole, and 1 mM PMSF; pH 7.5). The cells were lysed by sonication and centrifuged (10000g, 40 min, 4 °C) to remove debris. The supernatant was purified by injection into a Ni–NTA column (Merck, Darmstadt, Germany) and eluted with buffer containing imidazole at a gradient range of 15–300 mM. Pure protein fractions were collected, dialyzed with low-salt buffer, concentrated, and quantified by the Bradford method (BioShop Canada Inc., Burlington, ON, Canada)."}

    LitCovid-PD-CHEBI

    {"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T241","span":{"begin":15,"end":23},"obj":"Chemical"},{"id":"T242","span":{"begin":126,"end":134},"obj":"Chemical"},{"id":"T243","span":{"begin":221,"end":230},"obj":"Chemical"},{"id":"T244","span":{"begin":415,"end":417},"obj":"Chemical"},{"id":"T245","span":{"begin":577,"end":584},"obj":"Chemical"},{"id":"T246","span":{"begin":616,"end":625},"obj":"Chemical"},{"id":"T247","span":{"begin":655,"end":659},"obj":"Chemical"},{"id":"T248","span":{"begin":794,"end":800},"obj":"Chemical"},{"id":"T249","span":{"begin":809,"end":813},"obj":"Chemical"},{"id":"T250","span":{"begin":821,"end":825},"obj":"Chemical"},{"id":"T251","span":{"begin":826,"end":829},"obj":"Chemical"},{"id":"T252","span":{"begin":837,"end":846},"obj":"Chemical"},{"id":"T254","span":{"begin":857,"end":861},"obj":"Chemical"},{"id":"T255","span":{"begin":1013,"end":1015},"obj":"Chemical"},{"id":"T256","span":{"begin":1016,"end":1019},"obj":"Chemical"},{"id":"T258","span":{"begin":1071,"end":1077},"obj":"Chemical"},{"id":"T259","span":{"begin":1089,"end":1098},"obj":"Chemical"},{"id":"T261","span":{"begin":1138,"end":1145},"obj":"Chemical"},{"id":"T262","span":{"begin":1190,"end":1194},"obj":"Chemical"},{"id":"T264","span":{"begin":1195,"end":1201},"obj":"Chemical"}],"attributes":[{"id":"A241","pred":"chebi_id","subj":"T241","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A242","pred":"chebi_id","subj":"T242","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A243","pred":"chebi_id","subj":"T243","obj":"http://purl.obolibrary.org/obo/CHEBI_27570"},{"id":"A244","pred":"chebi_id","subj":"T244","obj":"http://purl.obolibrary.org/obo/CHEBI_29388"},{"id":"A245","pred":"chebi_id","subj":"T245","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A246","pred":"chebi_id","subj":"T246","obj":"http://purl.obolibrary.org/obo/CHEBI_30353"},{"id":"A247","pred":"chebi_id","subj":"T247","obj":"http://purl.obolibrary.org/obo/CHEBI_61448"},{"id":"A248","pred":"chebi_id","subj":"T248","obj":"http://purl.obolibrary.org/obo/CHEBI_35225"},{"id":"A249","pred":"chebi_id","subj":"T249","obj":"http://purl.obolibrary.org/obo/CHEBI_26710"},{"id":"A250","pred":"chebi_id","subj":"T250","obj":"http://purl.obolibrary.org/obo/CHEBI_9754"},{"id":"A251","pred":"chebi_id","subj":"T251","obj":"http://purl.obolibrary.org/obo/CHEBI_17883"},{"id":"A252","pred":"chebi_id","subj":"T252","obj":"http://purl.obolibrary.org/obo/CHEBI_14434"},{"id":"A253","pred":"chebi_id","subj":"T252","obj":"http://purl.obolibrary.org/obo/CHEBI_16069"},{"id":"A254","pred":"chebi_id","subj":"T254","obj":"http://purl.obolibrary.org/obo/CHEBI_8102"},{"id":"A255","pred":"chebi_id","subj":"T255","obj":"http://purl.obolibrary.org/obo/CHEBI_28112"},{"id":"A256","pred":"chebi_id","subj":"T256","obj":"http://purl.obolibrary.org/obo/CHEBI_39054"},{"id":"A257","pred":"chebi_id","subj":"T256","obj":"http://purl.obolibrary.org/obo/CHEBI_44557"},{"id":"A258","pred":"chebi_id","subj":"T258","obj":"http://purl.obolibrary.org/obo/CHEBI_35225"},{"id":"A259","pred":"chebi_id","subj":"T259","obj":"http://purl.obolibrary.org/obo/CHEBI_14434"},{"id":"A260","pred":"chebi_id","subj":"T259","obj":"http://purl.obolibrary.org/obo/CHEBI_16069"},{"id":"A261","pred":"chebi_id","subj":"T261","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A262","pred":"chebi_id","subj":"T262","obj":"http://purl.obolibrary.org/obo/CHEBI_24866"},{"id":"A263","pred":"chebi_id","subj":"T262","obj":"http://purl.obolibrary.org/obo/CHEBI_26710"},{"id":"A264","pred":"chebi_id","subj":"T264","obj":"http://purl.obolibrary.org/obo/CHEBI_35225"}],"text":"The MERS-CoV N proteins were prepared according to previously described methods.46 In brief, the cDNA fragments of MERS-CoV N proteins were cloned into a pET-28a expression vector (Merck, Darmstadt, Germany) containing a histidine tag-encoding sequence. Vectors encoding the single mutants N39A, N39G, and W43A were generated using the QuikChange site-directed mutagenesis protocol with the primers listed in Table S3. The vectors were transformed into Escherichia coli BL21 (DE3) pLysS cells. The cells were grown to an optical density range of 0.6–0.8 at 600 nm at 37 °C and protein expression induced with 1.0 mM isopropyl β-d-1-thiogalactopyranoside (IPTG), followed by incubation at 10 °C for 24 h. The cells were harvested by centrifugation (6000g, 12 min, 4 °C) and resuspended in lysis buffer (150 mM NaCl, 50 mM Tris-HCl, 15 mM imidazole, and 1 mM PMSF; pH 7.5). The cells were lysed by sonication and centrifuged (10000g, 40 min, 4 °C) to remove debris. The supernatant was purified by injection into a Ni–NTA column (Merck, Darmstadt, Germany) and eluted with buffer containing imidazole at a gradient range of 15–300 mM. Pure protein fractions were collected, dialyzed with low-salt buffer, concentrated, and quantified by the Bradford method (BioShop Canada Inc., Burlington, ON, Canada)."}

