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(+)-huperzine A
synthetic enantiomer of the anti-Alzheimer drug (-)-huperzine A and of its natural homologue (-)-huperzine B, interacts with the anionic subsite of the active site
(-)-huperzine A
anti-Alzheimer drug
(-)-S-3-[1-(dimethylamino)ethyl]phenol
competitive reversible inhibitor
(2,3-trans)-3-(3-hydroxy-5-methoxyphenyl)-N-(4-hydroxyphenethyl)-7-((E)-3-[(4-hydroxyphenethyl)amino]-3-oxoprop-1-enyl)-2,3-dihydro-benzo[b][1,4]dioxine-2-carboxamide
-
(2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one
a rigid DNP-like analogue compound, shows mixed-type inhibition
(2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5-methoxy-2,3-dihydro-1H-inden-1-one
a rigid DNP-like analogue compound, shows mixed-type inhibition
(7R,11R)-huprine 19
huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236
(7S,11S)-huprine W
huprines are a family of nano- to femtomolar inhibitors of AChE with specificity for the A-site interaction. The main feature is the remarkable embedding of the chloroquinolinium moiety into an aromatic stacking pile involving Trp86/HuprineW/Tyr337/Phe338/Phe295/Trp236
(RS)-tacrine(10)-hupyridone
-
(S,S)-(-)-bis(10)-hupyridone
enzyme binding structure, analysis using structure PDB ID 1H22, detailed overview
1-(1-benzyl-7-chloro-4-methoxy-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(1-benzylindol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(4-amino-5-chloro-2-methoxyphenyl)-3-(1-butyl-4-piperidinyl)-1-propanone
i.e. RS67333
1-(7-chloro-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(7-chloro-4-methoxy-1-methyl-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-(7-chloro-4-methoxy-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-benzyl-3-[(2E)-4-(4-benzylpiperazin-1-yl)but-2-en-1-yl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
-
1-benzyl-3-[(2E)-4-(4-benzylpiperazin-1-yl)but-2-en-1-yl]-6-methyl-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
-
1-benzyl-3-[4-(4-benzylpiperazin-1-yl)butyl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
-
1-[1-(benzenesulfonyl)-7-chloro-4-methoxy-indol-5-yl]-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
-
1-[3-(4-benzylpiperazin-1-yl)propyl]-3-methyl-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
-
1-[5-(5-nitro-1H-indazol-3-yl)thiophen-3-yl]ethanone
-
2-(2-phenyl-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl)phenol
-
2-[2-(4-fluorophenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
2-[2-(4-methylphenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
-
3,3'-demethyl-grossamide
87.37% inhibition at 0.1 mg/ml
3,3'-demethyl-heliotropamide
62.84% inhibition at 0.1 mg/ml
3,3'-[nonane-1,9-diylbis[(3S)-3-ethylazepane-1,3-diyl]]diphenol
binding by a bis-(-)-nor-meptazinol derivative disrupts the catalytic triad, structure analysis and molecular docking, overview
3-(1-benzyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
-
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-1H-indol-5-yl)propan-1-one
-
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-2-trimethylsilyl-1H-indol-5-yl)propan-1-one
-
3-(1-butyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
-
3-benzyl-1-[3-(4-benzylpiperazin-1-yl)propyl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
-
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
-
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(4-methoxy-1Hindol-5-yl)propan-1-one
-
3-[1-(cyclopentylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
-
4-oxo-N,N,N-trimethylpentanaminium iodide
i.e. OTMA, a hydrolysable substrate analogue, binding structure analysis
4-[4-(4-benzylpiperazin-1-yl)butyl]pyrrolo[1,2-a]thieno[2,3-e]pyrazin-5(4H)-one
-
4-[4-(4-benzylpiperazin-1-yl)butyl]pyrrolo[1,2-a]thieno[3,2-e]pyrazin-5(4H)-one
-
5,5'-dithiobis(2-nitrobenzoic acid)
inactivation, the peripheral site ligand propidium accelerates inactivation in the wild type ChE2, but retards inactivation in the F312I mutant
