PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9622489-1	1998	The role of dityrosine as a fluorescent crossbridge between adjacent calmodulin molecules within the high molecular mass polymers that are generated by Arthromyces peroxidase-catalyzed cross-linking [Malencik, D. A., and Anderson, S. R. (1996) Biochemistry 35, 4375] has been examined in frequency domain fluorescence anisotropy studies.	dityrosine	12-22	calmodulin 1	Homo sapiens	69-79	
1691599-6	1990	This method has been applied to the analysis of dityrosine in uv-irradiated calmodulin and cardiac troponin C and to the detection of phosphorylation sites in several polypeptides.	dityrosine	48-58	calmodulin 1	Homo sapiens	76-86	
2452650-5	1988	The fluorescence intensity and anisotropy of the dityrosine moiety demonstrate that this novel derivative undergoes interactions with calcium, smooth muscle myosin light chain kinase, and phenylagarose which are similar to those of unmodified calmodulin.	dityrosine	49-59	calmodulin 1	Homo sapiens	243-253	
14661087-6	2003	Calmodulin, which contains a single pair of tyrosyl residues, undergoes both photoactivated and enzyme-catalyzed dityrosine formation.	dityrosine	113-123	calmodulin 1	Homo sapiens	0-10	
14661087-7	2003	Polarization measurements, employing the intrinsic fluorescence of dityrosine, and catalytic activity determinations show how different patterns of inter- and intramolecular cross-linking affect the interactions of calmodulin with Ca(2+) and enzymes.	dityrosine	67-77	calmodulin 1	Homo sapiens	215-225