Pub. Date : 2014 Dec
PMID : 25411887
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Here, we describe crystallographic analyses of the mechanism of inhibition of the clinically relevant VIM-2 MBL by a rhodanine, which reveal that the rhodanine ring undergoes hydrolysis to give a thioenolate. | Rhodanine | mannose-binding lectin family member 3, pseudogene | Homo sapiens |
| 2 | Here, we describe crystallographic analyses of the mechanism of inhibition of the clinically relevant VIM-2 MBL by a rhodanine, which reveal that the rhodanine ring undergoes hydrolysis to give a thioenolate. | Rhodanine | mannose-binding lectin family member 3, pseudogene | Homo sapiens |
| 3 | Crystallization of VIM-2 in the presence of the intact rhodanine led to observation of a ternary complex of MBL, a thioenolate fragment and rhodanine. | Rhodanine | mannose-binding lectin family member 3, pseudogene | Homo sapiens |
| 4 | Crystallization of VIM-2 in the presence of the intact rhodanine led to observation of a ternary complex of MBL, a thioenolate fragment and rhodanine. | Rhodanine | mannose-binding lectin family member 3, pseudogene | Homo sapiens |
| 5 | The crystallographic observations are supported by kinetic and biophysical studies, including (19)F NMR analyses, which reveal the rhodanine-derived thioenolate to be a potent broad-spectrum MBL inhibitor and a lead structure for the development of new types of clinically useful MBL inhibitors. | Rhodanine | mannose-binding lectin family member 3, pseudogene | Homo sapiens |
| 6 | The crystallographic observations are supported by kinetic and biophysical studies, including (19)F NMR analyses, which reveal the rhodanine-derived thioenolate to be a potent broad-spectrum MBL inhibitor and a lead structure for the development of new types of clinically useful MBL inhibitors. | Rhodanine | mannose-binding lectin family member 3, pseudogene | Homo sapiens |