PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8558359-2	1995	The luminescence lifetime for Tb(III) measured by frequency domain fluorimetry increases from 1278 microseconds for the calmodulin complex to 1496 microsecond for the complex of calmodulin and M13, a peptide derived from the calmodulin target protein myosin light chain kinase.	Terbium	30-32	calmodulin 1	Homo sapiens	120-130	
8558359-2	1995	The luminescence lifetime for Tb(III) measured by frequency domain fluorimetry increases from 1278 microseconds for the calmodulin complex to 1496 microsecond for the complex of calmodulin and M13, a peptide derived from the calmodulin target protein myosin light chain kinase.	Terbium	30-32	calmodulin 1	Homo sapiens	178-188	
8558359-2	1995	The luminescence lifetime for Tb(III) measured by frequency domain fluorimetry increases from 1278 microseconds for the calmodulin complex to 1496 microsecond for the complex of calmodulin and M13, a peptide derived from the calmodulin target protein myosin light chain kinase.	Terbium	30-32	calmodulin 1	Homo sapiens	178-188	
1863267-0	1991	Effect of phosphorylation of calmodulin on calcium binding affinity as estimated by terbium fluorescence.	Terbium	84-91	calmodulin 1	Homo sapiens	29-39	
1863267-1	1991	The effect of phosphorylation of calmodulin by casein kinase 2 on the calcium binding of the former was studied by measurement of terbium fluorescence.	Terbium	130-137	calmodulin 1	Homo sapiens	33-43	
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.	Terbium	4-11	calmodulin 1	Homo sapiens	43-53	
6276400-2	1982	Terbium, a trivalent lanthanide, effectively substituted for Ca2+ in calmodulin as judged by several criteria: intrinsic fluorescence spectra, altered mobilities on polyacrylamide gel electrophoresis, formation of a stable complex with troponin I or calcineurin, and stimulation of phosphodiesterase.	Terbium	0-7	calmodulin 1	Homo sapiens	69-79	
3182830-3	1988	The combined study of direct calcium binding, modification of tryptophan fluorescence properties upon calcium binding, and terbium titration allows some discrimination among proposed mechanisms of cation binding to calmodulin.	Terbium	123-130	calmodulin 1	Homo sapiens	215-225	
3470740-1	1987	The fluorescence decay of the rare earth terbium when bound to the protein calmodulin changes from a simple exponential decay to a complex nonexponential decay as the temperature is lowered below 200 K. We have fit the observed decay curves by assuming that the terbium emission is a forced electric dipole transition and proteins have a distribution of continuous conformational states.	Terbium	41-48	calmodulin 1	Homo sapiens	75-85	
3470740-1	1987	The fluorescence decay of the rare earth terbium when bound to the protein calmodulin changes from a simple exponential decay to a complex nonexponential decay as the temperature is lowered below 200 K. We have fit the observed decay curves by assuming that the terbium emission is a forced electric dipole transition and proteins have a distribution of continuous conformational states.	Terbium	262-269	calmodulin 1	Homo sapiens	75-85	
15100408-1	2004	The conformational space sampled by the two-domain protein calmodulin has been explored by an approach based on four sets of NMR observables obtained on Tb(3+)- and Tm(3+)-substituted proteins.	Terbium	153-155	calmodulin 1	Homo sapiens	59-69	
15917089-5	2005	The CaM-CD2-III-5G-52 has stronger affinities to Ca(2+), Tb(3+) and La(3+) than CaM-CD2-IV-5G-52, indicating differential intrinsic metal-binding affinities of the EF-loops.	Terbium	57-59	calmodulin 1	Homo sapiens	4-7