PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7546215-0	1995	Vanadium (IV) inhibits calmodulin-stimulated skeletal muscle myosin light chain kinase activity.	Vanadium	0-8	calmodulin	Oryctolagus cuniculus	23-33	
7546215-2	1995	Using electron spin resonance spectroscopy, we have demonstrated that vanadyl, vanadium (IV), the predominant intracellular form of vanadate (vanadium V), binds to calmodulin in the presence of physiological concentrations of magnesium, extending earlier work which showed competitive binding of vanadyl and calcium to calmodulin.	Vanadium	79-87	calmodulin	Oryctolagus cuniculus	164-174	
7546215-2	1995	Using electron spin resonance spectroscopy, we have demonstrated that vanadyl, vanadium (IV), the predominant intracellular form of vanadate (vanadium V), binds to calmodulin in the presence of physiological concentrations of magnesium, extending earlier work which showed competitive binding of vanadyl and calcium to calmodulin.	Vanadium	79-87	calmodulin	Oryctolagus cuniculus	319-329	
7546215-2	1995	Using electron spin resonance spectroscopy, we have demonstrated that vanadyl, vanadium (IV), the predominant intracellular form of vanadate (vanadium V), binds to calmodulin in the presence of physiological concentrations of magnesium, extending earlier work which showed competitive binding of vanadyl and calcium to calmodulin.	Vanadium	142-152	calmodulin	Oryctolagus cuniculus	164-174