PMC:7210460 / 4958-6815 JSON TXT

Annnotations TAB JSON ListView MergeView

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T19","span":{"begin":121,"end":138},"obj":"Body_part"},{"id":"T20","span":{"begin":233,"end":239},"obj":"Body_part"},{"id":"T21","span":{"begin":240,"end":247},"obj":"Body_part"},{"id":"T22","span":{"begin":443,"end":449},"obj":"Body_part"},{"id":"T23","span":{"begin":450,"end":458},"obj":"Body_part"},{"id":"T24","span":{"begin":530,"end":535},"obj":"Body_part"},{"id":"T25","span":{"begin":1141,"end":1145},"obj":"Body_part"},{"id":"T26","span":{"begin":1179,"end":1182},"obj":"Body_part"},{"id":"T27","span":{"begin":1309,"end":1317},"obj":"Body_part"},{"id":"T28","span":{"begin":1465,"end":1468},"obj":"Body_part"},{"id":"T29","span":{"begin":1535,"end":1539},"obj":"Body_part"},{"id":"T30","span":{"begin":1658,"end":1662},"obj":"Body_part"},{"id":"T31","span":{"begin":1811,"end":1828},"obj":"Body_part"}],"attributes":[{"id":"A19","pred":"fma_id","subj":"T19","obj":"http://purl.org/sig/ont/fma/fma63841"},{"id":"A20","pred":"fma_id","subj":"T20","obj":"http://purl.org/sig/ont/fma/fma62970"},{"id":"A21","pred":"fma_id","subj":"T21","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A22","pred":"fma_id","subj":"T22","obj":"http://purl.org/sig/ont/fma/fma62970"},{"id":"A23","pred":"fma_id","subj":"T23","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A24","pred":"fma_id","subj":"T24","obj":"http://purl.org/sig/ont/fma/fma68877"},{"id":"A25","pred":"fma_id","subj":"T25","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A26","pred":"fma_id","subj":"T26","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A27","pred":"fma_id","subj":"T27","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A28","pred":"fma_id","subj":"T28","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A29","pred":"fma_id","subj":"T29","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A30","pred":"fma_id","subj":"T30","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A31","pred":"fma_id","subj":"T31","obj":"http://purl.org/sig/ont/fma/fma63841"}],"text":"The Boc group was removed in compound 14b resulting in inactive form which means the Boc group is necessary to cross the cellular membrane and even more hydrophobic moiety may be advantageous provided that it may result in increased plasma protein binding. Hilgenfeld’s group assessed the pharmacokinetics of 13a and 13b and found that the absorption-distribution-metabolism-excretion of both compounds was similar with a 90% binding to human plasma proteins. The 13b showed less clearance compared to 13a and good tropism to the lungs with a well-tolerated administration through inhalation in mice. Taken together, the authors designed α-ketoamide inhibitors with improved inhibition efficiency against recombinant SARS-CoV-2 Mpro to suppress disease progression (Fig. 1). Their work provides insights into the development of more potent pyridone containing anti-coronaviral drugs. Future structural-functional studies are recommended to improve the efficacy of targeted therapies to tackle the emerging pandemics due to coronaviruses.\nFig. 1 Inhibitors of protease Mpro prevent the replication of SARS-CoV-2. After entering into the host cell, SARS-CoV-2 releases its genomic RNA. The process of translation yields polyproteins pp1a and pp1ab, which are cleaved to the main protease Mpro and nonstructural proteins (nsps). Mpro is involved in the producing of nsps. Nsps is essential for assembling the viral replication transcription complex (RTC) to engage in RNA synthesis. Once inhibitors, such as 11r, 13a, and 13b, act in the cell, they bind to Mpro and inhibit the activity of this enzyme, resulting in failure of virion assembly. Ultimately, host cell fails to release the new intact virions. Colored box highlight the modifications from 11r to 14b. Due to lacking Boc group, 14b could not cross the cellular membrane to inhibit viral replication"}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T17","span":{"begin":717,"end":725},"obj":"Disease"},{"id":"T18","span":{"begin":1100,"end":1108},"obj":"Disease"},{"id":"T19","span":{"begin":1147,"end":1155},"obj":"Disease"}],"attributes":[{"id":"A17","pred":"mondo_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A18","pred":"mondo_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A19","pred":"mondo_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"The Boc group was removed in compound 14b resulting in inactive form which means the Boc group is necessary to cross the cellular membrane and even more hydrophobic moiety may be advantageous provided that it may result in increased plasma protein binding. Hilgenfeld’s group assessed the pharmacokinetics of 13a and 13b and found that the absorption-distribution-metabolism-excretion of both compounds was similar with a 90% binding to human plasma proteins. The 13b showed less clearance compared to 13a and good tropism to the lungs with a well-tolerated administration through inhalation in mice. Taken together, the authors designed α-ketoamide inhibitors with improved inhibition efficiency against recombinant SARS-CoV-2 Mpro to suppress disease progression (Fig. 1). Their work provides insights into the development of more potent pyridone containing anti-coronaviral drugs. Future structural-functional studies are recommended to improve the efficacy of targeted therapies to tackle the emerging pandemics due to coronaviruses.