PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
17977839-0	2008	hMSH4-hMSH5 adenosine nucleotide processing and interactions with homologous recombination machinery.	adenosine nucleotide	12-32	mutS homolog 4	Homo sapiens	0-5
20569198-10	2010	In this new state, adenosine nucleotide binding is competed for by other nucleotides (CTP, GTP and AMP-PNP), although ATP and ADP, but not the other nucleotides, partially stabilize the protein against spontaneous loss of aconitase activity when incubated at 37 degrees C. A mutant IRP-1(C437S) lacking aconitase activity shows only one ATP-binding site and lacks co-operativity.	adenosine nucleotide	19-39	aconitase 1	Homo sapiens	282-287
18790734-10	2008	We also demonstrate that these three mutations alter ATP-dependent conformation changes of hMSH2-hMSH6, suggesting that cancer-associated mutations in hMSH6 can disrupt the intramolecular signaling that coordinates mismatch binding with adenosine nucleotide processing.	adenosine nucleotide	237-257	mutS homolog 2	Homo sapiens	91-96
18790734-10	2008	We also demonstrate that these three mutations alter ATP-dependent conformation changes of hMSH2-hMSH6, suggesting that cancer-associated mutations in hMSH6 can disrupt the intramolecular signaling that coordinates mismatch binding with adenosine nucleotide processing.	adenosine nucleotide	237-257	mutS homolog 6	Homo sapiens	97-102
18790734-10	2008	We also demonstrate that these three mutations alter ATP-dependent conformation changes of hMSH2-hMSH6, suggesting that cancer-associated mutations in hMSH6 can disrupt the intramolecular signaling that coordinates mismatch binding with adenosine nucleotide processing.	adenosine nucleotide	237-257	mutS homolog 6	Homo sapiens	151-156
17977839-0	2008	hMSH4-hMSH5 adenosine nucleotide processing and interactions with homologous recombination machinery.	adenosine nucleotide	12-32	mutS homolog 5	Homo sapiens	6-11
15236592-5	2004	In the current study, the structural and regulatory consequences of adenosine nucleotide binding to GRP94 were investigated.	adenosine nucleotide	68-88	heat shock protein 90 beta family member 1	Homo sapiens	100-105
17602667-3	2007	We demonstrated that the probe reacted specifically with the lysine residue at the nucleotide-binding site of two purified adenosine nucleotide-binding proteins, Escherichia coli recombinase A (RecA) and Saccharomyces cerevisiae alcohol dehydrogenase-I (YADH-I).	adenosine nucleotide	123-143	RAD51 recombinase	Homo sapiens	194-198
16218172-1	2005	BACKGROUND: Tenofovir (TDF) is an adenosine nucleotide analogue that has been approved for the treatment of HIV-1 infection.	adenosine nucleotide	34-54	sex determining region Y	Homo sapiens	23-26
16397294-10	2006	The adenosine nucleotide cofactor bound to Ddx42p apparently acts as a switch that controls the two opposing activities: ATP triggers RNA strand separation, whereas ADP triggers annealing of complementary RNA strands.	adenosine nucleotide	4-24	DEAD-box helicase 42	Homo sapiens	43-49
16123314-6	2005	Nuclear magnetic resonance spectroscopy revealed a decline in alanine and a depletion of the adenosine nucleotide pool in vessels of 10-week-old apolipoprotein E(-/-) mice.	adenosine nucleotide	93-113	apolipoprotein E	Mus musculus	145-161
15123651-5	2004	Although there does not seem to be a long-lived interaction between hXRCC2 and hRAD51, we detail a strong adenosine nucleotide-regulated interaction between the hXRCC2-hRAD51D heterodimer and hRAD51.	adenosine nucleotide	106-126	X-ray repair cross complementing 2	Homo sapiens	161-167
15123651-5	2004	Although there does not seem to be a long-lived interaction between hXRCC2 and hRAD51, we detail a strong adenosine nucleotide-regulated interaction between the hXRCC2-hRAD51D heterodimer and hRAD51.	adenosine nucleotide	106-126	RAD51 recombinase	Homo sapiens	168-174
15123651-5	2004	Although there does not seem to be a long-lived interaction between hXRCC2 and hRAD51, we detail a strong adenosine nucleotide-regulated interaction between the hXRCC2-hRAD51D heterodimer and hRAD51.	adenosine nucleotide	106-126	RAD51 recombinase	Homo sapiens	168-174
15342215-0	2004	Inhibition of thrombin-induced signaling by resveratrol and quercetin: effects on adenosine nucleotide metabolism in endothelial cells and platelet-neutrophil interactions.	adenosine nucleotide	82-102	coagulation factor II, thrombin	Homo sapiens	14-22
