PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8399302-1	1993	In the presence as well as in the absence of calmodulin, Cd2+ inhibits the human erythrocyte plasma membrane Ca(2+)-ATPase activity non-competitively with Ki = 2 nM, whereas ATP-dependent Ca(2+)-transport across the red cell membrane was found to be inhibited competitively by Cd2+ (Verbost, P.M., Flik, G., Pang, P.K.T., Lock, R.A.C.	Adenosine Triphosphate	116-119	CD2 molecule	Homo sapiens	57-60	
9843450-12	1998	Kinetic studies revealed that inhibition by Cd2+ was competitive with respect to Mg2+ and noncompetitive with respect to MgATP.	Adenosine Triphosphate	121-126	CD2 molecule	Homo sapiens	44-47	
2992964-2	1985	In the presence of Cd2+ selectivity to ADP[alpha S] and to ATP[beta S] isomers is reversed; in the presence of Co2+, selectivity is lost.	Adenosine Triphosphate	59-62	CD2 molecule	Homo sapiens	19-22	
2944489-3	1986	By the same token Cd2+ inhibits the ADP and ATP exchange-reaction and also inhibits succinate oxidation.	Adenosine Triphosphate	44-47	CD2 molecule	Homo sapiens	18-21	
1648375-3	1991	The Cd2+ inhibition in the human erythrocyte was non-competitive with respect to Na+,K+, and ATP.	Adenosine Triphosphate	93-96	CD2 molecule	Homo sapiens	4-7	
6329303-2	1984	In the presence of Mg2+ the Rp diastereomers of both ATP[alpha S] and ATP[beta S] were the preferred substrates, whereas in the presence of Cd2+ the Sp diastereomers were the more active.	Adenosine Triphosphate	70-73	CD2 molecule	Homo sapiens	140-143	
6334536-1	1984	Stability constants for the Mg2+ and Cd2+ complexes of ATP, ADP, ATP alpha S, ATP beta S, and ADP alpha S have been determined at 30 degrees C and mu = 0.1 M by 31P NMR.	Adenosine Triphosphate	55-58	CD2 molecule	Homo sapiens	37-40	
6334536-1	1984	Stability constants for the Mg2+ and Cd2+ complexes of ATP, ADP, ATP alpha S, ATP beta S, and ADP alpha S have been determined at 30 degrees C and mu = 0.1 M by 31P NMR.	Adenosine Triphosphate	65-68	CD2 molecule	Homo sapiens	37-40	
6329303-5	1984	The Vmax for CdATP [gamma S] was some 90-fold less than that for MgATP[gamma S], suggesting that Cd2+ is bound to S from the gamma-P and that the breaking of the Cd-S bond is the rate determining step of the reaction.	Adenosine Triphosphate	65-70	CD2 molecule	Homo sapiens	97-100	
6329303-3	1984	Calculation of Vmax/Km values confirmed reversal of the Rp/Sp ratios for ATP[beta S] with Mg2+ [16] and Cd2+ [2], providing evidence that the metal is coordinated to the beta-phosphate at the active site.	Adenosine Triphosphate	73-76	CD2 molecule	Homo sapiens	104-107	
18359184-7	2008	We also found that EGCG and Cd2+ directly interacted with mitochondrial, and the mixture of EGCG and Cd2+ (EGCG+Cd2+) significantly caused loss of the mitochondrial membrane potential, decrease of the ATP content and activation of caspase-9 compared with EGCG treated alone.	Adenosine Triphosphate	201-204	CD2 molecule	Homo sapiens	28-31	
18359184-7	2008	We also found that EGCG and Cd2+ directly interacted with mitochondrial, and the mixture of EGCG and Cd2+ (EGCG+Cd2+) significantly caused loss of the mitochondrial membrane potential, decrease of the ATP content and activation of caspase-9 compared with EGCG treated alone.	Adenosine Triphosphate	201-204	CD2 molecule	Homo sapiens	101-104	
18359184-7	2008	We also found that EGCG and Cd2+ directly interacted with mitochondrial, and the mixture of EGCG and Cd2+ (EGCG+Cd2+) significantly caused loss of the mitochondrial membrane potential, decrease of the ATP content and activation of caspase-9 compared with EGCG treated alone.	Adenosine Triphosphate	201-204	CD2 molecule	Homo sapiens	101-104	
6235431-0	1984	Effects of Cd2+ on ATP-driven membrane potential in beef heart mitochondrial H+-ATPase: a study using the voltage-sensitive probe oxonol VI.	Adenosine Triphosphate	19-22	CD2 molecule	Homo sapiens	11-14	
16939420-4	2007	The AMP moiety of ATP binds at the ATP-binding site, and a Cd2+ ion binds at the active site and in a position to interact with the beta- and gamma-phosphates of ATP.	Adenosine Triphosphate	35-38	CD2 molecule	Homo sapiens	59-62	
16939420-4	2007	The AMP moiety of ATP binds at the ATP-binding site, and a Cd2+ ion binds at the active site and in a position to interact with the beta- and gamma-phosphates of ATP.	Adenosine Triphosphate	35-38	CD2 molecule	Homo sapiens	59-62