Pub. Date : 2008 May 1
PMID : 18241198
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | A critical role in structure-specific DNA binding for the acetylatable lysine residues in HMGB1. | Lysine | high mobility group box 1 | Homo sapiens |
| 2 | The structure-specific DNA-binding protein HMGB1 (high-mobility group protein B1) which comprises two tandem HMG boxes (A and B) and an acidic C-terminal tail, is acetylated in vivo at Lys(2) and Lys(11) in the A box. | Lysine | high mobility group box 1 | Homo sapiens |
| 3 | The structure-specific DNA-binding protein HMGB1 (high-mobility group protein B1) which comprises two tandem HMG boxes (A and B) and an acidic C-terminal tail, is acetylated in vivo at Lys(2) and Lys(11) in the A box. | Lysine | high mobility group box 1 | Homo sapiens |
| 4 | The structure-specific DNA-binding protein HMGB1 (high-mobility group protein B1) which comprises two tandem HMG boxes (A and B) and an acidic C-terminal tail, is acetylated in vivo at Lys(2) and Lys(11) in the A box. | Lysine | high mobility group box 1 | Homo sapiens |
| 5 | The structure-specific DNA-binding protein HMGB1 (high-mobility group protein B1) which comprises two tandem HMG boxes (A and B) and an acidic C-terminal tail, is acetylated in vivo at Lys(2) and Lys(11) in the A box. | Lysine | high mobility group box 1 | Homo sapiens |
| 6 | We conclude that Lys(2) and Lys(11) are critical for binding of the isolated A domain and HMGB1 to distorted DNA substrates. | Lysine | high mobility group box 1 | Homo sapiens |
| 7 | We conclude that Lys(2) and Lys(11) are critical for binding of the isolated A domain and HMGB1 to distorted DNA substrates. | Lysine | high mobility group box 1 | Homo sapiens |