5-(4-chlorophenyl)-N-[9-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]nonyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
-
5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
-
5-[(1-benzylpiperidin-4-yl)methoxy]-1-methylpyrrolo[1,2-a]thieno[2,3-e]pyrazine
-
5-[(1-benzylpiperidin-4-yl)methoxy]pyrrolo[1,2-a]thieno[3,2-e]pyrazine
-
5-[4-(4-benzylpiperazin-1-yl)butyl]-7-phenyl-1,5-dihydro-4H-furo[2,3-b]pyrrolo[2,3-d]pyridin-4-one
-
7-O-galloyl-D-sedoheptulose
a mixed-type inhibitor, enzyme interacting residues, overview
Acetylcholine
substrate inhibition due to choline exit being hindered by a substrate molecule bound at the peripheral site
acetylthiocholine
interaction with Glu199 of ATCh, substrate inhibition due to choline exit being hindered by a substrate molecule bound at the peripheral site
cannabisin A
47.13% inhibition at 0.1 mg/ml
cannabisin C
42.89% inhibition at 0.1 mg/ml
cannabisin D
13.97% inhibition at 0.1 mg/ml
cannabisin E
11.17% inhibition at 0.1 mg/ml
cannabisin F
47.16% inhibition at 0.1 mg/ml
cannabisin N
51.99% inhibition at 0.1 mg/ml
decamethonium
decamethonium is a prototypical dual binding site ligand of AChE that spans the active site gorge from the P-site to the choline binding pocket in the A-site, where it is stabilized by the cation-Pi interactions illustrated in its complex with Torpedo californica AChE (TcAChE), binding structure, overview
donecopride
synthesized from donepezil and RS67333, shows a double mechanism of action and good bioavailability. Replacement of the benzene ring of the compound by an indole residue should increase the interaction of the ligand with the peripheral anionic site (PAS), thus resulting in increased inhibition of beta-amyloid aggregation
ethyl 5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
-
grossamide
22.42% inhibition at 0.1 mg/ml
loganin
a mixed-type inhibitor, enzyme interacting residues, overview
morroniside
a noncompetitive inhibitor, enzyme interacting residues, overview
N-ethylmaleimide
inactivation
N-trans-caffeoyltyramine
83.28% inhibition at 0.1 mg/ml
N-trans-feruloyltyramine
13.25% inhibition at 0.1 mg/ml
propidium
structure of the complex is solved at 3.0 A resolution, absence involving Trp279 in TcAChE at the gorge
sodium 5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
-
thioflavin T
ThT, is not sufficiently long to span the P-site and the choline binding site pocket of enzyme TcAChE. The benzothiazole and dimethylaminophenyl rings, and the dimethylamino group of this ligand are coplanar and lay parallel to Trp279 and Tyr334 and Phe330, respectively. The dimethylamino group is at 3.3 A from the aromatic ring of Phe330 but remains far from the gorge bottom, at a distance of 8.5 A from the carboxylate oxygens of Glu199. This position at the P-site allows concomitant binding of A-site ligands like edrophonium or m-(N,N,N-trimethylammonio)trifluoroacetophenone (TMTFA) through an adjustment of the orientation of Phe330
[1-(2-nitrophenyl)-2,2,2-trifluoroethyl]-arsenocholine iodide
caged compound, binding structure and mechanism with AChE, binding within the active-site gorge, overview
(R,S)-1-benzyl-4-[(5,6-dimethoxy-1-indanon)-2-yl]methylpiperidine hydrochloride
-
E2020, acetylcholinesterase inhibitor used in treatment of Alzheimer's diaease, interacts with the active site and the peripheral anionic site of the enzyme
buxamine-B
-
50% inhibition at 0.074 mM, noncompetitive
buxamine-C
-
50% inhibition at 0.0075 mM, noncompetitive
BW284c51
-
a reversible elongated gorge-spanning inhibitor, which bridges the two sites, the anionic subsite at the bottom of the active-site gorge and the peripheral anionic site at the entrance to the gorge
decamethonium
-
a reversible elongated gorge-spanning inhibitor, which bridges the two sites, the anionic subsite at the bottom of the active-site gorge and the peripheral anionic site at the entrance to the gorge
