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Sakshi Tomar - One of the best experts on this subject based on the ideXlab platform.
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discovery synthesis and structure based optimization of a series of n tert butyl 2 n arylamido 2 pyridin 3 yl acetamides ml188 as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus sars cov 3cl protease
Journal of Medicinal Chemistry, 2013Co-Authors: Jon Jacobs, Valerie Grumtokars, Ya Zhou, Mark Turlington, Adrian S Saldanha, Peter Chase, Aimee Eggler, Eric S Dawson, Yahira M Baezsantos, Sakshi TomarAbstract:A high-throughput screen of the NIH molecular libraries sample collection and subsequent optimization of a lead dipeptide-like series of severe acute respiratory syndrome (SARS) main protease (3CLpro) inhibitors led to the identification of probe compound ML188 (16-(R), (R)-N-(4-(tert-butyl)phenyl)-N-(2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl)furan-2-carboxamide, Pubchem CID: 46897844). Unlike the majority of reported coronavirus 3CLpro inhibitors that act via covalent modification of the enzyme, 16-(R) is a noncovalent SARS-CoV 3CLpro inhibitor with moderate MW and good enzyme and antiviral inhibitory activity. A multicomponent Ugi reaction was utilized to rapidly explore structure–activity relationships within S1′, S1, and S2 enzyme binding pockets. The X-ray structure of SARS-CoV 3CLpro bound with 16-(R) was instrumental in guiding subsequent rounds of chemistry optimization. 16-(R) provides an excellent starting point for the further design and refinement of 3CLpro inhibitors that act by a nonco...
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discovery synthesis and structure based optimization of a series of n tert butyl 2 n arylamido 2 pyridin 3 yl acetamides ml188 as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus sars cov 3cl protease
Journal of Medicinal Chemistry, 2013Co-Authors: Jon Jacobs, Valerie Grumtokars, Ya Zhou, Mark Turlington, Adrian S Saldanha, Peter Chase, Aimee Eggler, Eric S Dawson, Yahira M Baezsantos, Sakshi TomarAbstract:A high-throughput screen of the NIH molecular libraries sample collection and subsequent optimization of a lead dipeptide-like series of severe acute respiratory syndrome (SARS) main protease (3CLpro) inhibitors led to the identification of probe compound ML188 (16-(R), (R)-N-(4-(tert-butyl)phenyl)-N-(2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl)furan-2-carboxamide, Pubchem CID: 46897844). Unlike the majority of reported coronavirus 3CLpro inhibitors that act via covalent modification of the enzyme, 16-(R) is a noncovalent SARS-CoV 3CLpro inhibitor with moderate MW and good enzyme and antiviral inhibitory activity. A multicomponent Ugi reaction was utilized to rapidly explore structure-activity relationships within S(1'), S(1), and S(2) enzyme binding pockets. The X-ray structure of SARS-CoV 3CLpro bound with 16-(R) was instrumental in guiding subsequent rounds of chemistry optimization. 16-(R) provides an excellent starting point for the further design and refinement of 3CLpro inhibitors that act by a noncovalent mechanism of action.
Jon Jacobs - One of the best experts on this subject based on the ideXlab platform.
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discovery synthesis and structure based optimization of a series of n tert butyl 2 n arylamido 2 pyridin 3 yl acetamides ml188 as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus sars cov 3cl protease
Journal of Medicinal Chemistry, 2013Co-Authors: Jon Jacobs, Valerie Grumtokars, Ya Zhou, Mark Turlington, Adrian S Saldanha, Peter Chase, Aimee Eggler, Eric S Dawson, Yahira M Baezsantos, Sakshi TomarAbstract:A high-throughput screen of the NIH molecular libraries sample collection and subsequent optimization of a lead dipeptide-like series of severe acute respiratory syndrome (SARS) main protease (3CLpro) inhibitors led to the identification of probe compound ML188 (16-(R), (R)-N-(4-(tert-butyl)phenyl)-N-(2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl)furan-2-carboxamide, Pubchem CID: 46897844). Unlike the majority of reported coronavirus 3CLpro inhibitors that act via covalent modification of the enzyme, 16-(R) is a noncovalent SARS-CoV 3CLpro inhibitor with moderate MW and good enzyme and antiviral inhibitory activity. A multicomponent Ugi reaction was utilized to rapidly explore structure–activity relationships within S1′, S1, and S2 enzyme binding pockets. The X-ray structure of SARS-CoV 3CLpro bound with 16-(R) was instrumental in guiding subsequent rounds of chemistry optimization. 16-(R) provides an excellent starting point for the further design and refinement of 3CLpro inhibitors that act by a nonco...
