PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
26502813-0	2016	Rhein-Huprine Derivatives Reduce Cognitive Impairment, Synaptic Failure and Amyloid Pathology in AbetaPPswe/PS-1 Mice of Different Ages.	huprine	6-13	presenilin 1	Mus musculus	108-112
26502813-2	2016	Two novel enantiopure rhein-huprine hybrids ((+)-1 and (-)-1) exhibit potent inhibitory effects against human acetylcholinesterase (AChE), butyrylcholinesterase (BuChE), BACE-1 and both Abeta and tau antiaggregation activity in vitro and reduction on the amyloid precursor protein (APP) processing in vivo.	huprine	28-35	acetylcholinesterase (Cartwright blood group)	Homo sapiens	110-130
26502813-2	2016	Two novel enantiopure rhein-huprine hybrids ((+)-1 and (-)-1) exhibit potent inhibitory effects against human acetylcholinesterase (AChE), butyrylcholinesterase (BuChE), BACE-1 and both Abeta and tau antiaggregation activity in vitro and reduction on the amyloid precursor protein (APP) processing in vivo.	huprine	28-35	acetylcholinesterase (Cartwright blood group)	Homo sapiens	132-136
26181606-4	2015	The levetiracetam-huprine hybrid 10 significantly reduced the incidence of epileptic seizures, cortical amyloid burden, and neuroinflammation in APP/PS1 mice after a 4-week treatment with a 5 mg/kg dose.	huprine	18-25	presenilin 1	Mus musculus	149-152
26502813-2	2016	Two novel enantiopure rhein-huprine hybrids ((+)-1 and (-)-1) exhibit potent inhibitory effects against human acetylcholinesterase (AChE), butyrylcholinesterase (BuChE), BACE-1 and both Abeta and tau antiaggregation activity in vitro and reduction on the amyloid precursor protein (APP) processing in vivo.	huprine	28-35	butyrylcholinesterase	Homo sapiens	139-160
26502813-2	2016	Two novel enantiopure rhein-huprine hybrids ((+)-1 and (-)-1) exhibit potent inhibitory effects against human acetylcholinesterase (AChE), butyrylcholinesterase (BuChE), BACE-1 and both Abeta and tau antiaggregation activity in vitro and reduction on the amyloid precursor protein (APP) processing in vivo.	huprine	28-35	butyrylcholinesterase	Homo sapiens	162-167
26502813-2	2016	Two novel enantiopure rhein-huprine hybrids ((+)-1 and (-)-1) exhibit potent inhibitory effects against human acetylcholinesterase (AChE), butyrylcholinesterase (BuChE), BACE-1 and both Abeta and tau antiaggregation activity in vitro and reduction on the amyloid precursor protein (APP) processing in vivo.	huprine	28-35	beta-secretase 1	Homo sapiens	170-176
26502813-2	2016	Two novel enantiopure rhein-huprine hybrids ((+)-1 and (-)-1) exhibit potent inhibitory effects against human acetylcholinesterase (AChE), butyrylcholinesterase (BuChE), BACE-1 and both Abeta and tau antiaggregation activity in vitro and reduction on the amyloid precursor protein (APP) processing in vivo.	huprine	28-35	microtubule associated protein tau	Homo sapiens	196-199
24216754-2	2014	Here, we report for the first time the use of the human acetylcholinesterase (AChE) as an enzyme for the design and synthesis of new potent heterodimeric huprine-based inhibitors.	huprine	154-161	acetylcholinesterase (Cartwright blood group)	Homo sapiens	56-76
24216754-2	2014	Here, we report for the first time the use of the human acetylcholinesterase (AChE) as an enzyme for the design and synthesis of new potent heterodimeric huprine-based inhibitors.	huprine	154-161	acetylcholinesterase (Cartwright blood group)	Homo sapiens	78-82
23522975-0	2013	Radiosynthesis and in vivo evaluation of fluorinated huprine derivates as PET radiotracers of acetylcholinesterase.	huprine	53-60	acetylcholinesterase	Rattus norvegicus	94-114
23679855-0	2013	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer"s drugs targeting acetyl- and butyryl-cholinesterase.	huprine	60-67	butyrylcholinesterase	Homo sapiens	28-42
23679855-3	2013	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.	huprine	178-185	acetylcholinesterase (Cartwright blood group)	Homo sapiens	73-78
23679855-3	2013	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.	huprine	178-185	butyrylcholinesterase	Homo sapiens	206-211
23679855-3	2013	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.	huprine	187-194	acetylcholinesterase (Cartwright blood group)	Homo sapiens	73-78
23679855-4	2013	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, pi-pi/cation-pi interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.	huprine	0-7	acetylcholinesterase (Cartwright blood group)	Homo sapiens	13-18
23679855-4	2013	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, pi-pi/cation-pi interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.	huprine	0-7	butyrylcholinesterase	Homo sapiens	34-39
23679855-5	2013	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.	huprine	0-7	acetylcholinesterase (Cartwright blood group)	Homo sapiens	45-50
