Pub. Date : 2003 Mar 11
PMID : 12614161
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Nature of full-length HMGB1 binding to cisplatin-modified DNA. | Cisplatin | high mobility group box 1 | Homo sapiens |
| 2 | HMGB1, a highly conserved non-histone DNA-binding protein, interacts with specific DNA structural motifs such as those encountered at cisplatin damage, four-way junctions, and supercoils. | Cisplatin | high mobility group box 1 | Homo sapiens |
| 3 | The interaction of full-length HMGB1, containing two tandem HMG box domains and a C-terminal acidic tail, with cisplatin-modified DNA was investigated by hydroxyl radical footprinting and electrophoretic gel mobility shift assays. | Cisplatin | high mobility group box 1 | Homo sapiens |
| 4 | Site-directed mutagenesis of intercalating residues in both HMG domains A and B in full-length HMGB1 further supports the conclusion that only one HMG box domain is bound to the site of cisplatin damage. | Cisplatin | high mobility group box 1 | Homo sapiens |
| 5 | These results illuminate the respective roles of the tandem HMG boxes and the C-terminal acidic tail of HMGB1 in binding to DNA and to the major DNA adducts formed by the anticancer drug cisplatin. | Cisplatin | high mobility group box 1 | Homo sapiens |