    LitCovid-PD-GO-BP

    {"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T23","span":{"begin":788,"end":793},"obj":"http://purl.obolibrary.org/obo/GO_0019835"}],"text":"The MERS-CoV N proteins were prepared according to previously described methods.46 In brief, the cDNA fragments of MERS-CoV N proteins were cloned into a pET-28a expression vector (Merck, Darmstadt, Germany) containing a histidine tag-encoding sequence. Vectors encoding the single mutants N39A, N39G, and W43A were generated using the QuikChange site-directed mutagenesis protocol with the primers listed in Table S3. The vectors were transformed into Escherichia coli BL21 (DE3) pLysS cells. The cells were grown to an optical density range of 0.6–0.8 at 600 nm at 37 °C and protein expression induced with 1.0 mM isopropyl β-d-1-thiogalactopyranoside (IPTG), followed by incubation at 10 °C for 24 h. The cells were harvested by centrifugation (6000g, 12 min, 4 °C) and resuspended in lysis buffer (150 mM NaCl, 50 mM Tris-HCl, 15 mM imidazole, and 1 mM PMSF; pH 7.5). The cells were lysed by sonication and centrifuged (10000g, 40 min, 4 °C) to remove debris. The supernatant was purified by injection into a Ni–NTA column (Merck, Darmstadt, Germany) and eluted with buffer containing imidazole at a gradient range of 15–300 mM. Pure protein fractions were collected, dialyzed with low-salt buffer, concentrated, and quantified by the Bradford method (BioShop Canada Inc., Burlington, ON, Canada)."}

    LitCovid-sentences

    {"project":"LitCovid-sentences","denotations":[{"id":"T220","span":{"begin":0,"end":253},"obj":"Sentence"},{"id":"T221","span":{"begin":254,"end":418},"obj":"Sentence"},{"id":"T222","span":{"begin":419,"end":493},"obj":"Sentence"},{"id":"T223","span":{"begin":494,"end":703},"obj":"Sentence"},{"id":"T224","span":{"begin":704,"end":871},"obj":"Sentence"},{"id":"T225","span":{"begin":872,"end":963},"obj":"Sentence"},{"id":"T226","span":{"begin":964,"end":1132},"obj":"Sentence"},{"id":"T227","span":{"begin":1133,"end":1301},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The MERS-CoV N proteins were prepared according to previously described methods.46 In brief, the cDNA fragments of MERS-CoV N proteins were cloned into a pET-28a expression vector (Merck, Darmstadt, Germany) containing a histidine tag-encoding sequence. Vectors encoding the single mutants N39A, N39G, and W43A were generated using the QuikChange site-directed mutagenesis protocol with the primers listed in Table S3. The vectors were transformed into Escherichia coli BL21 (DE3) pLysS cells. The cells were grown to an optical density range of 0.6–0.8 at 600 nm at 37 °C and protein expression induced with 1.0 mM isopropyl β-d-1-thiogalactopyranoside (IPTG), followed by incubation at 10 °C for 24 h. The cells were harvested by centrifugation (6000g, 12 min, 4 °C) and resuspended in lysis buffer (150 mM NaCl, 50 mM Tris-HCl, 15 mM imidazole, and 1 mM PMSF; pH 7.5). The cells were lysed by sonication and centrifuged (10000g, 40 min, 4 °C) to remove debris. The supernatant was purified by injection into a Ni–NTA column (Merck, Darmstadt, Germany) and eluted with buffer containing imidazole at a gradient range of 15–300 mM. Pure protein fractions were collected, dialyzed with low-salt buffer, concentrated, and quantified by the Bradford method (BioShop Canada Inc., Burlington, ON, Canada)."}

