PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7999774-2	1994	We have purified and partially characterized a Ni(2+)-binding protein (p40) from HeLa cell extracts that can specifically enhance the polymerase activity of DNA polymerase alpha (pol alpha) and other DNA polymerases in response to Ni2+.	Nickel(2+)	231-235	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	157-177	
7999774-2	1994	We have purified and partially characterized a Ni(2+)-binding protein (p40) from HeLa cell extracts that can specifically enhance the polymerase activity of DNA polymerase alpha (pol alpha) and other DNA polymerases in response to Ni2+.	Nickel(2+)	231-235	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	179-188	
7999774-5	1994	The p40 increased by 3- to 6-fold the rates at which pol alpha and the Klenow fragment of Escherichia coli DNA polymerase I (KF) replicate different DNA templates in response to Ni2+.	Nickel(2+)	178-182	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	53-62	
8162578-0	1994	The effect of divalent nickel (Ni2+) on in vitro DNA replication by DNA polymerase alpha.	Nickel(2+)	31-35	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	68-88	
8162578-2	1994	In the absence of Mg2+, the presence of Ni2+ ions at concentrations below 0.25 mM gave rise to a dose-dependent activation of pol alpha as monitored by [3H]dTMP incorporation into an activated DNA template.	Nickel(2+)	40-44	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	126-135	
8162578-3	1994	The apparent Km for Ni(2+)-dependent pol alpha incorporation of dTTP was estimated to be 25 microM, which was about 10 times higher than the Km for Mg2+ (2.3 microM).	Nickel(2+)	20-26	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	37-46	
8162578-4	1994	Above 0.25 mM, Ni2+ caused a dose-dependent inhibition of pol alpha activity and the Ki was calculated to be 1.5 mM.	Nickel(2+)	15-19	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	58-67	
8162578-5	1994	Scatchard analyses showed that Ni2+ binds to affinity-purified pol alpha and associated proteins at two tight binding sites with a Kd of approximately 50 microM and at eight weak binding sites with a Kd of approximately 4 mM.	Nickel(2+)	31-35	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	63-72	
8403077-6	1993	Some polymerases, such as E. coli DNA polymerase I, AMV reverse transcriptase and human DNA polymerase alpha, can utilize Ni2+ as a weak substitute for Mg2+ during DNA replication.	Nickel(2+)	122-126	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	88-108	
8200062-6	1994	In the absence of Mg2+, the low response of either DNA polymerase alpha or Klenow fragment to stimulation by Ni2+ was thought to be enhanced by the presence of Ni(2+)-binding proteins presented in the crude HeLa cell extract.	Nickel(2+)	109-113	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	51-71	
8200062-6	1994	In the absence of Mg2+, the low response of either DNA polymerase alpha or Klenow fragment to stimulation by Ni2+ was thought to be enhanced by the presence of Ni(2+)-binding proteins presented in the crude HeLa cell extract.	Nickel(2+)	160-166	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	51-71