PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15486204-0	2004	Differential recognition by the tumor suppressor protein p53 of DNA modified by the novel antitumor trinuclear platinum drug BBR3464 and cisplatin.	BBR 3464	125-132	tumor protein p53	Homo sapiens	57-60	
11313183-10	2001	Our data indicate that BBR3464 may be a promising agent in the treatment of tumours unresponsive to cisplatin and with a non-functional p53.	BBR 3464	23-30	tumor protein p53	Homo sapiens	136-139	
15486204-2	2004	BBR3464 retains significant activity in human tumor cell lines and xenografts that are refractory or poorly responsive to cisplatin, and displays a high activity in human tumor cell lines that are characterized by both wild-type and mutant p53 gene.	BBR 3464	0-7	tumor protein p53	Homo sapiens	240-243	
15486204-6	2004	This study, using gel-mobility-shift assays, was undertaken to examine the interactions of active and latent p53 protein with DNA fragments and oligodeoxyribonucleotide duplexes modified by BBR3464 in a cell free medium and to compare these results with those describing the interactions of these proteins with DNA modified by cisplatin.	BBR 3464	190-197	tumor protein p53	Homo sapiens	109-112	
15486204-7	2004	The results indicate that structurally different DNA adducts of BBR3464 and cisplatin exhibit a different efficiency to affect the binding affinity of the modified DNA to p53 protein.	BBR 3464	64-71	tumor protein p53	Homo sapiens	171-174	
15486204-8	2004	It has been suggested that different structural perturbations induced in DNA by the adducts of BBR3464 and cisplatin produce a differential response to p53 protein activation and recognition and that a "molecular approach" to control of downstream effects such as protein recognition and pathways of apoptosis induction may consist in design of structurally unique DNA adducts as cell signals.	BBR 3464	95-102	tumor protein p53	Homo sapiens	152-155