| Title : Development of highly potent inhibitors of the Ras-targeting human acyl protein thioesterases based on substrate similarity design - Hedberg_2011_Angew.Chem.Int.Ed.Engl_50_9832 |
| Author(s) : Hedberg C , Dekker FJ , Rusch M , Renner S , Wetzel S , Vartak N , Gerding-Reimers C , Bon RS , Bastiaens PI , Waldmann H |
| Ref : Angew Chem Int Ed Engl , 50 :9832 , 2011 |
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Abstract :
A matter of common sense: a common recognition motif consisting of a negatively charged group five to six bonds away (red) from the (thio)ester functionality (green) and a positively charged tail group ten to twelve bonds away (blue) was identified in two native acyl protein thioesterase 1 (APT1) substrates. This similarity led to the design of potent inhibitors of the Ras-depalmitoylating enzyme APT1. |
| PubMedSearch : Hedberg_2011_Angew.Chem.Int.Ed.Engl_50_9832 |
| PubMedID: 21905185 |
| Inhibitor | Palmostatin-M |
Hedberg C, Dekker FJ, Rusch M, Renner S, Wetzel S, Vartak N, Gerding-Reimers C, Bon RS, Bastiaens PI, Waldmann H (2011)
Development of highly potent inhibitors of the Ras-targeting human acyl protein thioesterases based on substrate similarity design
Angew Chem Int Ed Engl
50 :9832
Hedberg C, Dekker FJ, Rusch M, Renner S, Wetzel S, Vartak N, Gerding-Reimers C, Bon RS, Bastiaens PI, Waldmann H (2011)
Angew Chem Int Ed Engl
50 :9832