PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22291144-2	2012	To better understand how myoV navigates along actin, we used polarized total internal reflection fluorescence microscopy to examine angular changes of bifunctional rhodamine probes on the lever arms of single myoV molecules in vitro.	Rhodamines	164-173	myosin VA	Homo sapiens	209-213	
23528086-2	2013	We used high-speed polarized total internal reflection fluorescence (polTIRF) microscopy to study the structural dynamics of single myosin V molecules that had been labeled with bifunctional rhodamine linked to one of the calmodulins along the lever arm.	Rhodamines	191-200	myosin VA	Homo sapiens	132-140	
16614073-4	2006	We have measured the 3D orientation and stepping behavior of single bifunctional rhodamine probes attached to one of the calmodulins of the light-chain domain (LCD) of myosin V as myosin V moves along actin.	Rhodamines	81-90	myosin VA	Homo sapiens	168-176	
16614073-4	2006	We have measured the 3D orientation and stepping behavior of single bifunctional rhodamine probes attached to one of the calmodulins of the light-chain domain (LCD) of myosin V as myosin V moves along actin.	Rhodamines	81-90	myosin VA	Homo sapiens	180-188