about
Slow-binding inhibition of acetylcholinesterase by an alkylammonium derivative of 6-methyluracil: mechanism and possible advantages for myasthenia gravis treatmentInteractions outside the proteinase-binding loop contribute significantly to the inhibition of activated coagulation factor XII by its canonical inhibitor from corn.Characterization of a novel BCHE "silent" allele: point mutation (p.Val204Asp) causes loss of activity and prolonged apnea with suxamethonium.New Infestin-4 Mutants with Increased Selectivity against Factor XIIa.Conjugates of γ-Carbolines and Phenothiazine as new selective inhibitors of butyrylcholinesterase and blockers of NMDA receptors for Alzheimer DiseaseSlow-binding inhibition of cholinesterases, pharmacological and toxicological relevance.Emergence of catalytic bioscavengers against organophosphorus agents.Synthesis, molecular docking, and biological activity of polyfluoroalkyl dihydroazolo[5,1-c][1,2,4]triazines as selective carboxylesterase inhibitors.Molecular modeling of mechanism of action of anti-myasthenia gravis slow-binding inhibitor of acetylcholinesterase.Novel conjugates of aminoadamantanes with carbazole derivatives as potential multitarget agents for AD treatment.Three Faces of N-Acetylaspartate: Activator, Substrate, and Inhibitor of Human Aspartoacylase.Correlation between the substrate structure and the rate of acetylcholinesterase hydrolysis modeled with the combined quantum mechanical/molecular mechanical studies.Research on cholinesterases in the Soviet Union and Russia: a historical perspective.Characterization of a novel butyrylcholinesterase point mutation (p.Ala34Val), "silent" with mivacurium.This special Issue of Chemico-Biological Interactions comprises 70 manuscripts from lectures and short talks given at the 11th International Meeting on Cholinesterases. Preface.Effects of viscosity and osmotic stress on the reaction of human butyrylcholinesterase with cresyl saligenin phosphate, a toxicant related to aerotoxic syndrome: kinetic and molecular dynamics studies.Characterization of a complete cycle of acetylcholinesterase catalysis by ab initio QM/MM modeling.Kinetics and mechanism of inhibition of serine esterases by fluorinated carbethoxy 1-aminophosphonates.Role of Protein Dimeric Interface in Allosteric Inhibition of N-Acetyl-Aspartate Hydrolysis by Human Aspartoacylase.Esterase profiles of organophosphorus compounds in vitro predict their behavior in vivo.9-Substituted acridine derivatives as acetylcholinesterase and butyrylcholinesterase inhibitors possessing antioxidant activity for Alzheimer's disease treatment.C-547, a 6-methyluracil derivative with long-lasting binding and rebinding on acetylcholinesterase: Pharmacokinetic and pharmacodynamic studies.6-Methyluracil derivatives as acetylcholinesterase inhibitors for treatment of Alzheimer's disease.6-Methyluracil Derivatives as Bifunctional Acetylcholinesterase Inhibitors for the Treatment of Alzheimer's Disease.Characterization of butyrylcholinesterase in bovine serum.Computation of entropy contribution to protein-ligand binding free energy.Computation of hydration free energies of organic solutes with an implicit water model.Optimization of Cholinesterase-Based Catalytic Bioscavengers Against Organophosphorus Agents.Human butyrylcholinesterase polymorphism: Molecular modeling.Understanding the non-catalytic behavior of human butyrylcholinesterase silent variants: Comparison of wild-type enzyme, catalytically active Ala328Cys mutant, and silent Ala328Asp variant.Modeling the Complete Catalytic Cycle of Aspartoacylase.Molecular modeling evidence for His438 flip in the mechanism of butyrylcholinesterase hysteretic behavior.3D structure of the natural tetrameric form of human butyrylcholinesterase as revealed by cryoEM, SAXS and MDCatalytic bioscavengers