    LitCovid-PubTator

    {"project":"LitCovid-PubTator","denotations":[{"id":"446","span":{"begin":4,"end":12},"obj":"Species"},{"id":"447","span":{"begin":115,"end":123},"obj":"Species"},{"id":"448","span":{"begin":453,"end":480},"obj":"Species"},{"id":"449","span":{"begin":221,"end":230},"obj":"Chemical"},{"id":"450","span":{"begin":1013,"end":1019},"obj":"Chemical"},{"id":"451","span":{"begin":1089,"end":1098},"obj":"Chemical"},{"id":"452","span":{"begin":1190,"end":1194},"obj":"Chemical"},{"id":"453","span":{"begin":296,"end":300},"obj":"Mutation"}],"attributes":[{"id":"A446","pred":"tao:has_database_id","subj":"446","obj":"Tax:1335626"},{"id":"A447","pred":"tao:has_database_id","subj":"447","obj":"Tax:1335626"},{"id":"A448","pred":"tao:has_database_id","subj":"448","obj":"Tax:469008"},{"id":"A449","pred":"tao:has_database_id","subj":"449","obj":"MESH:D006639"},{"id":"A451","pred":"tao:has_database_id","subj":"451","obj":"MESH:C029899"},{"id":"A452","pred":"tao:has_database_id","subj":"452","obj":"MESH:D012492"},{"id":"A453","pred":"tao:has_standard_notation","subj":"453","obj":"p.N39G"}],"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":"The MERS-CoV N proteins were prepared according to previously described methods.46 In brief, the cDNA fragments of MERS-CoV N proteins were cloned into a pET-28a expression vector (Merck, Darmstadt, Germany) containing a histidine tag-encoding sequence. Vectors encoding the single mutants N39A, N39G, and W43A were generated using the QuikChange site-directed mutagenesis protocol with the primers listed in Table S3. The vectors were transformed into Escherichia coli BL21 (DE3) pLysS cells. The cells were grown to an optical density range of 0.6–0.8 at 600 nm at 37 °C and protein expression induced with 1.0 mM isopropyl β-d-1-thiogalactopyranoside (IPTG), followed by incubation at 10 °C for 24 h. The cells were harvested by centrifugation (6000g, 12 min, 4 °C) and resuspended in lysis buffer (150 mM NaCl, 50 mM Tris-HCl, 15 mM imidazole, and 1 mM PMSF; pH 7.5). The cells were lysed by sonication and centrifuged (10000g, 40 min, 4 °C) to remove debris. The supernatant was purified by injection into a Ni–NTA column (Merck, Darmstadt, Germany) and eluted with buffer containing imidazole at a gradient range of 15–300 mM. Pure protein fractions were collected, dialyzed with low-salt buffer, concentrated, and quantified by the Bradford method (BioShop Canada Inc., Burlington, ON, Canada)."}

    2_test

    {"project":"2_test","denotations":[{"id":"32105468-26249685-61929524","span":{"begin":80,"end":82},"obj":"26249685"}],"text":"The MERS-CoV N proteins were prepared according to previously described methods.46 In brief, the cDNA fragments of MERS-CoV N proteins were cloned into a pET-28a expression vector (Merck, Darmstadt, Germany) containing a histidine tag-encoding sequence. Vectors encoding the single mutants N39A, N39G, and W43A were generated using the QuikChange site-directed mutagenesis protocol with the primers listed in Table S3. The vectors were transformed into Escherichia coli BL21 (DE3) pLysS cells. The cells were grown to an optical density range of 0.6–0.8 at 600 nm at 37 °C and protein expression induced with 1.0 mM isopropyl β-d-1-thiogalactopyranoside (IPTG), followed by incubation at 10 °C for 24 h. The cells were harvested by centrifugation (6000g, 12 min, 4 °C) and resuspended in lysis buffer (150 mM NaCl, 50 mM Tris-HCl, 15 mM imidazole, and 1 mM PMSF; pH 7.5). The cells were lysed by sonication and centrifuged (10000g, 40 min, 4 °C) to remove debris. The supernatant was purified by injection into a Ni–NTA column (Merck, Darmstadt, Germany) and eluted with buffer containing imidazole at a gradient range of 15–300 mM. Pure protein fractions were collected, dialyzed with low-salt buffer, concentrated, and quantified by the Bradford method (BioShop Canada Inc., Burlington, ON, Canada)."}