PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9736494-4	1998	Comparison with a conjugate having only one phenanthroline unit linked to spermine showed that the high activity of Clip-Phen-spermine-Cu was not only due to the presence of spermine, which increases the affinity of the Clip-Phen entity for the DNA, but was effectively due to the presence of the two bridged phenanthroline entities.	Phenanthrolines	309-323	CAP-Gly domain containing linker protein 1	Homo sapiens	116-120	
11087339-1	2000	To target DNA A.T tracts, a three-ring polyamide containing an N-methylpyrrole amino acid has been linked, on solid support, to carboxylic derivatives of phenanthroline and dimers of phenanthroline: 2-Clip-Phen, 3-Clip-Phen, or 2-Clip-Phen containing a long tether.	Phenanthrolines	183-197	CAP-Gly domain containing linker protein 1	Homo sapiens	201-205	
11087339-1	2000	To target DNA A.T tracts, a three-ring polyamide containing an N-methylpyrrole amino acid has been linked, on solid support, to carboxylic derivatives of phenanthroline and dimers of phenanthroline: 2-Clip-Phen, 3-Clip-Phen, or 2-Clip-Phen containing a long tether.	Phenanthrolines	183-197	CAP-Gly domain containing linker protein 1	Homo sapiens	214-218	
11087339-1	2000	To target DNA A.T tracts, a three-ring polyamide containing an N-methylpyrrole amino acid has been linked, on solid support, to carboxylic derivatives of phenanthroline and dimers of phenanthroline: 2-Clip-Phen, 3-Clip-Phen, or 2-Clip-Phen containing a long tether.	Phenanthrolines	183-197	CAP-Gly domain containing linker protein 1	Homo sapiens	214-218	
9736494-4	1998	Comparison with a conjugate having only one phenanthroline unit linked to spermine showed that the high activity of Clip-Phen-spermine-Cu was not only due to the presence of spermine, which increases the affinity of the Clip-Phen entity for the DNA, but was effectively due to the presence of the two bridged phenanthroline entities.	Phenanthrolines	44-58	CAP-Gly domain containing linker protein 1	Homo sapiens	116-120	
9736494-4	1998	Comparison with a conjugate having only one phenanthroline unit linked to spermine showed that the high activity of Clip-Phen-spermine-Cu was not only due to the presence of spermine, which increases the affinity of the Clip-Phen entity for the DNA, but was effectively due to the presence of the two bridged phenanthroline entities.	Phenanthrolines	44-58	CAP-Gly domain containing linker protein 1	Homo sapiens	220-224	
9736494-4	1998	Comparison with a conjugate having only one phenanthroline unit linked to spermine showed that the high activity of Clip-Phen-spermine-Cu was not only due to the presence of spermine, which increases the affinity of the Clip-Phen entity for the DNA, but was effectively due to the presence of the two bridged phenanthroline entities.	Phenanthrolines	309-323	CAP-Gly domain containing linker protein 1	Homo sapiens	220-224	
31680391-0	2020	Oxidative DNA Cleavage with Clip-Phenanthroline Triplex Forming Oligonucleotide Hybrids.	Phenanthrolines	33-47	CAP-Gly domain containing linker protein 1	Homo sapiens	28-32	
31680391-1	2020	We report a systematic study of several new types of hybrids of Cu-chelated Clip-phenanthroline artificial metallonuclease (AMN) with triplex forming oligonucleotides (TFO) for sequence-specific cleavage of double stranded DNA.	Phenanthrolines	81-95	CAP-Gly domain containing linker protein 1	Homo sapiens	76-80