PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
3007520-4	1986	The uvsX protein purified from cells with a uvsX+ plasmid catalyzes ATP hydrolysis to ADP and AMP and, in the presence of the T4 gene 32 helix-destablizing protein, ATP-dependent strand exchange between homologous circular single-stranded and linear duplex DNA.	Adenosine Triphosphate	68-71	recombinase RecA	Escherichia phage T4	4-8
2522995-5	1989	UvsY protein enhances the rate of single-stranded-DNA-dependent ATP hydrolysis by UvsX protein, particularly in the presence of gp32 or high concentrations of salt, factors that otherwise reduce the ATPase activity of UvsX protein.	Adenosine Triphosphate	64-67	recombinase RecA	Escherichia phage T4	82-86
2522995-5	1989	UvsY protein enhances the rate of single-stranded-DNA-dependent ATP hydrolysis by UvsX protein, particularly in the presence of gp32 or high concentrations of salt, factors that otherwise reduce the ATPase activity of UvsX protein.	Adenosine Triphosphate	64-67	recombinase RecA	Escherichia phage T4	218-222
2522995-5	1989	UvsY protein enhances the rate of single-stranded-DNA-dependent ATP hydrolysis by UvsX protein, particularly in the presence of gp32 or high concentrations of salt, factors that otherwise reduce the ATPase activity of UvsX protein.	Salts	159-163	recombinase RecA	Escherichia phage T4	82-86
2522995-5	1989	UvsY protein enhances the rate of single-stranded-DNA-dependent ATP hydrolysis by UvsX protein, particularly in the presence of gp32 or high concentrations of salt, factors that otherwise reduce the ATPase activity of UvsX protein.	Salts	159-163	recombinase RecA	Escherichia phage T4	218-222
2522995-6	1989	The enhancement of ATP hydrolysis by UvsY protein is shown to result from the ability of UvsY protein to increase the affinity of UvsX protein for single-stranded DNA.	Adenosine Triphosphate	19-22	recombinase RecA	Escherichia phage T4	130-134
2967823-7	1988	The evidence suggests that individual uvsX protein monomers are continuously entering and leaving the cooperatively formed filament in a cycle that is strongly affected by their ATP hydrolysis.	Adenosine Triphosphate	178-181	recombinase RecA	Escherichia phage T4	38-42
2939071-6	1986	At physiological salt concentrations, the uvsX protein binds tightly and cooperatively to single-stranded DNA, covering about five nucleotides per protein monomer; at lower salt concentrations, a similar type of binding to double-stranded DNA is detected (Griffith, J., and Formosa, T., (1985) J. Biol.	Salts	17-21	recombinase RecA	Escherichia phage T4	42-46
2939071-6	1986	At physiological salt concentrations, the uvsX protein binds tightly and cooperatively to single-stranded DNA, covering about five nucleotides per protein monomer; at lower salt concentrations, a similar type of binding to double-stranded DNA is detected (Griffith, J., and Formosa, T., (1985) J. Biol.	Salts	173-177	recombinase RecA	Escherichia phage T4	42-46
2939071-11	1986	The catalysis of homologous pairing by the uvsX protein is shown to be greatly stimulated by the presence of the T4 gene 32 protein, a helix-destablizing protein previously studied in this laboratory, and it requires continued ATP hydrolysis.	Adenosine Triphosphate	227-230	recombinase RecA	Escherichia phage T4	43-47
3007520-4	1986	The uvsX protein purified from cells with a uvsX+ plasmid catalyzes ATP hydrolysis to ADP and AMP and, in the presence of the T4 gene 32 helix-destablizing protein, ATP-dependent strand exchange between homologous circular single-stranded and linear duplex DNA.	Adenosine Triphosphate	68-71	recombinase RecA	Escherichia phage T4	44-48
3007520-4	1986	The uvsX protein purified from cells with a uvsX+ plasmid catalyzes ATP hydrolysis to ADP and AMP and, in the presence of the T4 gene 32 helix-destablizing protein, ATP-dependent strand exchange between homologous circular single-stranded and linear duplex DNA.	Adenosine Diphosphate	86-89	recombinase RecA	Escherichia phage T4	4-8
3007520-4	1986	The uvsX protein purified from cells with a uvsX+ plasmid catalyzes ATP hydrolysis to ADP and AMP and, in the presence of the T4 gene 32 helix-destablizing protein, ATP-dependent strand exchange between homologous circular single-stranded and linear duplex DNA.	Adenosine Diphosphate	86-89	recombinase RecA	Escherichia phage T4	44-48
3007520-4	1986	The uvsX protein purified from cells with a uvsX+ plasmid catalyzes ATP hydrolysis to ADP and AMP and, in the presence of the T4 gene 32 helix-destablizing protein, ATP-dependent strand exchange between homologous circular single-stranded and linear duplex DNA.	Adenosine Monophosphate	94-97	recombinase RecA	Escherichia phage T4	4-8
3007520-4	1986	The uvsX protein purified from cells with a uvsX+ plasmid catalyzes ATP hydrolysis to ADP and AMP and, in the presence of the T4 gene 32 helix-destablizing protein, ATP-dependent strand exchange between homologous circular single-stranded and linear duplex DNA.	Adenosine Monophosphate	94-97	recombinase RecA	Escherichia phage T4	44-48