15342215-11	2004	CONCLUSION: Quercetin and resveratrol interfere with the proinflammatory signaling of thrombin resulting in the inhibition of adenosine nucleotide secretion from activated platelets and decreased neutrophil function.	adenosine nucleotide	126-146	coagulation factor II, thrombin	Homo sapiens	86-94
15342215-2	2004	Depending on adenosine nucleotide levels, resting platelets inhibit and thrombin-activated platelets increase respiratory burst of neutrophils.	adenosine nucleotide	13-33	coagulation factor II, thrombin	Homo sapiens	72-80
15342215-12	2004	Moreover, the polyphenols protect endothelial adenosine nucleotide metabolism when downregulated by thrombin.	adenosine nucleotide	46-66	coagulation factor II, thrombin	Homo sapiens	100-108
15342215-3	2004	Whether the red wine polyphenols quercetin and resveratrol affect thrombin-dependent adenosine nucleotide, metabolism and thrombin-induced signaling is unknown.	adenosine nucleotide	85-105	coagulation factor II, thrombin	Homo sapiens	66-74
10878012-0	2000	The effect of O6-methylguanine DNA adducts on the adenosine nucleotide switch functions of hMSH2-hMSH6 and hMSH2-hMSH3.	adenosine nucleotide	50-70	mutS homolog 2	Homo sapiens	91-96
11498787-0	2001	Adenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1.	adenosine nucleotide	0-20	mutS homolog 2	Homo sapiens	64-69
11498787-0	2001	Adenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1.	adenosine nucleotide	0-20	BRCA1 DNA repair associated	Homo sapiens	74-79
11498787-2	2001	The BRCA1-hMSH2 association involved several well-defined regions of both proteins which include the adenosine nucleotide binding domain of hMSH2.	adenosine nucleotide	101-121	BRCA1 DNA repair associated	Homo sapiens	4-9
11498787-2	2001	The BRCA1-hMSH2 association involved several well-defined regions of both proteins which include the adenosine nucleotide binding domain of hMSH2.	adenosine nucleotide	101-121	mutS homolog 2	Homo sapiens	10-15
11498787-2	2001	The BRCA1-hMSH2 association involved several well-defined regions of both proteins which include the adenosine nucleotide binding domain of hMSH2.	adenosine nucleotide	101-121	mutS homolog 2	Homo sapiens	140-145
11498787-3	2001	Moreover, the interaction of BRCA1 with purified hMSH2-hMSH6 appears to be modulated by adenosine nucleotide much like G protein downstream interaction/signaling is modulated by guanosine nucleotide.	adenosine nucleotide	88-108	BRCA1 DNA repair associated	Homo sapiens	29-34
11498787-3	2001	Moreover, the interaction of BRCA1 with purified hMSH2-hMSH6 appears to be modulated by adenosine nucleotide much like G protein downstream interaction/signaling is modulated by guanosine nucleotide.	adenosine nucleotide	88-108	mutS homolog 2	Homo sapiens	49-54
11498787-3	2001	Moreover, the interaction of BRCA1 with purified hMSH2-hMSH6 appears to be modulated by adenosine nucleotide much like G protein downstream interaction/signaling is modulated by guanosine nucleotide.	adenosine nucleotide	88-108	mutS homolog 6	Homo sapiens	55-60
11498787-6	2001	These observations implicate BRCA1/BARD1 as downstream effectors of the adenosine nucleotide-activated hMSH2-hMSH6 signaling complex, and suggest a global role for BRCA1 in DNA damage processing.	adenosine nucleotide	72-92	BRCA1 DNA repair associated	Homo sapiens	29-34
11498787-6	2001	These observations implicate BRCA1/BARD1 as downstream effectors of the adenosine nucleotide-activated hMSH2-hMSH6 signaling complex, and suggest a global role for BRCA1 in DNA damage processing.	adenosine nucleotide	72-92	BRCA1 associated RING domain 1	Homo sapiens	35-40
11498787-6	2001	These observations implicate BRCA1/BARD1 as downstream effectors of the adenosine nucleotide-activated hMSH2-hMSH6 signaling complex, and suggest a global role for BRCA1 in DNA damage processing.	adenosine nucleotide	72-92	mutS homolog 2	Homo sapiens	103-108
11498787-6	2001	These observations implicate BRCA1/BARD1 as downstream effectors of the adenosine nucleotide-activated hMSH2-hMSH6 signaling complex, and suggest a global role for BRCA1 in DNA damage processing.	adenosine nucleotide	72-92	mutS homolog 6	Homo sapiens	109-114
