PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10556528-1	1999	This work shows that the partial replacement of diamagnetic Ca2+ by paramagnetic Tb3+ in Ca2+/calmodulin systems in solution allows the measurement of interdomain NMR pseudocontact shifts and leads to magnetic alignment of the molecule such that significant residual dipolar couplings can be measured.	tb3+	81-85	calmodulin 1	Homo sapiens	94-104	
10556528-3	1999	Species in which Tb3+ ions are bound to only one domain of calmodulin (the N-domain) and Ca2+ ions to the other (the C-domain) provide convenient systems for measuring these parameters.	tb3+	17-21	calmodulin 1	Homo sapiens	59-69	
10556528-5	1999	In addition, the Tb3+ ions bound to the N-domain of calmodulin greatly enhance the magnetic susceptibility anisotropy of the molecule so that a certain degree of alignment is produced due to interaction with the external magnetic field.	tb3+	17-21	calmodulin 1	Homo sapiens	52-62	
1863267-2	1991	The binding of Tb3+ to calmodulin was followed by an increase in Tb3+ fluorescence at 545 nm.	tb3+	15-19	calmodulin 1	Homo sapiens	23-33	
1863267-2	1991	The binding of Tb3+ to calmodulin was followed by an increase in Tb3+ fluorescence at 545 nm.	tb3+	65-69	calmodulin 1	Homo sapiens	23-33	
1863267-3	1991	The terbium fluorescence of phosphorylated calmodulin increased at a lower concentration of Tb3+ than that of non-phosphorylated calmodulin, indicating that Tb3+ binding affinity of calmodulin was increased by phosphorylation.	tb3+	92-96	calmodulin 1	Homo sapiens	43-53	
1863267-3	1991	The terbium fluorescence of phosphorylated calmodulin increased at a lower concentration of Tb3+ than that of non-phosphorylated calmodulin, indicating that Tb3+ binding affinity of calmodulin was increased by phosphorylation.	tb3+	157-161	calmodulin 1	Homo sapiens	43-53	
1863267-3	1991	The terbium fluorescence of phosphorylated calmodulin increased at a lower concentration of Tb3+ than that of non-phosphorylated calmodulin, indicating that Tb3+ binding affinity of calmodulin was increased by phosphorylation.	tb3+	157-161	calmodulin 1	Homo sapiens	129-139	
1863267-3	1991	The terbium fluorescence of phosphorylated calmodulin increased at a lower concentration of Tb3+ than that of non-phosphorylated calmodulin, indicating that Tb3+ binding affinity of calmodulin was increased by phosphorylation.	tb3+	157-161	calmodulin 1	Homo sapiens	129-139	
3733748-1	1986	Distances between the four Ca2+-binding sites of calmodulin (CaM) have been measured by fluorescence energy transfer techniques using Eu3+ and Tb3+ as energy donors and a number of other lanthanide ions (Ln3+) as acceptors.	tb3+	143-147	calmodulin 1	Homo sapiens	49-59	
3733748-1	1986	Distances between the four Ca2+-binding sites of calmodulin (CaM) have been measured by fluorescence energy transfer techniques using Eu3+ and Tb3+ as energy donors and a number of other lanthanide ions (Ln3+) as acceptors.	tb3+	143-147	calmodulin 1	Homo sapiens	61-64	
3019337-1	1986	Calmodulin, spin labeled at Tyr-99, has been titrated with the lanthanides La3+, Nd3+, Eu3+, Tb3+, Er3+ and Lu3+ as well as Ca2+ and Cd2+.	tb3+	93-97	calmodulin 1	Homo sapiens	0-10	
4066663-3	1985	In the present study, we find that the metal cations La3+, Tb3+, Pb2+, and Cd2+ are all capable of abolishing the cooperativity (Hill coefficient = 2.0) among the two felodipine-binding sites on calmodulin and can increase the apparent affinity of calmodulin for felodipine by approximately 20-fold.	tb3+	59-63	calmodulin 1	Homo sapiens	195-205	
4066663-3	1985	In the present study, we find that the metal cations La3+, Tb3+, Pb2+, and Cd2+ are all capable of abolishing the cooperativity (Hill coefficient = 2.0) among the two felodipine-binding sites on calmodulin and can increase the apparent affinity of calmodulin for felodipine by approximately 20-fold.	tb3+	59-63	calmodulin 1	Homo sapiens	248-258	
4066663-6	1985	In each case, the calcium-binding sites of calmodulin must be occupied (by calcium, La3+, Tb3+, Pb2+, or by Cd2+) before these metals can bind to sites which are distinct from the calcium-binding sites to produce the active conformer of calmodulin which exhibits enhanced affinity for felodipine.	tb3+	90-94	calmodulin 1	Homo sapiens	43-53	
4079935-2	1985	The experimental results for protein preparations of calmodulin in which Ca2+ was isomorphically replaced by Tb3+ were obtained by a spectrometer working at the Institute of Nuclear Physics.	tb3+	109-113	calmodulin 1	Homo sapiens	53-63	
7084230-5	1982	With calmodulin selectively nitrated at either of the two tyrosine residues we found that, although both tyrosine groups can transfer energy to the bound Tb3+, the fluorescence of only Tyr-138 is sensitive to metal binding.	tb3+	154-158	calmodulin 1	Homo sapiens	5-15	
6276400-4	1982	The binding of Tb3+ to calmodulin was followed by the increase of Tb3+ fluorescence at 545 nm upon binding to calmodulin.	tb3+	15-19	calmodulin 1	Homo sapiens	23-33	
6276400-4	1982	The binding of Tb3+ to calmodulin was followed by the increase of Tb3+ fluorescence at 545 nm upon binding to calmodulin.	tb3+	15-19	calmodulin 1	Homo sapiens	110-120	
6276400-4	1982	The binding of Tb3+ to calmodulin was followed by the increase of Tb3+ fluorescence at 545 nm upon binding to calmodulin.	tb3+	66-70	calmodulin 1	Homo sapiens	23-33	
6276400-4	1982	The binding of Tb3+ to calmodulin was followed by the increase of Tb3+ fluorescence at 545 nm upon binding to calmodulin.	tb3+	66-70	calmodulin 1	Homo sapiens	110-120	
6276400-5	1982	This fluorescence was elicited either by exciting Tb3+ directly at 222 nm or by exciting the calmodulin tyrosine at 280 nm with resulting energy transfer from tyrosine to Tb3+.	tb3+	171-175	calmodulin 1	Homo sapiens	93-103