PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
21508668-7	2011	Biochemical studies showed that zinc partly induced the transition of mutant p53 protein (reactive to conformation-sensitive PAb240 antibody for mutant conformation) into a functional conformation (reactive to conformation-sensitive PAb1620 antibody for wild-type conformation).	pab1620	233-240	tumor protein p53	Homo sapiens	77-80
12881704-4	2003	Treatment with ellipticine alters mutant p53 reactivity to conformation-sensitive Pab1620 and Pab240 antibodies and increases its sequence-specific DNA-binding activity in vivo.	pab1620	82-89	transformation related protein 53, pseudogene	Mus musculus	41-44
10488156-5	1999	For this purpose, we applied a recently developed random mutagenesis technique called DNA shuffling and screened for p53 variants that could retain reactivity to the native conformation-specific anti-p53 antibody PAb1620 upon thermal treatment.	pab1620	213-220	tumor protein p53	Homo sapiens	117-120
10488156-5	1999	For this purpose, we applied a recently developed random mutagenesis technique called DNA shuffling and screened for p53 variants that could retain reactivity to the native conformation-specific anti-p53 antibody PAb1620 upon thermal treatment.	pab1620	213-220	tumor protein p53	Homo sapiens	200-203
18483253-5	2008	We present evidence that zinc supplementation to HIPK2i cells increased p53 reactivity to conformation-sensitive PAb1620 (wild-type conformation) antibody and restored p53 sequence-specific DNA binding in vivo and transcription of target genes in response to Adriamycin treatment.	pab1620	113-120	homeodomain interacting protein kinase 2	Homo sapiens	49-54
18483253-5	2008	We present evidence that zinc supplementation to HIPK2i cells increased p53 reactivity to conformation-sensitive PAb1620 (wild-type conformation) antibody and restored p53 sequence-specific DNA binding in vivo and transcription of target genes in response to Adriamycin treatment.	pab1620	113-120	tumor protein p53	Homo sapiens	72-75
10496344-6	1999	Moreover, studies in vitro and in vivo indicate that p53 mutants with intact conformational structure (as determined by immunoreactivity with PAb246 and PAb1620) retain the ability to undergo proteolytic cleavage similar, if not identical, to the wild-type p53 protein.	pab1620	153-160	tumor protein p53	Homo sapiens	53-56
9591783-4	1998	Based on these results, we propose a mechanism by which PAb1620 can allosterically inhibit p53 binding to DNA through an indirect interaction between the antibody binding site and the L1 loop (amino acids 112-124) of p53, which is a component of the DNA binding region.	pab1620	56-63	tumor protein p53	Homo sapiens	91-94
9591783-4	1998	Based on these results, we propose a mechanism by which PAb1620 can allosterically inhibit p53 binding to DNA through an indirect interaction between the antibody binding site and the L1 loop (amino acids 112-124) of p53, which is a component of the DNA binding region.	pab1620	56-63	tumor protein p53	Homo sapiens	217-220
7845681-4	1995	For murine p53 (mp53) we show (i) the 1620+ form is retained and stabilised in complex with DNA, and (ii) the complexes are dissociated by the PAb1620 monoclonal antibody.	pab1620	143-150	transformation related protein 53, pseudogene	Mus musculus	11-14
7966288-5	1994	Two conformation-specific anti-p53 monoclonal antibodies were used to dissect the phage-p53 interaction, the phage were found to preferentially bind the PAb1620-p53 conformation rather than the PAb240-p53 conformation.	pab1620	153-160	tumor protein p53	Homo sapiens	31-34
7966288-5	1994	Two conformation-specific anti-p53 monoclonal antibodies were used to dissect the phage-p53 interaction, the phage were found to preferentially bind the PAb1620-p53 conformation rather than the PAb240-p53 conformation.	pab1620	153-160	tumor protein p53	Homo sapiens	88-91
7966288-5	1994	Two conformation-specific anti-p53 monoclonal antibodies were used to dissect the phage-p53 interaction, the phage were found to preferentially bind the PAb1620-p53 conformation rather than the PAb240-p53 conformation.	pab1620	153-160	tumor protein p53	Homo sapiens	88-91
7966288-5	1994	Two conformation-specific anti-p53 monoclonal antibodies were used to dissect the phage-p53 interaction, the phage were found to preferentially bind the PAb1620-p53 conformation rather than the PAb240-p53 conformation.	pab1620	153-160	tumor protein p53	Homo sapiens	88-91