11498787-6	2001	These observations implicate BRCA1/BARD1 as downstream effectors of the adenosine nucleotide-activated hMSH2-hMSH6 signaling complex, and suggest a global role for BRCA1 in DNA damage processing.	adenosine nucleotide	72-92	BRCA1 DNA repair associated	Homo sapiens	164-169
10878012-0	2000	The effect of O6-methylguanine DNA adducts on the adenosine nucleotide switch functions of hMSH2-hMSH6 and hMSH2-hMSH3.	adenosine nucleotide	50-70	mutS homolog 6	Homo sapiens	97-102
10878012-0	2000	The effect of O6-methylguanine DNA adducts on the adenosine nucleotide switch functions of hMSH2-hMSH6 and hMSH2-hMSH3.	adenosine nucleotide	50-70	mutS homolog 2	Homo sapiens	107-112
10878012-0	2000	The effect of O6-methylguanine DNA adducts on the adenosine nucleotide switch functions of hMSH2-hMSH6 and hMSH2-hMSH3.	adenosine nucleotide	50-70	mutS homolog 3	Homo sapiens	113-118
10816560-0	2000	Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94.	adenosine nucleotide	27-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
10816560-0	2000	Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94.	adenosine nucleotide	27-47	heat shock protein 90 beta family member 1	Homo sapiens	87-92
10816560-3	2000	The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket that also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol.	adenosine nucleotide	72-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	36-41
10816560-7	2000	bis-ANS activation of GRP94 function was efficiently blocked by radicicol, an established inhibitory ligand for the adenosine nucleotide binding pocket.	adenosine nucleotide	116-136	heat shock protein 90 beta family member 1	Homo sapiens	22-27
10816560-3	2000	The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket that also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol.	adenosine nucleotide	72-92	heat shock protein 90 alpha family class A member 1	Homo sapiens	153-158
10816561-0	2000	Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94.	adenosine nucleotide	27-47	heat shock protein 90 alpha family class A member 1	Homo sapiens	70-75
10816560-4	2000	Although this domain is essential for Hsp90 function, the molecular basis for adenosine nucleotide-dependent regulation of GRP94, the endoplasmic reticulum paralog of Hsp90, remains to be established.	adenosine nucleotide	78-98	heat shock protein 90 beta family member 1	Homo sapiens	123-128
10816561-0	2000	Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94.	adenosine nucleotide	27-47	heat shock protein 90 beta family member 1	Homo sapiens	87-92
10816560-4	2000	Although this domain is essential for Hsp90 function, the molecular basis for adenosine nucleotide-dependent regulation of GRP94, the endoplasmic reticulum paralog of Hsp90, remains to be established.	adenosine nucleotide	78-98	heat shock protein 90 alpha family class A member 1	Homo sapiens	167-172
10816560-5	2000	We report that bis-ANS (1,1"-bis(4-anilino-5-napthalenesulfonic acid), an environment sensitive fluorophore known to interact with nucleotide-binding domains, binds to the adenosine nucleotide-binding domain of GRP94 and thereby activates its molecular chaperone and peptide binding activities.	adenosine nucleotide	172-192	heat shock protein 90 beta family member 1	Homo sapiens	211-216
10078208-1	1999	Mismatch recognition by the human MutS homologs hMSH2-hMSH6 is regulated by adenosine nucleotide binding, supporting the hypothesis that it functions as a molecular switch.	adenosine nucleotide	76-96	mutS homolog 2	Homo sapiens	48-53
10419475-5	1999	These studies support the idea that hMSH2-hMSH3 functions as an adenosine nucleotide-regulated molecular switch that must be activated by mismatched nucleotides for classical mismatch repair to occur.	adenosine nucleotide	64-84	mutS homolog 2	Homo sapiens	36-41
10419475-5	1999	These studies support the idea that hMSH2-hMSH3 functions as an adenosine nucleotide-regulated molecular switch that must be activated by mismatched nucleotides for classical mismatch repair to occur.	adenosine nucleotide	64-84	mutS homolog 3	Homo sapiens	42-47
10814545-3	2000	We find that ribose and adenine, two major parts of the adenosine nucleotide, bind tightly to phenol sulfotransferase (PST) separately, and various nucleotides also bind tightly to PST.	adenosine nucleotide	56-76	sulfotransferase family 1A member 1	Homo sapiens	94-117
