Публикации

2019 год:

1. Boyko, K.M., et al. 3D structure of the natural tetrameric form of human butyrylcholinesterase as revealed by cryoEM, SAXS and MD / K.M. Boyko, T.N. Baymukhametov, Y.M. Chesnokov et al. // Biochimie. - 2019. - Vol. 156. - P. 196–205.
2. Kangur, L., et al. Structural stability of human butyrylcholinesterase under high hydrostatic pressure / L. Kangur, K. Timpmann, D. Zeller et al. // Biochim. Biophys. Acta - Proteins Proteomics. - 2019. - Vol. 1867, № 2. - P. 107–113.
3. Nurullin, L.F., et al. Reorganization of Septins Modulates Synaptic Transmission at Neuromuscular Junctions / L.F. Nurullin, V.F. Khuzakhmetova, E.F. Khaziev et al. // Neuroscience. - 2019. - Vol. 404. - P. 91–101.
4. Lenina, O.A., et al. Blockade of Metabotropic GABA-B Receptors as an Approach to Reduce Toxic Peripheral Effects of Cholinesterase Inhibitors / O.A. Lenina, P. Masson, K.A. Petrov // Bionanoscience. - 2019. - Vol. 9, № 1. - P. 38–43.
5. Kovyazina, I. V., et al. Depression of the Evoked Quantal Acetylcholine Secretion in Frog Neuromuscular Junction by Phospholipases A2 from the Venom of Steppe Viper Vipera ursiniirenardi / I. V. Kovyazina, N. V. Kopylova, Y.N. Utkin et al. // Biochem. (Moscow), Suppl. Ser. A Membr. Cell Biol. - 2019. - Vol. 13, № 1. - P. 78–84.
6. Kuznetsov, M.S., et al. Bioinformatic Analysis of the Sciatic Nerve Trans­criptomes of Mice after 30-Day Spaceflight on Board the Bion-M1 Biosatellite / M.S. Kuznetsov, P.N. Rezvyakov, A.N. Lisyukov et al. // Russ. J. Genet. - 2019. - Vol. 55, № 3. - P. 388–392.
7. Khuzakhmetova, V., et al. Prenatal hyperhomocysteinemia induces oxidative stress and accelerates “aging” of mammalian neuromuscular synapses / V. Khuzakhmetova, O. Yakovleva, S. Dmitrieva et al. // Int. J. Dev. Neurosci. - 2019. - Vol. 75. - P. 1–12.
8. Goličnik, M., et al. Time-course of enzyme-catalyzed competing substrate degradation for michaelian behavior and for enzymes showing activation/inhibition by excess substrate / M. Goličnik, P. Masson // Chem. Biol. Interact. - 2019. - Vol. 309
9. Mukhametgalieva, A.R., et al. Time course of human cholinesterases-catalyzed competing substrate kinetics / A.R. Mukhametgalieva, A.R. Aglyamova, S. V. Lushchekina et al. // Chem. Biol. Interact. - 2019. -
10. Fedorenko, S., et al. Fluorescent magnetic nanoparticles for modulating the level of intracellular Ca2+ in motoneurons / S. Fedorenko, A. Stepanov, G. Sibgatullina et al. // Nanoscale. - 2019. -
11. Malomouzh, A., et al. Components of the GABAergic signaling in the peripheral cholinergic synapses of vertebrates: a review / A. Malomouzh, V. Ilyin, E. Nikolsky // Amino Acids. - 2019. - Vol. 51, № 8. - P. 1093–1102.
12. Tsentsevitsky, A.N., et al. Diverse Effects of Noradrenaline and Adrenaline on the Quantal Secretion of Acetylcholine at the Mouse Neuromuscular Junction / A.N. Tsentsevitsky, I. V. Kovyazina, E.A. Bukharaeva // Neuroscience. - 2019. - Vol. 423. - P. 162–171.
13. Diuba, A. V., et al. CLARITY analysis of the Cl/pH sensor expression in the brain of transgenic mice / A. V. Diuba, D. V. Samigullin, A. Kaszas et al. // Neuroscience. - 2019. 