edrophonium
-
a reversible active-site directed inhibitor, which interacts with the catalytic anionic subsite, at the bottom of the active-site gorge
epinorgalanthamine
-
isolated from mother liquors/waste material obtained after industrial production of galanthamine hydrobromide from Leucojum aestivum leaves
lycorine
-
isolated from mother liquors/waste material obtained after industrial production of galanthamine hydrobromide from Leucojum aestivum leaves
N-(14-methylallyl)norgalanthamine
-
isolated from mother liquors/waste material obtained after industrial production of galanthamine hydrobromide from Leucojum aestivum leaves, structure determination by NMR spectroscopy
N-allylnorgalanthamine
-
isolated from mother liquors/waste material obtained after industrial production of galanthamine hydrobromide from Leucojum aestivum leaves, structure determination by NMR spectroscopy
narwedine
-
isolated from mother liquors/waste material obtained after industrial production of galanthamine hydrobromide from Leucojum aestivum leaves
propidium
-
a reversible peripheral anionic site inhibitor, which interacts with a site at the entrance to the gorge
tacrine
-
a reversible active-site directed inhibitor, which interacts with the catalytic anionic subsite, at the bottom of the active-site gorge
tubocurarine
-
a reversible peripheral anionic site inhibitor, which interacts with a site at the entrance to the gorge
donepezil
-
donepezil
enzyme binding structure, analysis using structure PDB ID 1EVE, detailed overview
galantamine
-
galantamine
89.26% inhibition at 0.1 mg/ml, docking study using the enzyme's crystal structure, PBD ID 1DX6
rivastigmine
-
rivastigmine
trade name: Exelon, carbamylates the enzyme, 10% spontaneous reactivation after 48 h
galanthamine
-
-
galanthamine
-
mixed type inhibition
galanthamine
-
isolated from mother liquors/waste material obtained after industrial production of galanthamine hydrobromide from Leucojum aestivum leaves
additional information
binding structure of sulfhydryl reagents to AChE, overview
-
additional information
three-dimensional structure and molecular docking to AChE of benzodiazepine inhibitors, amino acid residues involved in docking, overview
-
additional information
inhibitor binding, molecular modelling, overview
-
additional information
inhibitor identification by docking and pharmacophore virtual screenings, overview
-
additional information
acetylcholinesterase inhibitory activities of lignanamides from hemp, Cannabis sativa, seeds, NMR compound structure analysis and structure comparisons, molecular modeling studies on AChE, overview
-
additional information
determination and analysis of the crystal structures of enzyme-bound ligands
-
additional information
development, synthesis, and evaluation of a series of indole derivatives possessing in vitro inhibitory activities against AChE, structure-function analysis, overview. Crystal structures of complexes of the most promising compounds with Torpedo californica AChE are solved in order to further understand their mode of inhibition
-
additional information
-
development, synthesis, and evaluation of a series of indole derivatives possessing in vitro inhibitory activities against AChE, structure-function analysis, overview. Crystal structures of complexes of the most promising compounds with Torpedo californica AChE are solved in order to further understand their mode of inhibition
-
additional information
kinetics and molecular docking studies of loganin, morroniside and 7-O-galloyl-D-sedoheptulose derived from Cornus officinalis fruits (Corni fructus) as cholinesterase and beta-secretase 1 inhibitors, overview
-
additional information
the DNP rigidification results in a likely entropy-enthalpy compensation with solvation effects contributing primarily to AChE binding affinity. Detailed kinetic study and inhibition mechanism of 1 and 2 with Torpedo californica AChE (TcAChE), enzyme-ligands crystal structure (PDB ID 5E4T) analysis, molecular docking study, overview