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discovery synthesis and structure based optimization of a series of n tert butyl 2 n arylamido 2 pyridin 3 yl acetamides ml188 as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus sars cov 3cl protease
Journal of Medicinal Chemistry, 2013Co-Authors: Jon Jacobs, Valerie Grumtokars, Ya Zhou, Mark Turlington, Adrian S Saldanha, Peter Chase, Aimee Eggler, Eric S Dawson, Yahira M Baezsantos, Sakshi TomarAbstract:A high-throughput screen of the NIH molecular libraries sample collection and subsequent optimization of a lead dipeptide-like series of severe acute respiratory syndrome (SARS) main protease (3CLpro) inhibitors led to the identification of probe compound ML188 (16-(R), (R)-N-(4-(tert-butyl)phenyl)-N-(2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl)furan-2-carboxamide, Pubchem CID: 46897844). Unlike the majority of reported coronavirus 3CLpro inhibitors that act via covalent modification of the enzyme, 16-(R) is a noncovalent SARS-CoV 3CLpro inhibitor with moderate MW and good enzyme and antiviral inhibitory activity. A multicomponent Ugi reaction was utilized to rapidly explore structure-activity relationships within S(1'), S(1), and S(2) enzyme binding pockets. The X-ray structure of SARS-CoV 3CLpro bound with 16-(R) was instrumental in guiding subsequent rounds of chemistry optimization. 16-(R) provides an excellent starting point for the further design and refinement of 3CLpro inhibitors that act by a noncovalent mechanism of action.
Valerie Grumtokars - One of the best experts on this subject based on the ideXlab platform.
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discovery synthesis and structure based optimization of a series of n tert butyl 2 n arylamido 2 pyridin 3 yl acetamides ml188 as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus sars cov 3cl protease
Journal of Medicinal Chemistry, 2013Co-Authors: Jon Jacobs, Valerie Grumtokars, Ya Zhou, Mark Turlington, Adrian S Saldanha, Peter Chase, Aimee Eggler, Eric S Dawson, Yahira M Baezsantos, Sakshi TomarAbstract:A high-throughput screen of the NIH molecular libraries sample collection and subsequent optimization of a lead dipeptide-like series of severe acute respiratory syndrome (SARS) main protease (3CLpro) inhibitors led to the identification of probe compound ML188 (16-(R), (R)-N-(4-(tert-butyl)phenyl)-N-(2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl)furan-2-carboxamide, Pubchem CID: 46897844). Unlike the majority of reported coronavirus 3CLpro inhibitors that act via covalent modification of the enzyme, 16-(R) is a noncovalent SARS-CoV 3CLpro inhibitor with moderate MW and good enzyme and antiviral inhibitory activity. A multicomponent Ugi reaction was utilized to rapidly explore structure–activity relationships within S1′, S1, and S2 enzyme binding pockets. The X-ray structure of SARS-CoV 3CLpro bound with 16-(R) was instrumental in guiding subsequent rounds of chemistry optimization. 16-(R) provides an excellent starting point for the further design and refinement of 3CLpro inhibitors that act by a nonco...
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discovery synthesis and structure based optimization of a series of n tert butyl 2 n arylamido 2 pyridin 3 yl acetamides ml188 as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus sars cov 3cl protease
Journal of Medicinal Chemistry, 2013Co-Authors: Jon Jacobs, Valerie Grumtokars, Ya Zhou, Mark Turlington, Adrian S Saldanha, Peter Chase, Aimee Eggler, Eric S Dawson, Yahira M Baezsantos, Sakshi TomarAbstract:A high-throughput screen of the NIH molecular libraries sample collection and subsequent optimization of a lead dipeptide-like series of severe acute respiratory syndrome (SARS) main protease (3CLpro) inhibitors led to the identification of probe compound ML188 (16-(R), (R)-N-(4-(tert-butyl)phenyl)-N-(2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl)furan-2-carboxamide, Pubchem CID: 46897844). Unlike the majority of reported coronavirus 3CLpro inhibitors that act via covalent modification of the enzyme, 16-(R) is a noncovalent SARS-CoV 3CLpro inhibitor with moderate MW and good enzyme and antiviral inhibitory activity. A multicomponent Ugi reaction was utilized to rapidly explore structure-activity relationships within S(1'), S(1), and S(2) enzyme binding pockets. The X-ray structure of SARS-CoV 3CLpro bound with 16-(R) was instrumental in guiding subsequent rounds of chemistry optimization. 16-(R) provides an excellent starting point for the further design and refinement of 3CLpro inhibitors that act by a noncovalent mechanism of action.
Ya Zhou - One of the best experts on this subject based on the ideXlab platform.
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discovery synthesis and structure based optimization of a series of n tert butyl 2 n arylamido 2 pyridin 3 yl acetamides ml188 as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus sars cov 3cl protease
Journal of Medicinal Chemistry, 2013Co-Authors: Jon Jacobs, Valerie Grumtokars, Ya Zhou, Mark Turlington, Adrian S Saldanha, Peter Chase, Aimee Eggler, Eric S Dawson, Yahira M Baezsantos, Sakshi TomarAbstract:A high-throughput screen of the NIH molecular libraries sample collection and subsequent optimization of a lead dipeptide-like series of severe acute respiratory syndrome (SARS) main protease (3CLpro) inhibitors led to the identification of probe compound ML188 (16-(R), (R)-N-(4-(tert-butyl)phenyl)-N-(2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl)furan-2-carboxamide, Pubchem CID: 46897844). Unlike the majority of reported coronavirus 3CLpro inhibitors that act via covalent modification of the enzyme, 16-(R) is a noncovalent SARS-CoV 3CLpro inhibitor with moderate MW and good enzyme and antiviral inhibitory activity. A multicomponent Ugi reaction was utilized to rapidly explore structure–activity relationships within S1′, S1, and S2 enzyme binding pockets. The X-ray structure of SARS-CoV 3CLpro bound with 16-(R) was instrumental in guiding subsequent rounds of chemistry optimization. 16-(R) provides an excellent starting point for the further design and refinement of 3CLpro inhibitors that act by a nonco...