23679855-5	2013	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.	huprine	0-7	butyrylcholinesterase	Homo sapiens	204-209
23522975-4	2013	METHODS: Three structural analogs of huprine, a specific AChE inhibitor presenting high affinity towards AChE in vitro, were synthesized and labeled with fluorine-18 via a mesylate/fluoro-nucleophilic aliphatic substitution: ([(18)F]-FHUa, [(18)F]-FHUb and [(18)F]-FHUc).	huprine	37-44	acetylcholinesterase	Rattus norvegicus	57-61
23522975-4	2013	METHODS: Three structural analogs of huprine, a specific AChE inhibitor presenting high affinity towards AChE in vitro, were synthesized and labeled with fluorine-18 via a mesylate/fluoro-nucleophilic aliphatic substitution: ([(18)F]-FHUa, [(18)F]-FHUb and [(18)F]-FHUc).	huprine	37-44	acetylcholinesterase	Rattus norvegicus	105-109
22726956-0	2012	Human butyrylcholinesterase produced in insect cells: huprine-based affinity purification and crystal structure.	huprine	54-61	butyrylcholinesterase	Homo sapiens	6-27
20689242-2	2010	Huprine X (HX), a reversible AChE inhibitor hybrid of tacrine and huperzine A, has shown to affect the amyloidogenic process in vitro.	huprine	0-7	acetylcholinesterase	Mus musculus	29-33
21344648-0	2011	New huprine derivatives functionalized at position 9 as highly potent acetylcholinesterase inhibitors.	huprine	4-11	acetylcholinesterase (Cartwright blood group)	Homo sapiens	70-90
21344648-1	2011	A series of 24 huprine derivatives diversely functionalized at position 9 have been synthesized and evaluated for their inhibitory activity against human recombinant acetylcholinesterase (AChE).	huprine	15-22	acetylcholinesterase (Cartwright blood group)	Homo sapiens	166-186
21344648-1	2011	A series of 24 huprine derivatives diversely functionalized at position 9 have been synthesized and evaluated for their inhibitory activity against human recombinant acetylcholinesterase (AChE).	huprine	15-22	acetylcholinesterase (Cartwright blood group)	Homo sapiens	188-192
11863435-7	2002	Steady-state inhibition data show that huprine X binds to human AChE and Torpedo AChE 28- and 54-fold, respectively, more tightly than tacrine.	huprine	39-46	acetylcholinesterase (Cartwright blood group)	Homo sapiens	64-68
19473849-0	2009	Synthesis and structure-activity relationship of Huprine derivatives as human acetylcholinesterase inhibitors.	huprine	49-56	acetylcholinesterase (Cartwright blood group)	Homo sapiens	78-98
19473849-1	2009	New series of Huprine (12-amino-6,7,10,11-tetrahydro-7,11-methanocycloocta[b]quinolines) derivatives have been synthesized and their inhibiting activities toward recombinant human acetylcholinesterase (rh-AChE) are reported.	huprine	14-21	acetylcholinesterase (Cartwright blood group)	Homo sapiens	180-200
19473849-1	2009	New series of Huprine (12-amino-6,7,10,11-tetrahydro-7,11-methanocycloocta[b]quinolines) derivatives have been synthesized and their inhibiting activities toward recombinant human acetylcholinesterase (rh-AChE) are reported.	huprine	14-21	acetylcholinesterase (Cartwright blood group)	Homo sapiens	205-209
11863435-7	2002	Steady-state inhibition data show that huprine X binds to human AChE and Torpedo AChE 28- and 54-fold, respectively, more tightly than tacrine.	huprine	39-46	acetylcholinesterase (Cartwright blood group)	Homo sapiens	81-85
11863435-9	2002	Furthermore, both tacrine and huprine X bind more tightly to Torpedo than to human AChE, suggesting that their quinoline substructures interact better with Phe330 than with Tyr337, the corresponding residue in the human AChE structure.	huprine	30-37	acetylcholinesterase (Cartwright blood group)	Homo sapiens	83-87
11863435-9	2002	Furthermore, both tacrine and huprine X bind more tightly to Torpedo than to human AChE, suggesting that their quinoline substructures interact better with Phe330 than with Tyr337, the corresponding residue in the human AChE structure.	huprine	30-37	acetylcholinesterase (Cartwright blood group)	Homo sapiens	220-224
10648652-6	2000	The association and dissociation rate constants for huprine X with AChE were determined, and the location of its binding site on the enzyme was probed in competition studies with the peripheral site inhibitor propidium and the acylation site inhibitor edrophonium.	huprine	52-59	acetylcholinesterase (Cartwright blood group)	Homo sapiens	67-71
10648652-8	2000	In contrast, huprine X did form a ternary complex with propidium and AChE, although its affinity for the free enzyme was found to be 17 times its affinity for the propidium-AChE complex.	huprine	13-20	acetylcholinesterase (Cartwright blood group)	Homo sapiens	69-73
10648652-8	2000	In contrast, huprine X did form a ternary complex with propidium and AChE, although its affinity for the free enzyme was found to be 17 times its affinity for the propidium-AChE complex.	huprine	13-20	acetylcholinesterase (Cartwright blood group)	Homo sapiens	173-177
