PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19804726-2	2009	To understand the myosin-ATP interaction and in particular, the interactions with the base, we have used molecular dynamics simulations to model the interactions of myosin with ATP, CTP, UTP, aza-ATP, ITP, and GTP (in decreasing order of effectiveness as a substrate for the generation of motility) docked at the active site.	Inosine Triphosphate	201-204	myosin heavy chain 14	Homo sapiens	165-171	
8649181-9	1996	ITP and UTP, in contrast to ATP, are less effective substrates for the myosin light chain kinase, and their effect on actin-myosin interaction is thus less than that of ATP.	Inosine Triphosphate	0-3	myosin heavy chain 14	Homo sapiens	71-77	
9266842-3	1997	On the other hand, with ATP analogues of CTP and ITP, sliding movements of cleaved actin and particularly intact actin were inhibited by native tropomyosin, indicating that native tropomyosin augmented specificity of the myosin substrate of NTP.	Inosine Triphosphate	49-52	myosin heavy chain 14	Homo sapiens	149-155	
6327728-6	1984	ATP gamma S and ITP are particularly interesting in that ATP gamma S, on the one hand, can be used by kinases to phosphorylate proteins (e.g., myosin light chains) but resists cleavage by phosphatases or adenosine triphosphatases (ATPases), e.g., myosin ATPase.	Inosine Triphosphate	16-19	myosin heavy chain 14	Homo sapiens	143-149	
6327728-6	1984	ATP gamma S and ITP are particularly interesting in that ATP gamma S, on the one hand, can be used by kinases to phosphorylate proteins (e.g., myosin light chains) but resists cleavage by phosphatases or adenosine triphosphatases (ATPases), e.g., myosin ATPase.	Inosine Triphosphate	16-19	myosin heavy chain 14	Homo sapiens	247-253	
6327728-7	1984	ITP, on the other hand, can be used by myosin ATPase but does not support Ca++/calmodulin mediated phosphorylation of myosin light chains by myosin light chain kinase.	Inosine Triphosphate	0-3	myosin heavy chain 14	Homo sapiens	39-45	
37922-1	1979	The rate of enzymic reaction of ATP, ITP, GTP with myosin is studied in the presence of potassiu, ammonium and calcium ions in H2O--D2O solutions.	Inosine Triphosphate	37-40	myosin heavy chain 14	Homo sapiens	51-57	
6652677-5	1983	Although ITP and GTP serve as myosin ATPase substrates, they do not cause BB contraction, myosin release, or phosphorylation.	Inosine Triphosphate	9-12	myosin heavy chain 14	Homo sapiens	30-36	
6124282-0	1982	[Role of cations in the occurrence of differences in the myosin hydrolysis of ATP and ITP].	Inosine Triphosphate	86-89	myosin heavy chain 14	Homo sapiens	57-63	
195936-9	1977	Blocking of S1 brought about the inhibition of ATP- and ITP-induced superprecipitation and Mg2+-ITPase activity, suggesting that S1-blocking decreases the affinity of myosin and actin.	Inosine Triphosphate	56-59	myosin heavy chain 14	Homo sapiens	167-173	
4309596-17	1969	The behaviour of the hydrolytic activity of myosin on ATP or ITP in the presence of both Ca(2+) and Mg(2+) is consistent with the explanation that the inhibition by Mg(2+) is due to the tight binding of Mg(2+) to myosin, whereas the activation by Ca(2+) is caused either by a weak binding of Ca(2+) to myosin or by CaATP(2-) or by both.	Inosine Triphosphate	61-64	myosin heavy chain 14	Homo sapiens	44-50	
4309596-5	1969	The relationship between the rate of hydrolysis of ATP or ITP and the concentration of Ca(2+) suggests that a relatively weak binding of Ca(2+) either to myosin or to the substrate nucleotide is responsible for the activation of the enzymic activity.	Inosine Triphosphate	58-61	myosin heavy chain 14	Homo sapiens	154-160	
4239137-1	1969	The Mg chelates of ITP, GTP, and UTP in addition to that of ATP were shown to be capable of causing complete relaxation of myofibrils as indicated by the complete inhibition of syneresis and the reduction of the NTPase activity to that of isolated myosin.	Inosine Triphosphate	19-22	myosin heavy chain 14	Homo sapiens	248-254	
14464767-0	1962	Effect of temperature on the rate of hydrolysis of adenosine triphosphate and inosine triphosphate by myosin with and without modifiers.	Inosine Triphosphate	78-98	myosin heavy chain 14	Homo sapiens	102-108	
19873391-14	1944	Effects similar to those of adenosinetriphosphate on the physicochemical properties of purified myosin have been obtained so far only with inosinetriphosphate.	Inosine Triphosphate	139-158	myosin heavy chain 14	Homo sapiens	96-102	
19873391-16	1944	Inorganic phosphate is split off by myosin from inosinetriphosphate as well as from adenosinetriphosphate.	Inosine Triphosphate	48-67	myosin heavy chain 14	Homo sapiens	36-42