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discovery synthesis and structure based optimization of a series of n tert butyl 2 n arylamido 2 pyridin 3 yl acetamides ml188 as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus sars cov 3cl protease
Journal of Medicinal Chemistry, 2013Co-Authors: Jon Jacobs, Valerie Grumtokars, Ya Zhou, Mark Turlington, Adrian S Saldanha, Peter Chase, Aimee Eggler, Eric S Dawson, Yahira M Baezsantos, Sakshi TomarAbstract:A high-throughput screen of the NIH molecular libraries sample collection and subsequent optimization of a lead dipeptide-like series of severe acute respiratory syndrome (SARS) main protease (3CLpro) inhibitors led to the identification of probe compound ML188 (16-(R), (R)-N-(4-(tert-butyl)phenyl)-N-(2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl)furan-2-carboxamide, Pubchem CID: 46897844). Unlike the majority of reported coronavirus 3CLpro inhibitors that act via covalent modification of the enzyme, 16-(R) is a noncovalent SARS-CoV 3CLpro inhibitor with moderate MW and good enzyme and antiviral inhibitory activity. A multicomponent Ugi reaction was utilized to rapidly explore structure-activity relationships within S(1'), S(1), and S(2) enzyme binding pockets. The X-ray structure of SARS-CoV 3CLpro bound with 16-(R) was instrumental in guiding subsequent rounds of chemistry optimization. 16-(R) provides an excellent starting point for the further design and refinement of 3CLpro inhibitors that act by a noncovalent mechanism of action.
Yahira M Baezsantos - One of the best experts on this subject based on the ideXlab platform.
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discovery synthesis and structure based optimization of a series of n tert butyl 2 n arylamido 2 pyridin 3 yl acetamides ml188 as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus sars cov 3cl protease
Journal of Medicinal Chemistry, 2013Co-Authors: Jon Jacobs, Valerie Grumtokars, Ya Zhou, Mark Turlington, Adrian S Saldanha, Peter Chase, Aimee Eggler, Eric S Dawson, Yahira M Baezsantos, Sakshi TomarAbstract:A high-throughput screen of the NIH molecular libraries sample collection and subsequent optimization of a lead dipeptide-like series of severe acute respiratory syndrome (SARS) main protease (3CLpro) inhibitors led to the identification of probe compound ML188 (16-(R), (R)-N-(4-(tert-butyl)phenyl)-N-(2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl)furan-2-carboxamide, Pubchem CID: 46897844). Unlike the majority of reported coronavirus 3CLpro inhibitors that act via covalent modification of the enzyme, 16-(R) is a noncovalent SARS-CoV 3CLpro inhibitor with moderate MW and good enzyme and antiviral inhibitory activity. A multicomponent Ugi reaction was utilized to rapidly explore structure–activity relationships within S1′, S1, and S2 enzyme binding pockets. The X-ray structure of SARS-CoV 3CLpro bound with 16-(R) was instrumental in guiding subsequent rounds of chemistry optimization. 16-(R) provides an excellent starting point for the further design and refinement of 3CLpro inhibitors that act by a nonco...
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discovery synthesis and structure based optimization of a series of n tert butyl 2 n arylamido 2 pyridin 3 yl acetamides ml188 as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus sars cov 3cl protease
Journal of Medicinal Chemistry, 2013Co-Authors: Jon Jacobs, Valerie Grumtokars, Ya Zhou, Mark Turlington, Adrian S Saldanha, Peter Chase, Aimee Eggler, Eric S Dawson, Yahira M Baezsantos, Sakshi TomarAbstract:A high-throughput screen of the NIH molecular libraries sample collection and subsequent optimization of a lead dipeptide-like series of severe acute respiratory syndrome (SARS) main protease (3CLpro) inhibitors led to the identification of probe compound ML188 (16-(R), (R)-N-(4-(tert-butyl)phenyl)-N-(2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl)ethyl)furan-2-carboxamide, Pubchem CID: 46897844). Unlike the majority of reported coronavirus 3CLpro inhibitors that act via covalent modification of the enzyme, 16-(R) is a noncovalent SARS-CoV 3CLpro inhibitor with moderate MW and good enzyme and antiviral inhibitory activity. A multicomponent Ugi reaction was utilized to rapidly explore structure-activity relationships within S(1'), S(1), and S(2) enzyme binding pockets. The X-ray structure of SARS-CoV 3CLpro bound with 16-(R) was instrumental in guiding subsequent rounds of chemistry optimization. 16-(R) provides an excellent starting point for the further design and refinement of 3CLpro inhibitors that act by a noncovalent mechanism of action.