34502472-3	2021	Huprine-derived molecules have a high affinity towards the enzyme acetylcholinesterase (AChE), act as potent Abeta(1-42) peptide aggregation inhibitors, and improve the behavior of experimental animals.	huprine	0-7	acetylcholinesterase (Cartwright blood group)	Homo sapiens	66-86
10648652-0	2000	Huprine X is a novel high-affinity inhibitor of acetylcholinesterase that is of interest for treatment of Alzheimer"s disease.	huprine	0-7	acetylcholinesterase (Cartwright blood group)	Homo sapiens	48-68
10648652-4	2000	Huprine X inhibited human AChE with an inhibition constant K(I) of 26 pM, indicating that it binds to this enzyme with one of the highest affinities yet reported.	huprine	0-7	acetylcholinesterase (Cartwright blood group)	Homo sapiens	26-30
34502472-3	2021	Huprine-derived molecules have a high affinity towards the enzyme acetylcholinesterase (AChE), act as potent Abeta(1-42) peptide aggregation inhibitors, and improve the behavior of experimental animals.	huprine	0-7	acetylcholinesterase (Cartwright blood group)	Homo sapiens	88-92
30181440-2	2018	AVCRI104P3 is a huprine derivative that exhibits potent inhibitory effects on human AChE, BuChE, and BACE-1 activities, as well as on AChE-induced and self-induced Abeta aggregation.	huprine	16-23	acetylcholinesterase (Cartwright blood group)	Homo sapiens	84-88
30181440-2	2018	AVCRI104P3 is a huprine derivative that exhibits potent inhibitory effects on human AChE, BuChE, and BACE-1 activities, as well as on AChE-induced and self-induced Abeta aggregation.	huprine	16-23	beta-secretase 1	Homo sapiens	101-107
27779818-7	2017	Furthermore, the binding free energy between the inhibitor and hAChE for hAChE/TZ5 is significantly lower than of either hAChE/huprine or hAChE/1YL.	huprine	127-134	acetylcholinesterase (Cartwright blood group)	Homo sapiens	63-68
29186056-7	2017	Here, we extend this study by solving the crystal structures of human BChE in complex with five reversible ligands, namely, decamethonium, thioflavin T, propidium, huprine, and ethopropazine.	huprine	164-171	butyrylcholinesterase	Homo sapiens	70-74
27779818-7	2017	Furthermore, the binding free energy between the inhibitor and hAChE for hAChE/TZ5 is significantly lower than of either hAChE/huprine or hAChE/1YL.	huprine	127-134	acetylcholinesterase (Cartwright blood group)	Homo sapiens	73-78
27779818-7	2017	Furthermore, the binding free energy between the inhibitor and hAChE for hAChE/TZ5 is significantly lower than of either hAChE/huprine or hAChE/1YL.	huprine	127-134	acetylcholinesterase (Cartwright blood group)	Homo sapiens	73-78
27779818-7	2017	Furthermore, the binding free energy between the inhibitor and hAChE for hAChE/TZ5 is significantly lower than of either hAChE/huprine or hAChE/1YL.	huprine	127-134	acetylcholinesterase (Cartwright blood group)	Homo sapiens	73-78
28125507-5	2017	Huprine X, a reversible AChE inhibitor, designed by molecular hybridization of tacrine and huperzine A, has been shown to affect the amyloidogenic process in vitro, and the AD-related neuropathology in vivo in mice models of the disease.	huprine	0-7	acetylcholinesterase	Mus musculus	24-28
28125507-6	2017	More recently, we have shown that a group of donepezil-huprine heterodimers exerts a highly potent and selective inhibitory action on AChE both in vitro and ex vivo, simultaneously interacting with both peripheral and catalytic binding sites, and inhibiting the beta-amyloid aggregation, whereas some levetiracetam-huprine hybrids have been shown to reduce epileptiform activity, neuroinflammation and amyloid burden in an animal model of AD.	huprine	55-62	acetylcholinesterase	Mus musculus	134-138
28125507-6	2017	More recently, we have shown that a group of donepezil-huprine heterodimers exerts a highly potent and selective inhibitory action on AChE both in vitro and ex vivo, simultaneously interacting with both peripheral and catalytic binding sites, and inhibiting the beta-amyloid aggregation, whereas some levetiracetam-huprine hybrids have been shown to reduce epileptiform activity, neuroinflammation and amyloid burden in an animal model of AD.	huprine	315-322	acetylcholinesterase	Mus musculus	134-138
27604478-2	2016	As anticipated by the initial properties of huprine, both probes displayed a high affinity and selectivity for AChE toward BChE, with IC50 values in the nanomolar range and without any non-specific binding in the tissues.	huprine	44-51	acetylcholinesterase (Cartwright blood group)	Homo sapiens	111-115
27604478-2	2016	As anticipated by the initial properties of huprine, both probes displayed a high affinity and selectivity for AChE toward BChE, with IC50 values in the nanomolar range and without any non-specific binding in the tissues.	huprine	44-51	butyrylcholinesterase	Homo sapiens	123-127