PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
16473140-3	2006	Using display PCR, we found that acquisition of resistance to the multinuclear platinum complex BBR3464 was associated with modulation of several transcripts, including up-regulation of the major substrate of protein kinase C (PKC), the myristoylated alanine-rich C kinase substrate (MARCKS).	BBR 3464	96-103	protein kinase C alpha	Homo sapiens	227-230
16473140-3	2006	Using display PCR, we found that acquisition of resistance to the multinuclear platinum complex BBR3464 was associated with modulation of several transcripts, including up-regulation of the major substrate of protein kinase C (PKC), the myristoylated alanine-rich C kinase substrate (MARCKS).	BBR 3464	96-103	myristoylated alanine rich protein kinase C substrate	Homo sapiens	237-282
16473140-3	2006	Using display PCR, we found that acquisition of resistance to the multinuclear platinum complex BBR3464 was associated with modulation of several transcripts, including up-regulation of the major substrate of protein kinase C (PKC), the myristoylated alanine-rich C kinase substrate (MARCKS).	BBR 3464	96-103	myristoylated alanine rich protein kinase C substrate	Homo sapiens	284-290
16473140-7	2006	A number of approaches designed to modulate the function or expression of PKCalpha support that the isoenzyme may play a role in determining resistance only to cisplatin but not to BBR3464, which is known to activate a different pathway of cell response.	BBR 3464	181-188	protein kinase C alpha	Homo sapiens	74-82
15992354-9	2005	BBR3464 has shown in vivo activity at its MTD in several pre-clinical and clinical trials; however, recent phase II trials have shown that BBR3464, and other multi-nuclear platinum drugs, did not yield results substantially different from cisplatin, possibly due to their binding and degradation by human plasma proteins.	BBR 3464	0-7	metallothionein 1E	Homo sapiens	42-45
12740909-8	2003	Cisplatin induced an appreciable increase of p21(WAF1) levels in both models, in contrast to BBR3464 that produced a substantial upregulation of p21(WAF1) only in parental cells.	BBR 3464	93-100	cyclin dependent kinase inhibitor 1A	Homo sapiens	145-148
12740909-8	2003	Cisplatin induced an appreciable increase of p21(WAF1) levels in both models, in contrast to BBR3464 that produced a substantial upregulation of p21(WAF1) only in parental cells.	BBR 3464	93-100	cyclin dependent kinase inhibitor 1A	Homo sapiens	149-153
11313183-7	2001	In astrocytoma cells, cisplatin treatment resulted in the upregulation of p53, p21 and bax, while only p21 induction was observed after BBR3464 treatment.	BBR 3464	136-143	H3 histone pseudogene 16	Homo sapiens	103-106
11313183-8	2001	In cisplatin-resistant cells, the reduced sensitivity to cisplatin paralleled a resistance to the induction of p53/p21 pathway by cisplatin, while the same doses of BBR3464 induced p21 to a similar extent in the resistant cells as in the parental cells.	BBR 3464	165-172	H3 histone pseudogene 16	Homo sapiens	181-184
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
15486204-0	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
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