against organophosphorus agents: mechanistic issues of self-reactivating cholinesterasesSynthesis, molecular docking, and biological activity of 2-vinyl chromones: Toward selective butyrylcholinesterase inhibitors for potential Alzheimer's disease therapeuticsWater structure changes in oxime-mediated reactivation process of phosphorylated human acetylcholinesteraseSynthesis, molecular docking and biological evaluation of N,N-disubstituted 2-aminothiazolines as a new class of butyrylcholinesterase and carboxylesterase inhibitorsAlkyl 2-arylhydrazinylidene-3-oxo-3-polyfluoroalkylpropionates as new effective and selective inhibitors of carboxylesteraseOn quantum mechanical – molecular mechanical (QM/MM) approaches to model hydrolysis of acetylcholine by acetylcholinesteraseConjugates of methylene blue with γ-carboline derivatives as new multifunctional agents for the treatment of neurodegenerative diseases
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Q27704207-2B48AE8E-E64C-438B-99AD-C9FC8863D893Q33619462-16F3EF6E-B774-4D0B-A7AC-531AD35F1DF7Q33940451-D9BE4B7C-5DEC-4DA0-B750-BED849DC325EQ35869485-3FFDC1A4-2382-47C0-8E11-F624C4FF5F03Q36273566-0AEF98B6-5C93-4738-9470-4166133A6826Q38732174-F350F415-C6E6-414F-A6D5-BD87985F184FQ38742996-14A0976A-E08F-45D2-B6D1-30C75B561B31Q38746015-14821398-9199-40A9-BD7A-775C4C2792FDQ40240109-498E8167-7D10-4FBA-B10A-D229D31E568EQ42293352-29A9E8CE-39E7-4840-A4F2-4A0A2A372536Q42690258-FA649EBE-BAD3-4035-A944-1C0D185873EDQ43096157-287CC431-7472-4406-9AC5-E3481659E2D3Q43926105-348582A6-D44B-4658-B186-EBF91CF959A0Q43952669-410EC6E9-AABE-4974-B0FC-DD6C3B2D7E42Q44649652-6AC4F698-73BF-4C03-BF06-4B1CAC7F2754Q44953963-7D52A429-FD05-4CC5-9DD8-88DB91F616ECQ46699211-F50A8255-C6E9-41D6-BCDA-B735EC905E27Q47704916-D6483A3E-2BE2-465A-B33C-9D9DBE916038Q47754184-ADF2B55D-7C5B-4227-988E-69E14E713568Q48761651-4E2273FE-8EA9-4D9F-BB5E-8D9CF8F86C8BQ49550481-96F6A881-0D7D-4514-B909-D74641BFE340Q49579654-2223034C-91F0-4371-A4B5-455338ED71A0Q50545970-5582C472-9DEC-4620-90E9-FC08C09EDD21Q50705887-7EDF82C6-BEF7-4A8D-A745-4D7AFFC7864BQ51140938-8270D8CB-6E77-47D1-94A6-C2C9BFED3F32Q51625830-8A7124B5-25B4-46FC-A4F6-58BA928C6BAEQ51631340-74EFC1EF-DC33-4C15-A776-2EF64A7EFB24Q51758680-73B50AA1-E0BA-4887-9D3A-A155744A880CQ52666034-1CEE4FA5-09DF-4127-8D7B-69ED1AF0E64FQ52670346-6EFE301E-571A-4687-8CA2-D7D9498CB160Q52874436-E6D9D852-416E-48C7-B58E-A77282441FB2Q54483424-54547A86-5919-4F1A-A56B-8B1EFCCADDE2Q58596172-9B78398A-DEA6-4083-8F29-101C2F22FFBBQ60648565-9D0C16F4-B97B-4C30-B051-AC13BC3EEFA1Q60648566-762E25EF-C6FF-4270-B787-6547E6A5EE16Q60648567-FEE1ABBB-03FB-4994-A813-CBDBB84594B5Q60648594-F95B8E1C-64AB-4B28-A995-1EB6DB3B2D22Q60648595-0A7F8304-0DBD-4309-9D8F-4D869386CF96Q60648607-81E12EDE-9A33-40F8-8C34-965BE562F065Q64077918-F1FD6297-D472-48AB-95D8-AED6092E9306
P50
description
hulumtuese
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
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name
Sofya V Lushchekina
@bar
Sofya V Lushchekina
@de
Sofya V Lushchekina
@fr
Sofya V Lushchekina
@sl
Sofya V. Lushchekina
@en
Sofya V. Lushchekina
@es
Sofya V. Lushchekina
@nl
type
label
Sofya V Lushchekina
@bar
Sofya V Lushchekina
@de
Sofya V Lushchekina
@fr
Sofya V Lushchekina
@sl
Sofya V. Lushchekina
@en
Sofya V. Lushchekina
@es
Sofya V. Lushchekina
@nl
altLabel
Sofia Luschekina
@en
Sofia Lushchekina
@en
Sofia V. Luschekina
@en
Sofia V. Lushchekina
@en
Sofia Vladimirovna Luschekina
@en
Sofia Vladimirovna Lushchekina
@en
Sofya Luschekina
@en
Sofya V. Luschekina
@en
Sofya V. Lushchekina
@en
Sofya Vladimirovna Luschekina
@en
prefLabel
Sofya V Lushchekina
@bar
Sofya V Lushchekina
@de
Sofya V Lushchekina
@fr
Sofya V Lushchekina
@sl
Sofya V. Lushchekina
@en
Sofya V. Lushchekina
@es
Sofya V. Lushchekina
@nl
P1053
F-8469-2010
P106
P1153
17345987500
P21
P31
P3829
P496
0000-0002-6922-020X