\nFig. 1 Inhibitors of protease Mpro prevent the replication of SARS-CoV-2. After entering into the host cell, SARS-CoV-2 releases its genomic RNA. The process of translation yields polyproteins pp1a and pp1ab, which are cleaved to the main protease Mpro and nonstructural proteins (nsps). Mpro is involved in the producing of nsps. Nsps is essential for assembling the viral replication transcription complex (RTC) to engage in RNA synthesis. Once inhibitors, such as 11r, 13a, and 13b, act in the cell, they bind to Mpro and inhibit the activity of this enzyme, resulting in failure of virion assembly. Ultimately, host cell fails to release the new intact virions. Colored box highlight the modifications from 11r to 14b. Due to lacking Boc group, 14b could not cross the cellular membrane to inhibit viral replication"}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T61","span":{"begin":130,"end":138},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T62","span":{"begin":233,"end":239},"obj":"http://purl.obolibrary.org/obo/UBERON_0001969"},{"id":"T63","span":{"begin":420,"end":421},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T64","span":{"begin":437,"end":442},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T65","span":{"begin":443,"end":449},"obj":"http://purl.obolibrary.org/obo/UBERON_0001969"},{"id":"T66","span":{"begin":530,"end":535},"obj":"http://www.ebi.ac.uk/efo/EFO_0000934"},{"id":"T67","span":{"begin":541,"end":542},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T68","span":{"begin":884,"end":901},"obj":"http://purl.obolibrary.org/obo/UBERON_0006598"},{"id":"T69","span":{"begin":1141,"end":1145},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T70","span":{"begin":1535,"end":1539},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T71","span":{"begin":1575,"end":1583},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T72","span":{"begin":1658,"end":1662},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T73","span":{"begin":1820,"end":1828},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"}],"text":"The Boc group was removed in compound 14b resulting in inactive form which means the Boc group is necessary to cross the cellular membrane and even more hydrophobic moiety may be advantageous provided that it may result in increased plasma protein binding. Hilgenfeld’s group assessed the pharmacokinetics of 13a and 13b and found that the absorption-distribution-metabolism-excretion of both compounds was similar with a 90% binding to human plasma proteins. The 13b showed less clearance compared to 13a and good tropism to the lungs with a well-tolerated administration through inhalation in mice. Taken together, the authors designed α-ketoamide inhibitors with improved inhibition efficiency against recombinant SARS-CoV-2 Mpro to suppress disease progression (Fig. 1). Their work provides insights into the development of more potent pyridone containing anti-coronaviral drugs. Future structural-functional studies are recommended to improve the efficacy of targeted therapies to tackle the emerging pandemics due to coronaviruses.\nFig. 1 Inhibitors of protease Mpro prevent the replication of SARS-CoV-2. After entering into the host cell, SARS-CoV-2 releases its genomic RNA. The process of translation yields polyproteins pp1a and pp1ab, which are cleaved to the main protease Mpro and nonstructural proteins (nsps). Mpro is involved in the producing of nsps. Nsps is essential for assembling the viral replication transcription complex (RTC) to engage in RNA synthesis. Once inhibitors, such as 11r, 13a, and 13b, act in the cell, they bind to Mpro and inhibit the activity of this enzyme, resulting in failure of virion assembly. Ultimately, host cell fails to release the new intact virions. Colored box highlight the modifications from 11r to 14b. Due to lacking Boc group, 14b could not cross the cellular membrane to inhibit viral replication"}

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T3","span":{"begin":364,"end":374},"obj":"http://purl.obolibrary.org/obo/GO_0008152"},{"id":"T4","span":{"begin":375,"end":384},"obj":"http://purl.obolibrary.org/obo/GO_0007588"},{"id":"T5","span":{"begin":515,"end":522},"obj":"http://purl.obolibrary.org/obo/GO_0009606"},{"id":"T6","span":{"begin":1199,"end":1210},"obj":"http://purl.obolibrary.org/obo/GO_0006412"},{"id":"T7","span":{"begin":1406,"end":1423},"obj":"http://purl.obolibrary.org/obo/GO_0019079"},{"id":"T8","span":{"begin":1406,"end":1423},"obj":"http://purl.obolibrary.org/obo/GO_0019058"},{"id":"T9","span":{"begin":1424,"end":1437},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T10","span":{"begin":1465,"end":1478},"obj":"http://purl.obolibrary.org/obo/GO_0032774"},{"id":"T11","span":{"begin":1469,"end":1478},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T12","span":{"begin":1624,"end":1639},"obj":"http://purl.obolibrary.org/obo/GO_0019068"},{"id":"T13","span":{"begin":1832,"end":1857},"obj":"http://purl.obolibrary.org/obo/GO_1903901"},{"id":"T14","span":{"begin":1840,"end":1857},"obj":"http://purl.obolibrary.org/obo/GO_0019079"},{"id":"T15","span":{"begin":1840,"end":1857},"obj":"http://purl.obolibrary.org/obo/GO_0019058"}],"text":"The