PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27794044-3	2017	We found that under these and adenosine diphosphate (ADP)-generating suppressive conditions for the recombinase activity, RecA or Rad51 at similar optimal concentrations enhances the DNA ligase-catalyzed dsDNA end-joining (DNA ligation) about 30- to 40-fold.	Adenosine Diphosphate	30-51	recombinase RAD51	Saccharomyces cerevisiae S288C	130-135	
27794044-3	2017	We found that under these and adenosine diphosphate (ADP)-generating suppressive conditions for the recombinase activity, RecA or Rad51 at similar optimal concentrations enhances the DNA ligase-catalyzed dsDNA end-joining (DNA ligation) about 30- to 40-fold.	Adenosine Diphosphate	53-56	recombinase RAD51	Saccharomyces cerevisiae S288C	130-135	
27794044-4	2017	The DNA ligation enhancement by RecA or Rad51 transforms most of the substrate DNA into multimers within 2-5 min, and for this enhancement, ADP is the common and best cofactor.	Adenosine Diphosphate	140-143	recombinase RAD51	Saccharomyces cerevisiae S288C	40-45	
17567608-5	2007	Experiments with Rad51-K191R as well as with wild-type Rad51-dsDNA filaments formed in the presence of ATP, ADP or ATP-gamma-S showed that efficient Rad51 turnover from dsDNA requires both the Rad51 ATPase and the Rad54 ATPase activities.	Adenosine Diphosphate	108-111	recombinase RAD51	Saccharomyces cerevisiae S288C	55-60	
19327367-6	2009	We show that Rad51 readily dissociates from DNA in the presence of ADP or in the absence of nucleotide cofactor, but that free ATP in solution confers a fivefold increase in the stability of the nucleoprotein filaments.	Adenosine Diphosphate	67-70	recombinase RAD51	Saccharomyces cerevisiae S288C	13-18	
17567608-5	2007	Experiments with Rad51-K191R as well as with wild-type Rad51-dsDNA filaments formed in the presence of ATP, ADP or ATP-gamma-S showed that efficient Rad51 turnover from dsDNA requires both the Rad51 ATPase and the Rad54 ATPase activities.	Adenosine Diphosphate	108-111	recombinase RAD51	Saccharomyces cerevisiae S288C	55-60	
17567608-5	2007	Experiments with Rad51-K191R as well as with wild-type Rad51-dsDNA filaments formed in the presence of ATP, ADP or ATP-gamma-S showed that efficient Rad51 turnover from dsDNA requires both the Rad51 ATPase and the Rad54 ATPase activities.	Adenosine Diphosphate	108-111	recombinase RAD51	Saccharomyces cerevisiae S288C	55-60	
9497339-4	1998	Rad51p binding to both 1-N6-ethenoadenosine and 3-N4-ethenocytidine ssDNA (epsilonDNA) and dsDNA requires the presence of Mg2+ and ATP; no binding occurs in the presence of ADP, AMP-PNP, or ATPgammaS.	Adenosine Diphosphate	173-176	recombinase RAD51	Saccharomyces cerevisiae S288C	0-6	
9497339-5	1998	Binding of Rad51p to dsDNA also requires ATP; ADP is ineffective, whereas ATPgammaS and AMP-PNP are considerably less able to promote binding and only at elevated concentrations of Rad51p.	Adenosine Diphosphate	46-49	recombinase RAD51	Saccharomyces cerevisiae S288C	11-17