Home
→
Browsing by Subject

Browsing by Subject "Butyrylcholinesterase"

Now showing items 1-19 of 19

3D structure of the natural tetrameric form of human butyrylcholinesterase as revealed by cryoEM, SAXS and MD

Boyko K.; Baymukhametov T.; Chesnokov Y.; Hons M.; Lushchekina S.; Konarev P.; Lipkin A.; Vasiliev A.; Masson P.; Popov V.; Kovalchuk M. (2019)

© 2018 The Authors Human plasma butyrylcholinesterase (BChE) is an endogenous bioscavenger that hydrolyzes numerous medicamentous and poisonous esters and scavenges potent organophosphorus nerve agents. BChE is thus a ...
A new sensitive spectrofluorimetric method for measurement of activity and kinetic study of cholinesterases

Mukhametgalieva A.R.; Zueva I.V.; Aglyamova A.R.; Lushchekina S.V.; Masson P. (2020)

© 2019 Elsevier B.V. A new spectrofluorimetric method more sensitive than the Ellman method was developed for determination of both acetylcholinesterase and butyrylcholinesterase activity and for kinetic analysis of these ...
A novel expression cassette delivers efficient production of exclusively tetrameric human butyrylcholinesterase with improved pharmacokinetics for protection against organophosphate poisoning

Terekhov S.; Smirnov I.; Bobik T.; Shamborant O.; Zenkova M.; Chernolovskaya E.; Gladkikh D.; Murashev A.; Dyachenko I.; Palikov V.; Palikova Y.; Knorre V.; Belogurov A.; Ponomarenko N.; Blackburn G.; Masson P.; Gabibov A. (2015)

© 2015 Published by Elsevier B.V. Butyrylcholinesterase is a stoichiometric bioscavenger against poisoning by organophosphorus pesticides and nerve agents. The low level of expression and extremely rapid clearance of ...
Analysis of Apparent Catalytic Parameters of Multiple Molecular Forms of Human Plasma Butyrylcholinesterase by Activity Gel-Scanning Following Non-denaturing Electrophoresis

Unknown author (2018)

© 2018, Springer Science+Business Media, LLC, part of Springer Nature. Butyrylcholinesterase (BChE) in human plasma is composed of four molecular forms: C1 (monomer); C2, covalent conjugate between BChE monomer and albumin; ...
Catalytic bioscavengers against organophosphorus agents: mechanistic issues of self-reactivating cholinesterases

Lushchekina S.; Masson P. (2018)

© 2018 Elsevier B.V. Catalytic bioscavengers are the second-generation bioscavengers. These biopharmaceuticals are intended to degrade toxic organophosphorus agents on the skin for decontamination or in the bloodstream for ...
Chemical polysialylation and in vivo tetramerization improve pharmacokinetic characteristics of recombinant human butyrylcholinesterase-based bioscavengers

Terekhov S.; Smirnov I.; Shamborant O.; Bobik T.; Ilyushin D.; Murashev A.; Dyachenko I.; Palikov V.; Knorre V.; Belogurov A.; Ponomarenko N.; Kuzina E.; Genkin D.; Masson P.; Gabibov A. (2015)

© 2015 Park-media, Ltd. Organophosphate toxins (OPs) are the most toxic low-molecular compounds. The extremely potent toxicity of OPs is determined by their specificity toward the nerve system. Human butyrylcholinesterase ...
Chemical polysialylation of recombinant human proteins

Smirnov I.; Vorobiev I.; Belogurov A.; Genkin D.; Deyev S.; Gabibov A. (2015)

© Springer Science+Business Media New York 2015. All right reserved. Design of drug with prolonged therapeutic action is one of the rapid developing fields of modern medical science and required implementation of different ...
Computer-designed active human butyrylcholinesterase double mutant with a new catalytic triad

Grigorenko B.; Novichkova D.; Lushchekina S.; Zueva I.; Schopfer L.; Nemukhin A.; Varfolomeev S.; Lockridge O.; Masson P. (2019)

© 2019 Elsevier B.V. A computer-designed mutant of human butyrylcholinesterase (BChE), N322E/E325G, with a novel catalytic triad was made. The catalytic triad of the wild-type enzyme (S198·H438·E325) was replaced by ...
Excessive labeling technique provides a highly sensitive fluorescent probe for real-time monitoring of biodegradation of biopolymer pharmaceuticals in vivo

Terekhov S.; Smirnov I.; Shamborant O.; Zenkova M.; Chernolovskaya E.; Gladkikh D.; Murashev A.; Dyachenko I.; Knorre V.; Belogurov A.; Ponomarenko N.; Deyev S.; Vlasov V.; Gabibov A. (2014)

© 2014 Park-media, Ltd. Recombinant proteins represent a large sector of the biopharma market. Determination of the main elimination pathways raises the opportunities to significantly increase their half-lives in vivo. ...
Ligands affinity for regulatory sites of human acetylcholesterase and butyrylcholinesterase: A comparative bioinformatic analysis

Mukhametgalieva A.R.; Kozlova A.S.; Akberova N.I.; Fattakhova A.N. (2021)

