Pub. Date : 2010 Aug
PMID : 20464001
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Identification by nuclear magnetic resonance spectroscopy of an active-site hydrogen-bond network in human monoacylglycerol lipase (hMGL): implications for hMGL dynamics, pharmacological inhibition, and catalytic mechanism. | Hydrogen | monoglyceride lipase | Homo sapiens |
| 2 | Identification by nuclear magnetic resonance spectroscopy of an active-site hydrogen-bond network in human monoacylglycerol lipase (hMGL): implications for hMGL dynamics, pharmacological inhibition, and catalytic mechanism. | Hydrogen | monoglyceride lipase | Homo sapiens |
| 3 | Identification by nuclear magnetic resonance spectroscopy of an active-site hydrogen-bond network in human monoacylglycerol lipase (hMGL): implications for hMGL dynamics, pharmacological inhibition, and catalytic mechanism. | Hydrogen | monoglyceride lipase | Homo sapiens |
| 4 | hMGL inhibition by AM6701 alters this hydrogen-bonding pattern through subtle active-site structural rearrangements without influencing hydrogen-bond occupancies. | Hydrogen | monoglyceride lipase | Homo sapiens |
| 5 | In contrast, hMGL titration with NAM, which leads to cysteine alkylation, stoichiometrically decreases the population of the active-site hydrogen bonds. | Hydrogen | monoglyceride lipase | Homo sapiens |
| 6 | These data provide detailed molecular insight into the distinctive mechanisms of two covalent hMGL inhibitors and implicate a hydrogen-bond network as a structural feature of hMGL catalytic function. | Hydrogen | monoglyceride lipase | Homo sapiens |
| 7 | These data provide detailed molecular insight into the distinctive mechanisms of two covalent hMGL inhibitors and implicate a hydrogen-bond network as a structural feature of hMGL catalytic function. | Hydrogen | monoglyceride lipase | Homo sapiens |