-
additional information
-
the DNP rigidification results in a likely entropy-enthalpy compensation with solvation effects contributing primarily to AChE binding affinity. Detailed kinetic study and inhibition mechanism of 1 and 2 with Torpedo californica AChE (TcAChE), enzyme-ligands crystal structure (PDB ID 5E4T) analysis, molecular docking study, overview
-
additional information
-
inhibitor structural screening by GC-MS, binding structure, overview
-
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0.0002606
1-(1-benzyl-7-chloro-4-methoxy-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.000133
1-(1-benzylindol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.0000288
1-(7-chloro-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.0000844
1-(7-chloro-4-methoxy-1-methyl-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.0000914
1-(7-chloro-4-methoxy-1H-indol-5-yl)-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.000045
1-benzyl-3-[(2E)-4-(4-benzylpiperazin-1-yl)but-2-en-1-yl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
Tetronarce californica
-
0.000553
1-benzyl-3-[(2E)-4-(4-benzylpiperazin-1-yl)but-2-en-1-yl]-6-methyl-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
Tetronarce californica
-
0.000298
1-benzyl-3-[4-(4-benzylpiperazin-1-yl)butyl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
Tetronarce californica
-
0.000559
1-[1-(benzenesulfonyl)-7-chloro-4-methoxy-indol-5-yl]-3-[1-(cyclohexylmethyl)-4-piperidyl]propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.00039
1-[3-(4-benzylpiperazin-1-yl)propyl]-3-methyl-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
Tetronarce californica
-
0.00054
1-[5-(5-nitro-1H-indazol-3-yl)thiophen-3-yl]ethanone
Tetronarce californica
-
0.0008
2-(2-phenyl-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl)phenol
Tetronarce californica
pH 8.0, 25°C
0.0011
2-[2-(4-fluorophenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
Tetronarce californica
pH 8.0, 25°C
0.0015
2-[2-(4-methylphenyl)-2,3,4,5-tetrahydro-1,5-benzothiazepin-4-yl]phenol
Tetronarce californica
pH 8.0, 25°C
0.0387
3,3'-demethyl-grossamide
Tetronarce californica
pH 7.8, 25°C
0.0462
3,3'-demethyl-heliotropamide
Tetronarce californica
pH 7.8, 25°C
0.0000133
3-(1-benzyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.0000204
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.000275
3-(1-benzyl-4-piperidyl)-1-(7-chloro-4-methoxy-2-trimethylsilyl-1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.000716
3-(1-butyl-4-piperidyl)-1-(1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.001374
3-benzyl-1-[3-(4-benzylpiperazin-1-yl)propyl]-1,3-dihydro-2H-thieno[2,3-d]imidazol-2-one
Tetronarce californica
-
0.000051
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.00004
3-[1-(cyclohexylmethyl)-4-piperidyl]-1-(4-methoxy-1Hindol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.000094
3-[1-(cyclopentylmethyl)-4-piperidyl]-1-(1H-indol-5-yl)propan-1-one
Tetronarce californica
pH 8.0, 25°C
0.001283
4-[4-(4-benzylpiperazin-1-yl)butyl]pyrrolo[1,2-a]thieno[2,3-e]pyrazin-5(4H)-one
Tetronarce californica
-
0.000514
4-[4-(4-benzylpiperazin-1-yl)butyl]pyrrolo[1,2-a]thieno[3,2-e]pyrazin-5(4H)-one
Tetronarce californica
-
0.000093
5-(4-chlorophenyl)-N-[9-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]nonyl]-3,4-dihydro-2H-pyrano[3,2-c]quinoline-9-carboxamide
Tetronarce californica
-
0.000015
5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
Tetronarce californica
-
0.000527
5-[(1-benzylpiperidin-4-yl)methoxy]-1-methylpyrrolo[1,2-a]thieno[2,3-e]pyrazine
Tetronarce californica
-
0.000423
5-[(1-benzylpiperidin-4-yl)methoxy]pyrrolo[1,2-a]thieno[3,2-e]pyrazine
Tetronarce californica
-
0.000183
5-[4-(4-benzylpiperazin-1-yl)butyl]-7-phenyl-1,5-dihydro-4H-furo[2,3-b]pyrrolo[2,3-d]pyridin-4-one