Cholinesterase inhibitors have been the subject of many studies aimed at developing an effective treatment for various cognitive disorders. Therefore, studying cholinesterases and elucidating the mechanism of their interaction ...
Microfluidic droplet platform for ultrahigh-throughput single-cell screening of biodiversity

Terekhov S.; Smirnov I.; Stepanova A.; Bobik T.; Mokrushina Y.; Ponomarenko N.; Belogurov A.; Rubtsova M.; Kartseva O.; Gomzikova M.; Moskovtsev A.; Bukatin A.; Dubina M.; Kostryukova E.; Babenko V.; Vakhitova M.; Manolov A.; Malakhova M.; Kornienko M.; Tyakht A.; Vanyushkina A.; Ilina E.; Masson P.; Gabibov A.; Altman S. (2017)

© 2017, National Academy of Sciences. All rights reserved.Ultrahigh-throughput screening (uHTS) techniques can identify unique functionality from millions of variants. To mimic the natural selection mechanisms that occur ...
Optimization of cholinesterase-based catalytic bioscavengers against organophosphorus agents

Unknown author (2018)

© 2018 Lushchekina, Schopfer, Grigorenko, Nemukhin, Varfolomeev, Lockridge and Masson. Organophosphorus agents (OPs) are irreversible inhibitors of acetylcholinesterase (AChE). OP poisoning causes major cholinergic syndrome. ...
Purification of recombinant human butyrylcholinesterase on Hupresin®

Lockridge O.; David E.; Schopfer L.; Masson P.; Brazzolotto X.; Nachon F. (2018)

© 2018 Affinity chromatography on procainamide-Sepharose has been an important step in the purification of butyrylcholinesterase (BChE) and acetylcholinesterase (AChE) since its introduction in 1978. The procainamide ...
QM/MM description of newly selected catalytic bioscavengers against organophosphorus compounds revealed reactivation stimulus mediated by histidine residue in the acyl-binding loop

Zlobin A.; Mokrushina Y.; Terekhov S.; Zalevsky A.; Bobik T.; Stepanova A.; Aliseychik M.; Kartseva O.; Panteleev S.; Golovin A.; Belogurov A.; Gabibov A.; Smirnov I. (2018)

© 2018 Zlobin, Mokrushina, Terekhov, Zalevsky, Bobik, Stepanova, Aliseychik, Kartseva, Panteleev, Golovin, Belogurov, Gabibov and Smirnov. Butyrylcholinesterase (BChE) is considered as an efficient stoichiometric antidote ...
Slow-binding inhibition of acetylcholinesterase by an alkylammonium derivative of 6-methyluracil: Mechanism and possible advantages for myasthenia gravis treatment

Kharlamova A.; Lushchekina S.; Petrov K.; Kots E.; Nachon F.; Villard-Wandhammer M.; Zueva I.; Krejci E.; Reznik V.; Zobov V.; Nikolsky E.; Masson P. (2016)

© 2016 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.Inhibition of human AChE (acetylcholinesterase) and BChE (butyrylcholinesterase) by an alkylammonium derivative of 6-methyluracil, ...
Slow-binding inhibition of cholinesterases, pharmacological and toxicological relevance

Masson P.; Lushchekina S. (2016)

© 2016 Elsevier Inc. All rights reserved. Slow-binding inhibition (SBI) of enzymes is characterized by slow establishment of enzyme-inhibitor equilibrium. Cholinesterases (ChEs) display slow onset of inhibition with certain ...
The C5 variant of the butyrylcholinesterase tetramer includes a noncovalently bound 60 kDa lamellipodin fragment

Schopfer L.; Delacour H.; Masson P.; Leroy J.; Krejci E.; Lockridge O. (2017)

© 2017 by the authors. Licensee MDPI. Humans with the C5 genetic variant of butyrylcholinesterase (BChE) have 30–200% higher plasma BChE activity, low body weight, and shorter duration of action of the muscle relaxant ...
The four-helix bundle in cholinesterase dimers: Structural and energetic determinants of stability

Novichkova D.; Lushchekina S.; Dym O.; Masson P.; Silman I.; Sussman J. (2019)

© 2019 Elsevier B.V. The crystal structures of truncated forms of cholinesterases provide good models for assessing the role of non-covalent interactions in dimer assembly in the absence of cross-linking disulfide bonds. ...
Time-course of human cholinesterases-catalyzed competing substrate kinetics

Mukhametgalieva A.; Aglyamova A.; Lushchekina S.; Goličnik M.; Masson P. (2019)

© 2019 Elsevier B.V. Competing substrate kinetic analysis of human butyrylcholinesterase (BChE) and acetylcholinesterase (AChE) from the time-course of enzyme-catalyzed substrate hydrolysis, using spectrophotometric assays ...

Now showing items 1-19 of 19

Search DSpace

Advanced Search

Browse

All of Kazan Federal University Digital Repository

Browsing by Subject "Butyrylcholinesterase"

Browsing by Subject "Butyrylcholinesterase"

Search DSpace

Browse

All of Kazan Federal University Digital Repository

My Account