10814545-3	2000	We find that ribose and adenine, two major parts of the adenosine nucleotide, bind tightly to phenol sulfotransferase (PST) separately, and various nucleotides also bind tightly to PST.	adenosine nucleotide	56-76	sulfotransferase family 1A member 1	Homo sapiens	119-122
10814545-3	2000	We find that ribose and adenine, two major parts of the adenosine nucleotide, bind tightly to phenol sulfotransferase (PST) separately, and various nucleotides also bind tightly to PST.	adenosine nucleotide	56-76	sulfotransferase family 1A member 1	Homo sapiens	181-184
10657530-6	1999	The marked effect of the non-hydrolysable adenosine nucleotide App(NH)p also supports a cAMP-dependent TyrOH activation not related to ADP or an ADP-dependent mechanism.	adenosine nucleotide	42-62	amyloid beta precursor protein	Rattus norvegicus	63-71
10657530-6	1999	The marked effect of the non-hydrolysable adenosine nucleotide App(NH)p also supports a cAMP-dependent TyrOH activation not related to ADP or an ADP-dependent mechanism.	adenosine nucleotide	42-62	tyrosine hydroxylase	Rattus norvegicus	103-108
10078208-1	1999	Mismatch recognition by the human MutS homologs hMSH2-hMSH6 is regulated by adenosine nucleotide binding, supporting the hypothesis that it functions as a molecular switch.	adenosine nucleotide	76-96	mutS homolog 6	Homo sapiens	54-59
9297974-7	1997	Bcl-2-type molecules, being able to modulate the permeability transition pores by interaction with adenosine nucleotide translocators, may have played an essential role in conferring a means of controlling apoptosis.	adenosine nucleotide	99-119	BCL2 apoptosis regulator	Homo sapiens	0-5
6052711-0	1967	Effects of vitamins K1 and K3 on adenosine nucleotide content of rat tissues.	adenosine nucleotide	33-53	keratin 1	Rattus norvegicus	20-29
1532553-4	1992	oATP binding to the intact light sarcoplasmic reticulum is observed in the absence and presence of the competitive adenosine nucleotide inhibitor, fluorescein isothiocyanate with apparent affinity constants of 1.2 mM and 2.2 mM, respectively.	adenosine nucleotide	115-135	solute carrier organic anion transporter family member 1A2	Homo sapiens	0-4
2207277-0	1990	The linkage between adenosine nucleotide binding and amidase activity in human alpha-thrombin.	adenosine nucleotide	20-40	coagulation factor II, thrombin	Homo sapiens	85-93
2207277-4	1990	A simple, phenomenological description of the linkage between adenosine nucleotide binding and amidase activity of human alpha-thrombin is proposed and the free energy changes for the underlying reactions involved in the linkage scheme are resolved by global analysis of the experimental data.	adenosine nucleotide	62-82	coagulation factor II, thrombin	Homo sapiens	127-135
1008824-4	1976	Examples presented to illustrate the validity of the theory are of the latter type and are from studies on the myosin-adenosine nucleotide-PPi system.	adenosine nucleotide	118-138	myosin heavy chain 14	Homo sapiens	111-117
7883834-5	1995	Subsequently, digestion of polymerase chain reaction-amplified portions of exon 4 of the apo E gene with endonucleases HaeIII, TaqI, and Sau3AI demonstrated a second DNA variant that encoded a single amino acid substitution (gly127-->asp, G127D) due to a guanosine-to-adenosine nucleotide change resulting in the apo E1 isoform (G127D, R158C), which had arisen from a parent apo E2 allele.	adenosine nucleotide	271-291	apolipoprotein E	Homo sapiens	89-94
3030408-10	1987	However, whenever the first and/or third adenosine nucleotide units were replaced by tubercidin, a dramatic decrease in ability to activate RNase L occurred.	adenosine nucleotide	41-61	ribonuclease L (2', 5'-oligoisoadenylate synthetase-dependent)	Mus musculus	140-147
24065680-4	2013	Molecular genetic analysis showed a homozygous UGT1A1 promoter mutation [A(TA)7TAA] and a heterozygous insertion of 1 adenosine nucleotide between positions 353 and 354 in exon 1 of UGT1A1 that caused a frameshift with a premature stop codon.	adenosine nucleotide	118-138	UDP glucuronosyltransferase family 1 member A1	Homo sapiens	182-188
30828714-3	2019	By solving the crystal structure of Prp22 in different adenosine nucleotide-free states, we identified two missing conformational snapshots of genuine DEAH-box ATPases that help to unravel the molecular mechanism of translocation for this protein family.	adenosine nucleotide	55-75	DEAH-box helicase 8	Homo sapiens	36-41