Tetronarce californica
-
0.0105
7-O-galloyl-D-sedoheptulose
Tetronarce californica
pH and temperature not specified in the publication
0.00045
Berberine
Tetronarce californica
pH and temperature not specified in the publication
0.00006
ethyl 5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
Tetronarce californica
-
0.00276
galantamine
Tetronarce californica
pH 7.8, 25°C
0.00033
loganin
Tetronarce californica
pH and temperature not specified in the publication
0.00395
morroniside
Tetronarce californica
pH and temperature not specified in the publication
0.216
N-trans-caffeoyltyramine
Tetronarce californica
pH 7.8, 25°C
0.0000053
sodium 5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
Tetronarce californica
-
0.00182
galanthamine
Tetronarce californica
-
-
0.00016
N-(14-methylallyl)norgalanthamine
Tetronarce californica
-
-
0.00018
N-allylnorgalanthamine
Tetronarce californica
-
-
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analysis of crystal structure PDB ID 4ey4
complex with rivastigmine or (-)-S-3-[1-(dimethylamino)ethyl]phenol, hanging drop vapor diffusion method
complexed with (-)-huperzine B and (+)-huperzine A
enzyme in complex with inhibitors (2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one and (2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5-methoxy-2,3-dihydro-1H-inden-1-one, ligands dissolved in 100 mM DMSO, soaking of native crystals at 4°C for 24 h, in a solution containing 2 mM (2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one or (2E)-2-[(1-benzylpiperidin-4-yl)methylidene]-5-methoxy-2,3-dihydro-1H-inden-1-one, 30% PEG 200, 8% DMSO, and 100 mM MES at pH 6.2, X-ray diffraction structure determination and analysis at 2.17.A and 2.25 A resolution, respectively
in complex with aflatoxin
native enzyme by hanging-drop vapour diffusion method, 4°C, 11.5 mg/ml protein, mother liquor is 32% PEG 200 in 0.15 M MES, pH 5.8-6.2, soaking of crystals at 4°C in mother liquor at pH 6.0, containing either 0.5 mM OTMA for 24 h in 5 ml soaking solution, 20 mM TCh for 12 h in 5 ml soaking solution, 500 mM ATCh for 40 min in 1.5 ml soaking solution, or 20 mM ATCh for 12 h in 200 ml soaking solution, X-ray diffraction structure determination and anaylsis at 2.0-2.7 A resolution
purified enzyme with bound bis-(-)-nor-meptazinol derivative 3,3'-[nonane-1,9-diylbis[(3S)-3-ethylazepane-1,3-diyl]]diphenol, trigonal crystals of the enzyme are soaked for 20 h at 4°C in 0.002 ml of 1 mM 5h dissolved in the crystallization solution containing 40% PEG 200 v/v, 150 mM MES, pH 7.4, by hanging drop procedure, X-ray diffraction structure determination and analysis at 2.7 A resolution
purified enzyme, hangingdrop vapour-diffusion method, 4°C, 11.5 mg/ml protein, the mother liquor contains 32% PEG 200, 0.15 M MES, pH 5.8-6.2, soaking of the crystals in the dark for 12 h at 4°C in mother liquor containing 5 mM [1-(2-nitrophenyl)-2,2,2-trifluoroethyl]-arsenocholine iodide, pH 6.0, X-ray diffraction structure determination and anaylsis at 2.4 A resolution
trigonal and orthorhombic crystals in complex with inhibitor (RS)-tacrine(10)-hupyridone
X-ray diffraction crystal structure determination at 1.8 A resolution, crystal structure analysis of ligand-complexed enzyme and of native enzyme side-chain conformations accessed by molecular dynamics simulations, structure comparisons, overview
crystal structure analysis, overview
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Dvir, H.; Jiang, H.L.; Wong, D.M.; Harel, M.; Chetrit, M.; He, X.C.; Jin, G.Y.; Yu, G.L.; Tang, X.C.; Silman, I.; Bai, D.L.; Sussman, J.L.
X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-huperzine A and (-)-huperzine B: Structural evidence for an active site rearrangement
Biochemistry
41
10810-10818
2002
Tetronarce californica (P04058), Tetronarce californica
brenda
Bar-On, P.; Millard, C.B.; Harel, M.; Dvir, H.; Enz, A.; Sussman, J.L.; Silman, I.
Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug Rivastigmine
Biochemistry
41
3555-3564
2002
Drosophila melanogaster, Homo sapiens, Tetronarce californica (P04058), Tetronarce californica
brenda
Saxena, A.; Fedorko, J.M.; Vinayaka, C.R.; Medhekar, R.; Radic, Z.; Taylor, P.; Lockridge, O.; Doctor, B.P.
Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept) to cholinesterases
Eur. J. Biochem.
270
4447-4458
2003
Mus musculus, Tetronarce californica
brenda
Khalid, A.; Azim, M.K.; Parveen, S.; Atta ur, R.; Choudhary, M.I.
Structural basis of acetylcholinesterase inhibition by triterpenoidal alkaloids
Biochem. Biophys. Res. Commun.
331
1528-1532
2005
Tetronarce californica
brenda
Haviv, H.; Wong, D.M.; Greenblatt, H.M.; Carlier, P.R.; Pang, Y.P.; Silman, I.; Sussman, J.L.
Crystal packing mediates enantioselective ligand recognition at the peripheral site of acetylcholinesterase
J. Am. Chem. Soc.
127
11029-11036
2005
Tetronarce californica (P04058), Tetronarce californica
brenda
Colletier, J.P.; Royant, A.; Specht, A.; Sanson, B.; Nachon, F.; Masson, P.; Zaccai, G.; Sussman, J.L.; Goeldner, M.; Silman, I.; Bourgeois, D.; Weik, M.
Use of a caged analogue to study the traffic of choline within acetylcholinesterase by kinetic crystallography
Acta Crystallogr. Sect. D
63
1115-1128
2007
Tetronarce californica (P04058)
brenda
Colletier, J.P.; Fournier, D.; Greenblatt, H.M.; Stojan, J.; Sussman, J.L.; Zaccai, G.; Silman, I.; Weik, M.
Structural insights into substrate traffic and inhibition in acetylcholinesterase
EMBO J.
25
2746-2756
2006
Tetronarce californica (P04058), Tetronarce californica
brenda
Pezzementi, L.; Rowland, M.; Wolfe, M.; Tsigelny, I.
Inactivation of an invertebrate acetylcholinesterase by sulfhydryl reagents: the roles of two cysteines in the catalytic gorge of the enzyme
Invert. Neurosci.
6
47-55
2006
Tetronarce californica (P04058)
brenda
Weiner, L.; Shnyrov, V.L.; Konstantinovskii, L.; Roth, E.; Ashani, Y.; Silman, I.
Stabilization of Torpedo californica acetylcholinesterase by reversible inhibitors
Biochemistry
48
563-574
2009
Tetronarce californica
brenda
Berkov, S.; Codina, C.; Viladomat, F.; Bastida, J.
N-Alkylated galanthamine derivatives: potent acetylcholinesterase inhibitors from Leucojum aestivum
Bioorg. Med. Chem. Lett.
18
2263-2266
2008
Tetronarce californica
brenda
Nawaz, S.A.; Umbreen, S.; Kahlid, A.; Ansari, F.L.; Choudhary, M.I.
Structural insight into the inhibition of acetylcholinesterase by 2,3,4, 5-tetrahydro-1, 5-benzothiazepines
J. Enzyme Inhib. Med. Chem.
23
206-212
2008
Tetronarce californica (P04058)
brenda
Nemukhin, A.V.; Lushchekina, S.V.; Bochenkova, A.V.; Golubeva, A.A.; Varfolomeev, S.D.
Characterization of a complete cycle of acetylcholinesterase catalysis by ab initio QM/MM modeling
J. Mol. Model.
14
409-416
2008
Tetronarce californica
brenda
Xu, Y.; Colletier, J.P.; Jiang, H.; Silman, I.; Sussman, J.L.; Weik, M.
Induced-fit or preexisting equilibrium dynamics? Lessons from protein crystallography and MD simulations on acetylcholinesterase and implications for structure-based drug design
Protein Sci.
17
601-605
2008
Tetronarce californica (P04058)
brenda
Soriano, E.; Samadi, A.; Chioua, M.; Rios, C.D.; Marco-Contelles, J.
