PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
3754328-0	1986	The role of metaphosphate in the activation of the nucleotide by TPS and DCC in the oligonucleotide synthesis.	metaphosphate	12-25	DCC netrin 1 receptor	Homo sapiens	73-76
9477223-11	1998	Bioactivation of methamidophos via a metaphosphate analogue would directly yield a phosphorylated and aged AChE resistant to reactivating agents, an intriguing hypothesis worthy of further consideration.	metaphosphate	37-50	acetylcholinesterase	Mus musculus	107-111
25006262-6	2014	The simulations reveal that the catalytic strategy of myosin employs a three-pronged tactic: (i) Stabilization of the gamma-phosphate of ATP in a dissociated metaphosphate (PgammaO3(-)) state.	metaphosphate	158-171	myosin heavy chain 14	Homo sapiens	54-60
15368224-2	2004	Glasses were produced from NaH(2)PO(4) as a starting material, providing an intrinsic Na(2)O:P(2)O(5) ratio of 1:1 and giving an O/P = 3, that is, a metaphosphate.	metaphosphate	149-162	solute carrier family 10 member 3	Homo sapiens	131-136
24165121-2	2013	A combined quantum/classical analysis of this dissociated nucleotide state inside myosin provides a quantitative understanding of how the enzyme stabilizes this unusual metaphosphate.	metaphosphate	169-182	myosin heavy chain 14	Homo sapiens	82-88
12444784-11	2002	Thermal analysis (TGA and DSC) indicates that compounds 1-3 convert to the corresponding crystalline metaphosphate materials M(PO(3))(2), in each case at temperatures below 500 degrees C. Similarly, the thermal decomposition of 4 results in the formation of Mn(PO(3))(3) and Mn(2)P(2)O(7).	metaphosphate	101-114	desmocollin 3	Homo sapiens	26-29
12044161-2	2002	The catalytic mechanism of phospho-CDK2/cyclin A (pCDK2/cyclin A) has been probed with structural and kinetic studies using the trigonal NO(3)(-) ion, which can be viewed as a mimic of the metaphosphate transition state.	metaphosphate	189-202	cyclin dependent kinase 2	Homo sapiens	35-39
12044161-2	2002	The catalytic mechanism of phospho-CDK2/cyclin A (pCDK2/cyclin A) has been probed with structural and kinetic studies using the trigonal NO(3)(-) ion, which can be viewed as a mimic of the metaphosphate transition state.	metaphosphate	189-202	cyclin A2	Homo sapiens	40-48
12044161-2	2002	The catalytic mechanism of phospho-CDK2/cyclin A (pCDK2/cyclin A) has been probed with structural and kinetic studies using the trigonal NO(3)(-) ion, which can be viewed as a mimic of the metaphosphate transition state.	metaphosphate	189-202	cyclin A2	Homo sapiens	56-64