3007520-4	1986	The uvsX protein purified from cells with a uvsX+ plasmid catalyzes ATP hydrolysis to ADP and AMP and, in the presence of the T4 gene 32 helix-destablizing protein, ATP-dependent strand exchange between homologous circular single-stranded and linear duplex DNA.	Adenosine Triphosphate	165-168	recombinase RecA	Escherichia phage T4	4-8
8683569-0	1996	Bacteriophage T4 strand transfer protein UvsX tolerates symmetric and asymmetric heterologies in short double-stranded oligonucleotides.	Oligonucleotides	119-135	recombinase RecA	Escherichia phage T4	41-45
21035462-2	2011	We have determined the crystal structure of the T4 UvsX recombinase, and the overall architecture and fold closely resemble those of RecA, including a highly conserved ATP binding site.	Adenosine Triphosphate	168-171	recombinase RecA	Escherichia phage T4	51-55
21035462-3	2011	Based on this new structure, we reanalyzed electron microscopy reconstructions of UvsX-DNA filaments and docked the UvsX crystal structure into two different filament forms: a compressed filament generated in the presence of ADP and an elongated filament generated in the presence of ATP and aluminum fluoride.	Adenosine Diphosphate	225-228	recombinase RecA	Escherichia phage T4	116-120
21035462-3	2011	Based on this new structure, we reanalyzed electron microscopy reconstructions of UvsX-DNA filaments and docked the UvsX crystal structure into two different filament forms: a compressed filament generated in the presence of ADP and an elongated filament generated in the presence of ATP and aluminum fluoride.	Adenosine Triphosphate	284-287	recombinase RecA	Escherichia phage T4	116-120
21035462-3	2011	Based on this new structure, we reanalyzed electron microscopy reconstructions of UvsX-DNA filaments and docked the UvsX crystal structure into two different filament forms: a compressed filament generated in the presence of ADP and an elongated filament generated in the presence of ATP and aluminum fluoride.	aluminum fluoride	292-309	recombinase RecA	Escherichia phage T4	116-120
9790840-3	1998	Central to these three processes is the T4 UvsX protein, a member of the filamentous, ATP-dependent class of general recombination enzymes typified by the Escherichia coli RecA protein.	Adenosine Triphosphate	86-89	recombinase RecA	Escherichia phage T4	43-47
3156858-6	1985	In solutions containing Mg2+, the uvsX protein also binds cooperatively to ssDNA.	magnesium ion	24-28	recombinase RecA	Escherichia phage T4	34-38
19244311-8	2009	Other results suggest that UvsY acts as a nucleotide exchange factor for UvsX, enhancing filament stability by increasing the lifetime of the high-affinity, ATP-bound form of the enzyme.	Adenosine Triphosphate	157-160	recombinase RecA	Escherichia phage T4	73-77
16829679-6	2006	Under stringent salt conditions the disruption of Gp32-ssDNA by UvsX is both ATP- and UvsY-dependent.	Adenosine Triphosphate	77-80	recombinase RecA	Escherichia phage T4	64-68
16829679-10	2006	The data directly support the Gp32 displacement model of UvsY-mediated presynaptic filament assembly, and demonstrate that the transient induction of high affinity UvsX-ssDNA interactions by ATP are essential, although not sufficient, for Gp32 displacement.	Adenosine Triphosphate	191-194	recombinase RecA	Escherichia phage T4	164-168
8683569-2	1996	We demonstrate here that UvsX mediates strand transfer efficiently from synthetic double-stranded donor oligonucleotides of 30 to 117 bp in length to circular single-stranded recipient M13mp19 DNA.	Oligonucleotides	104-120	recombinase RecA	Escherichia phage T4	25-29
2002035-4	1991	Isolation of the complexes by centrifugation through a glycerol gradient revealed their protein constituents and showed that the uvsX protein-uvsY protein-24-mer ssDNA complex formed even in the presence of excess gene 32 protein.	Glycerol	55-63	recombinase RecA	Escherichia phage T4	129-133
8331653-3	1993	The bacteriophage T4 UvsX protein is only weakly homologous to RecA, but it has very similar ATP-dependent DNA binding and strand-exchange activities.	Adenosine Triphosphate	93-96	recombinase RecA	Escherichia phage T4	21-25
1851754-7	1991	It is found that the helicase also reduces the level of uvsX protein-mediated, single-stranded DNA-dependent ATP hydrolysis in the strand-exchange reactions, suggesting that the helicase may also act to destabilize the uvsX protein-DNA filaments that are important intermediates in the pairing reaction.	Adenosine Triphosphate	109-112	recombinase RecA	Escherichia phage T4	56-60
1851754-7	1991	It is found that the helicase also reduces the level of uvsX protein-mediated, single-stranded DNA-dependent ATP hydrolysis in the strand-exchange reactions, suggesting that the helicase may also act to destabilize the uvsX protein-DNA filaments that are important intermediates in the pairing reaction.	Adenosine Triphosphate	109-112	recombinase RecA	Escherichia phage T4	219-223
2146483-10	1990	A double-amber mutant of uvsX was also generated by oligonucleotide site-directed mutagenesis.	Oligonucleotides	52-67	recombinase RecA	Escherichia phage T4	25-29