2018 год:

1. Mukhametshina AR  , Fedorenko SV  , Petrov AM , Zakyrjanova GF , Petrov KA  , Nurullin LF  , Nizameev IR  , Mustafina AR  , Sinyashin OG  . Targeted Nanoparticles for Selective Marking of Neuromuscular Junctions and ex Vivo Monitoring of Endogenous Acetylcholine Hydrolysis. ACS Appl Mater Interfaces. 2018 May 2;10(17):14948-14955.
2. Nurullin LF , Nikolsky EE , Malomouzh AI Elements of molecular machinery of GABAergic signaling in the vertebrate cholinergic neuromuscular junction. Acta Histochem. 2018 Apr;120(3):298-301. doi: 10.1016/j.acthis.2018.02.003. Epub 2018 Feb 26.
3. Petrov K, Zueva I, Kovyazina I, Sedov I, Lushchekina S, Kharlamova A, Lenina O, Koshkin S, Shtyrlin Y, Nikolsky E, Masson P. C-547, a 6-methyluracil derivative with long-lasting binding and rebinding on acetylcholinesterase: Pharmacokinetic and pharmacodynamic studies. Neuropharmacology. 2018 Mar 15;131:304-315.
4. Petrov К,  Kharlamova А, Lenina О, Nurtdinov А, Sitdykova М, Ilyin  V, Zueva I, Nikolsky E. Specific inhibition of acetylcholinesterase as an approach to decrease muscarinic side effects during myasthenia gravis treatment Scientific RepoRts   2018,  8:304 | DOI:10.1038/s41598-017-18307-9
5. Ковязина И.В., Копылова Н.В., Уткин Ю.Н., Бухараева Е.А., Никольский Е.Е., Вульфиус Е.А. Угнетение вызванной секреции ацетилхолина в нервно-мышечном синапсе лягушки фосфолипазами а2 из яда степной гадюки vipera ursinii renardi. Биологические мембраны,  2018, том 35,  № 1,  с.  71–78
6. Ларионов И.А., Ларионов А.Л., Никольский Е.Е. Могут ли силы ампера быть фактором латеральной подвижности ионных каналов?  математическое моделирование.  Биологические мембраны,  2018, том 35,  № 1,  с.  3–15
7. Маломуж А.И., Никольский Е.Е. Современные представления о холинергической нейротрансмиссии в моторных синапсах,  Биологические мембраны,  2018, том 35,  № 3,  с.  169–185
8. Khaziev EF, Samigullin DV, Tsentsevitsky AN, Bukharaeva EA, Nikolsky EE ATP Reduces the Entry of Calcium Ions into the Nerve Ending by Blocking L-type Calcium Channels, Acta Naturae, 2018 Apr-Jun;10(2):93-96.
9. Samigullin, D.V., Zhilyakov, N.V., Khaziev, E.F. Bukharaeva, EA, Nikolsky, EE. Calcium Transient and Quantal Release in Mouse Neuromuscular Junction Under Extracellular Calcium Concentration Change BioNanoSci. (2018). https://doi.org/10.1007/s12668-018-0558-8
10. Petrov KA, Nikolsky EE, Masson P,  Autoregulation of Acetylcholine Release and Micro-Pharmacodynamic Mechanisms at Neuromuscular Junction: Selective Acetylcholinesterase Inhibitors for Therapy of Myasthenic Syndromes. Front Pharmacol. 2018 Jul 12;9:766. doi: 10.3389/fphar.2018.00766. eCollection 2018.
11. Mukhametshina A, Petrov A, Fedorenko S, Petrov K, Nizameev I, Mustafina A, Sinyashin O Luminescent nanoparticles for rapid monitoring of endogenous acetylcholine release in mice atria. Luminescence. 2018 May;33(3):588-593. doi: 10.1002/bio.3450. Epub 2018 Jan 29
12. Жиляков Н.В. , Хазиев Э.Ф., Латфуллин  А.Р., Маломуж А.И. , Бухараева Э.А., Никольский Е.Е. Самигуллин Д.В.  Изменения уровня кальция в моторном нервном окончании мыши при активации метаботропных холинорецепторов и рецепторов гамк, Российский физиологический журнал им. И. М. Сеченова  т104  № 6,  2018, 640-646  doi: 10.7868/s0869813918060047
13. Petrov KA, Nikolsky EE, Masson P. Autoregulation of Acetylcholine Release and Micro-Pharmacodynamic Mechanisms at Neuromuscular Junction: Selective Acetylcholinesterase Inhibitors for Therapy of Myasthenic Syndromes. Front Pharmacol. 2018 Jul 12;9:766. doi: 10.3389/fphar.2018.00766. eCollection 2018
14. Lushchekina S.V., Schopfer L.M., Grigorenko B.L., Nemukhin A.V., Varfolomeev S.D., Lockridge O., Masson P., “Optimization of Cholinesterase-Based Catalytic Bioscavengers Against Organophosphorus Agents”, Frontiers in Pharmacology (IF=3.931), 2018, 9, 211(1-13). DOI: 10.3389/fphar.2018.00211
15. Zueva I.V., Lushchekina S.V., Masson P., “Water structure changes in oxime-mediated reactivation process of phosphorylated human acetylcholinesterase”, Bioscience Reports (IF=2.899), 2018, 38(3), BSR20180609(1-10). DOI: 10.1042/BSR20180609.
16. Lushchekina S.V., Masson P., “Catalytic bioscavengers against organophosphorus agents: mechanistic issues of self-reactivating cholinesterases”, Toxicology (IF=3.265), 2018, 409, 91-102.  DOI: 10.1016/j.tox.2018.07.020