Molecular modelling, synthesis and acetylcholinesterase inhibition of ethyl 5-amino-2-methyl-6,7,8,9-tetrahydrobenzo[b][1,8]naphthyridine-3-carboxylate
Bioorg. Med. Chem. Lett.
20
2950-2953
2010
Tetronarce californica (P04058)
brenda
Sopkova-de Oliveira Santos, J.; Lesnard, A.; Agondanou, J.H.; Dupont, N.; Godard, A.M.; Stiebing, S.; Rochais, C.; Fabis, F.; Dallemagne, P.; Bureau, R.; Rault, S.
Virtual screening discovery of new acetylcholinesterase inhibitors issued from CERMN chemical library
J. Chem. Inf. Model.
50
422-428
2010
Tetronarce californica (P04058)
brenda
Paz, A.; Xie, Q.; Greenblatt, H.M.; Fu, W.; Tang, Y.; Silman, I.; Qiu, Z.; Sussman, J.L.
The crystal structure of a complex of acetylcholinesterase with a bis-(-)-nor-meptazinol derivative reveals disruption of the catalytic triad
J. Med. Chem.
52
2543-2549
2009
Tetronarce californica (P04058), Tetronarce californica
brenda
Sanson, B.; Colletier, J.P.; Xu, Y.; Lang, P.T.; Jiang, H.; Silman, I.; Sussman, J.L.; Weik, M.
Backdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and molecular dynamics simulations
Protein Sci.
20
1114-1118
2011
Tetronarce californica (P04058), Tetronarce californica
brenda
Meirer, K.; Glatzel, D.; Kretschmer, S.; Wittmann, S.K.; Hartmann, M.; Bloecher, R.; Angioni, C.; Geisslinger, G.; Steinhilber, D.; Hofmann, B.; Fuerst, R.; Proschak, E.
Design, synthesis and cellular characterization of a dual inhibitor of 5-lipoxygenase and soluble epoxide hydrolase
Molecules
22
45
2016
Pardosa pseudoannulata (A0A1B1FIV8), Pardosa pseudoannulata (A0A1B1FIW0), Pardosa pseudoannulata (A0A1B1FIW2), Pardosa pseudoannulata (A0A1B1FIZ1), Pardosa pseudoannulata (V5QQC6), Tetronarce californica (P04058), Homo sapiens (P22303), Tetranychus urticae (Q86CZ4)
brenda
Bhakta, H.K.; Park, C.H.; Yokozawa, T.; Min, B.S.; Jung, H.A.; Choi, J.S.
Kinetics and molecular docking studies of loganin, morroniside and 7-O-galloyl-D-sedoheptulose derived from Corni fructus as cholinesterase and beta-secretase 1 inhibitors
Arch. Pharm. Res.
39
794-805
2016
Tetronarce californica (P04058)
brenda
Lalut, J.; Santoni, G.; Karila, D.; Lecoutey, C.; Davis, A.; Nachon, F.; Silman, I.; Sussman, J.; Weik, M.; Maurice, T.; Dallemagne, P.; Rochais, C.
Novel multitarget-directed ligands targeting acetylcholinesterase and sigma1 receptors as lead compounds for treatment of Alzheimers disease synthesis, evaluation, and structural characterization of their complexes with acetylcholinesterase
Eur. J. Med. Chem.
162
234-248
2018
Tetronarce californica (P04058), Tetronarce californica, Homo sapiens (P22303)
brenda
Yan, X.; Tang, J.; dos Santos Passos, C.; Nurisso, A.; Simoes-Pires, C.A.; Ji, M.; Lou, H.; Fan, P.
Characterization of lignanamides from hemp (Cannabis sativa L.) seed and their antioxidant and acetylcholinesterase inhibitory activities
J. Agric. Food Chem.
63
10611-10619
2015
Tetronarce californica (P04058)
brenda
Caliandro, R.; Pesaresi, A.; Cariati, L.; Procopio, A.; Oliverio, M.; Lamba, D.
Kinetic and structural studies on the interactions of Torpedo californica acetylcholinesterase with two donepezil-like rigid analogues
J. Enzyme Inhib. Med. Chem.
33
794-803
2018
Tetronarce californica (P04058), Tetronarce californica
brenda