PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1658335-3	1991	Complexes of Rep protein were formed with short single-stranded and duplex hairpin oligodeoxynucleotides with lengths such that only a single Rep monomer could bind per oligodeoxynucleotide (i.e. 2 Rep monomers could not bind contiguously on the oligodeoxynucleotides).	Oligodeoxyribonucleotides	83-104	replication protein	Escherichia coli	13-16	
9454579-3	1998	Using fluorescence resonance energy transfer and stopped-flow techniques, we have examined the mechanism of ss-oligodeoxynucleotide binding to preformed Rep dimers in which one binding site is occupied by a single-stranded oligodeoxynucleotide, while the other site is free (P2S dimer).	Oligodeoxyribonucleotides	111-131	replication protein	Escherichia coli	153-156	
8918597-4	1996	Stopped-flow experiments show that the dissociation rate of a fluorescent ss oligodeoxynucleotide bound to one subunit of the dimeric Rep helicase is stimulated by ssDNA binding to the other subunit, and that the rate of this ssDNA exchange reaction is further stimulated approximately 60-fold upon ATP hydrolysis.	Oligodeoxyribonucleotides	77-97	replication protein	Escherichia coli	134-137	
8816749-1	1996	To examine the coupling of ATP hydrolysis to helicase translocation along DNA, we have purified and characterized complexes of the Escherichia coli Rep protein, a dimeric DNA helicase, covalently crosslinked to a single-stranded hexadecameric oligodeoxynucleotide (S).	Oligodeoxyribonucleotides	243-263	replication protein	Escherichia coli	148-151	
8652567-2	1996	Using stopped-flow fluorescence, we have determined a minimal kinetic mechanism for this reaction in which Rep monomer (P) binds to ss oligodeoxynucleotides (dN(pN)15) (S) by a two-step mechanism to form PS*, which can then dimerize with P to form P2S as indicated: [reaction in text].	Oligodeoxyribonucleotides	135-156	replication protein	Escherichia coli	107-110	
1658335-3	1991	Complexes of Rep protein were formed with short single-stranded and duplex hairpin oligodeoxynucleotides with lengths such that only a single Rep monomer could bind per oligodeoxynucleotide (i.e. 2 Rep monomers could not bind contiguously on the oligodeoxynucleotides).	Oligodeoxyribonucleotides	83-103	replication protein	Escherichia coli	13-16	
1658335-3	1991	Complexes of Rep protein were formed with short single-stranded and duplex hairpin oligodeoxynucleotides with lengths such that only a single Rep monomer could bind per oligodeoxynucleotide (i.e. 2 Rep monomers could not bind contiguously on the oligodeoxynucleotides).	Oligodeoxyribonucleotides	246-267	replication protein	Escherichia coli	13-16	
1658335-5	1991	However, the binding of Rep monomers to single-stranded (ss) oligodeoxynucleotides, d(pN)n (12 less than or equal to n less than or equal to 20), induces the Rep monomers to oligomerize.	Oligodeoxyribonucleotides	61-82	replication protein	Escherichia coli	24-27	
1658335-5	1991	However, the binding of Rep monomers to single-stranded (ss) oligodeoxynucleotides, d(pN)n (12 less than or equal to n less than or equal to 20), induces the Rep monomers to oligomerize.	Oligodeoxyribonucleotides	61-82	replication protein	Escherichia coli	158-161	
1658335-6	1991	Upon treatment of the Rep-ss oligodeoxynucleotide complexes with the protein crosslinking reagent dimethyl-suberimidate (DMS) and subsequent removal of the DNA, crosslinked Rep dimers are observed, independent of oligodeoxynucleotide length (n less than or equal to 20).	Oligodeoxyribonucleotides	29-49	replication protein	Escherichia coli	22-25	
1658335-6	1991	Upon treatment of the Rep-ss oligodeoxynucleotide complexes with the protein crosslinking reagent dimethyl-suberimidate (DMS) and subsequent removal of the DNA, crosslinked Rep dimers are observed, independent of oligodeoxynucleotide length (n less than or equal to 20).	Oligodeoxyribonucleotides	29-49	replication protein	Escherichia coli	173-176	
1658335-7	1991	Furthermore, short duplex oligodeoxynucleotides also induce the Rep monomers to dimerize.	Oligodeoxyribonucleotides	26-47	replication protein	Escherichia coli	64-67