Boc group was removed in compound 14b resulting in inactive form which means the Boc group is necessary to cross the cellular membrane and even more hydrophobic moiety may be advantageous provided that it may result in increased plasma protein binding. Hilgenfeld’s group assessed the pharmacokinetics of 13a and 13b and found that the absorption-distribution-metabolism-excretion of both compounds was similar with a 90% binding to human plasma proteins. The 13b showed less clearance compared to 13a and good tropism to the lungs with a well-tolerated administration through inhalation in mice. Taken together, the authors designed α-ketoamide inhibitors with improved inhibition efficiency against recombinant SARS-CoV-2 Mpro to suppress disease progression (Fig. 1). Their work provides insights into the development of more potent pyridone containing anti-coronaviral drugs. Future structural-functional studies are recommended to improve the efficacy of targeted therapies to tackle the emerging pandemics due to coronaviruses.\nFig. 1 Inhibitors of protease Mpro prevent the replication of SARS-CoV-2. After entering into the host cell, SARS-CoV-2 releases its genomic RNA. The process of translation yields polyproteins pp1a and pp1ab, which are cleaved to the main protease Mpro and nonstructural proteins (nsps). Mpro is involved in the producing of nsps. Nsps is essential for assembling the viral replication transcription complex (RTC) to engage in RNA synthesis. Once inhibitors, such as 11r, 13a, and 13b, act in the cell, they bind to Mpro and inhibit the activity of this enzyme, resulting in failure of virion assembly. Ultimately, host cell fails to release the new intact virions. Colored box highlight the modifications from 11r to 14b. Due to lacking Boc group, 14b could not cross the cellular membrane to inhibit viral replication"}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T29","span":{"begin":0,"end":256},"obj":"Sentence"},{"id":"T30","span":{"begin":257,"end":459},"obj":"Sentence"},{"id":"T31","span":{"begin":460,"end":600},"obj":"Sentence"},{"id":"T32","span":{"begin":601,"end":774},"obj":"Sentence"},{"id":"T33","span":{"begin":775,"end":883},"obj":"Sentence"},{"id":"T34","span":{"begin":884,"end":1037},"obj":"Sentence"},{"id":"T35","span":{"begin":1038,"end":1111},"obj":"Sentence"},{"id":"T36","span":{"begin":1112,"end":1183},"obj":"Sentence"},{"id":"T37","span":{"begin":1184,"end":1325},"obj":"Sentence"},{"id":"T38","span":{"begin":1326,"end":1368},"obj":"Sentence"},{"id":"T39","span":{"begin":1369,"end":1479},"obj":"Sentence"},{"id":"T40","span":{"begin":1480,"end":1640},"obj":"Sentence"},{"id":"T41","span":{"begin":1641,"end":1703},"obj":"Sentence"},{"id":"T42","span":{"begin":1704,"end":1760},"obj":"Sentence"},{"id":"T43","span":{"begin":1761,"end":1857},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The Boc group was removed in compound 14b resulting in inactive form which means the Boc group is necessary to cross the cellular membrane and even more hydrophobic moiety may be advantageous provided that it may result in increased plasma protein binding. Hilgenfeld’s group assessed the pharmacokinetics of 13a and 13b and found that the absorption-distribution-metabolism-excretion of both compounds was similar with a 90% binding to human plasma proteins. The 13b showed less clearance compared to 13a and good tropism to the lungs with a well-tolerated administration through inhalation in mice. Taken together, the authors designed α-ketoamide inhibitors with improved inhibition efficiency against recombinant SARS-CoV-2 Mpro to suppress disease progression (Fig. 1). Their work provides insights into the development of more potent pyridone containing anti-coronaviral drugs. Future structural-functional studies are recommended to improve the efficacy of targeted therapies to tackle the emerging pandemics due to coronaviruses.\nFig. 1 Inhibitors of protease Mpro prevent the replication of SARS-CoV-2. After entering into the host cell, SARS-CoV-2 releases its genomic RNA. The process of translation yields polyproteins pp1a and pp1ab, which are cleaved to the main protease Mpro and nonstructural proteins (nsps). Mpro is involved in the producing of nsps. Nsps is essential for assembling the viral replication transcription complex (RTC) to engage in RNA synthesis. Once inhibitors, such as 11r, 13a, and 13b, act in the cell, they bind to Mpro and inhibit the activity of this enzyme, resulting in failure of virion assembly. Ultimately, host cell fails to release the new intact virions. Colored box highlight the modifications from 11r to 14b. Due to lacking Boc group, 14b could not cross the cellular membrane to inhibit viral replication"}

LitCovid-PubTator