Pub. Date : 2015
PMID : 25972811
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Pseudo-acetylation of K326 and K328 of actin disrupts Drosophila melanogaster indirect flight muscle structure and performance. | Famotidine | Actin 79B | Drosophila melanogaster |
| 2 | Recently, LC-MS/MS analysis of the cardiac acetyl-lysine proteome revealed K326 and K328 of actin were acetylated, a post-translational modification (PTM) that masks the residues" inherent positive charges. | Famotidine | Actin 79B | Drosophila melanogaster |
| 3 | Based on F-actin-Tm and F-actin-Tm-myosin models and on our physiological data, we conclude that acetylating K326 and K328 of actin alters electrostatic associations with Tm and/or myosin and thereby augments contractile properties. | Famotidine | Actin 79B | Drosophila melanogaster |
| 4 | Based on F-actin-Tm and F-actin-Tm-myosin models and on our physiological data, we conclude that acetylating K326 and K328 of actin alters electrostatic associations with Tm and/or myosin and thereby augments contractile properties. | Famotidine | Actin 79B | Drosophila melanogaster |
| 5 | Based on F-actin-Tm and F-actin-Tm-myosin models and on our physiological data, we conclude that acetylating K326 and K328 of actin alters electrostatic associations with Tm and/or myosin and thereby augments contractile properties. | Famotidine | Actin 79B | Drosophila melanogaster |