2017  год:

1. Tsentsevitsky A.N., Kovyazina I.V., Nurullin L.F., Nikolsky E.E.      Muscarinic cholinoreceptors (M1-, M2-, M3- and M4-type) modulate the acetylcholine secretion in the frog neuromuscular junction. Neuroscience Letters. IF 2,18
2. Nurullin L., Tyapkina O., Malomouzh A.  Adrenoceptors at the Frog Neuromuscular Junction: an Immunohistochemical Study. BioNanoScience.
3. Khaziev E., Bukharaeva E., Nikolsky E., Samigullin D.         Contribution of Ryanodine Receptors in Forming Presynaptic Ca2+ Level and Cholinergic Modulation in Response to Single Potential in Frog Neuromuscular Junction. BioNanoScience.
4. Ayupov R., Petrov K.A., Masson P.           Computational Exploration of Reactivity of 6-Methyluracil/Imidazole-2-Carbaldehyde Oxime Conjugate. BioNanoScience.
5. Samigullin D.V., Khaziev E.F., Zhilyakov N.V., Bukharaeva E.A., Nikolsky E.E.         Calcium Transient Registration in Response to Single Stimulation and During Train of Pulses in Mouse Neuromuscular Junction. BioNanoScience.
6. Khaziev E., Golovyahina A., Bukharaeva E., Nikolsky E., Samigullin D.        Action of ATP on Ca2+-Transient in Different Parts of the Frog Motor Nerve Ending. BioNanoScience
7. Petrov K.A., Masson P.  Role of Acetylcholinesterase in β-Amyloid Aggregation Studied by Accelerated Molecular Dynamics. BioNanoScience.
8. Masson P.           Cholinesterase reactivators and bioscavengers for pre- and post-exposure treatments of organophosphorus poisoning. Journal of Neurochemistry. IF 4,083
9. Petrov K.A., Masson P.  Nanoparticle-Delivered 2-PAM for Rat Brain Protection against Paraoxon Central Toxicity. ACS Applied Materials and Interfaces. IF 7,504
10. Samigullin D.V., Khaziev E.F., Zhilyakov N.V., Bukharaeva E.A., Nikolsky E.E.         Loading a calcium dye into frog nerve endings through the nerve stump: Calcium transient registration in the frog neuromuscular junction. Journal of Visualized Experiments. IF 1,232
11. Masson, P           The C5 Variant of the Butyrylcholinesterase Tetramer Includes a Noncovalently Bound 60 kDa Lamellipodin Fragment. MOLECULES. IF 2,861
12. Nikolsky, E; Masson, P   Slow-binding inhibition of acetylcholinesterase by an alkylammonium derivative of 6-methyluracil: molecular modeling, X-ray crystallography and kinetic study of the inhibition mechanism. JOURNAL OF NEUROCHEMISTRY. IF 4,083

2016  год:

1. Elistratova , J. Sensing Activity of Cholinesterases through Luminescence Response of Hexarhenium Cluster Complex [{Re6S8}(OH)6]4–/ J. Elistratova, A. Mustafina, K. Brylev, K.A. Petrov, M.A. Shestopalov, Y.V. Mironov, V. Babaev, I.K. Rizvanov, P. Masson, O.G. Sinyashin // The Analyst. – 2016. -V 141. – P. 4204-4210 DOI: 10.1039/c6an00581k
2. Gazizova G., Kozlova O., Tyapkina O., Nurullin L., Shagimardanova E. Semaphorins Are likely to Be Involved in the Control of Hibernation // BioNanoScience. 2016. doi:10.1007/s12668-016-0292-z.
3. Islamov R.R., Gusev О.А., Tanabe A., Terada M., Tyapkina O.V., Petrov K.A., Rizvanov А.А., Kozlovskaya I.B., Nikolskiy E.E., Grigorjev A.I. Full-genome study of gene expression in lumbar spinal cord of miceafter30-dayspace flight on Bion-M1biosatellite // Acta Astronautica. 2016. V. 122. P. 231–236.
4. Jacquet, P. Current and emerging strategies for organophosphate decontamination: special focus on hyperstable enzymes / P. Jacquet, D. Daudé, J. Bzdrenga, P. Masson, M. Elias, E. Chabrière // Environmental Science and Pollution Research. – 2016. - V23.- №9. – P.8200-8218. DOI: 10.1007/s11356-016-6143-1. ISSN: 09441344 
5. Khaziev E, Golovyahina A., Bukharaeva E, Nikolsky E, Samigullin D.Action of ATP on Ca2+-transient in different parts of the frog motor nerve ending. // BioNanoScience. 2016. doi: 10.1007/s12668-016-0350-6
6. Khaziev E, Bukharaeva E, Nikolsky E, Samigullin D.Contribution of Ryanodine Receptors in Forming Presynaptic Ca2+ Level and Cholinergic Modulation in Response to Single Potential in Frog Neuromuscular Junction// BioNanoScience. 2016. doi:: 10.1007/s12668-016-0308-8
7. Khaziev E, Samigullin D, Zhilyakov N, Fatikhov N, Bukharaeva E, Verkhratsky A and Nikolsky E (2016). Acetylcholine-induced inhibition of presynaptic calcium signals and transmitter release in the frog neuromuscular junction. Front. Physiol. 7:621. doi: 10.3389/fphys.2016.00621
8. Kharlamova AD, Lushchekina SV, Petrov KA, Kots ED, Nachon F, Villard-Wandhammer M, Zueva IV, Krejci E, Reznik VS, Zobov VV, Nikolsky EE, Masson P. Slow-binding inhibition of acetylcholinesterase by an alkylammonium derivative of 6-methyluracil: mechanism and possible advantages for myasthenia gravis treatment.// Biochemical Journal. 2016.  V. 473, № 9. P. 1225-1236. doi: 10.1042/BCJ20160084.
9. Khuzakhmetova V, Nurullin L, Bukharaeva E Cytoskeletal Protein Septins Participate in the Modulation of the Kinetics of Acetylcholine Quanta Release at Neuromuscular Junction // BioNanoScience.  2016. V. 6, № 3 , P. 249–251.DOI 10.1007/s12668-016-0217-x
10. Lushchekina, S. Understanding the non-catalytic behavior of human butyrylcholinesterase silent variants: comparison of wild-type enzyme, catalytically active Ala328Cys mutant, and silent Ala328Asp variant / S. Lushchekina, A. Nemukhin, S. Varfolomeev, P. Masson // Chem.-Biol. Interact.- 2016. - Apr 7.-  pii: S0009-2797(16)30121-1, DOI: 10.1016/j.cbi.2016.04.007 , ISSN: 00092797
11. Masson, P. Slow-binding inhibition of cholinesterases, pharmacological and toxicological relevance / P. Masson,  S.V. Lushchekina // Arch. Biochem. Biophys.- 2016.- V. 593 . – P.60-68., DOI: 10.1016/j.abb.2016.02.010., ISSN: 00039861
12. Masson, P. Emergence of catalytic bioscavengers against organophosphorus agents / P. Masson, S.V. Lushchekina //, Chem.-Biol. Interact. – 2016. - Feb 17.-  pii: S0009-2797(16)30046-1.
13. Mukhametshina, A.R.  Luminescent silica nanoparticles for sensing acetylcholinesterase-catalyzed hydrolysis of acetylcholine / A.R. Mukhametshina, S.V. Fedorenko, I.V. Zueva, K.A. Petrov, P. Masson, I.R. Nizameev, A.R. Mustafina, O.G. Sinyashin, //  Biosens. Bioelectron. – 2016.-  V77.- P. 871-878. DOI: 10.1016/j.bios.2015.10.059., ISSN: 09565663
14. Nurullin L., Tyapkina O., Malomouzh A.I. Adrenoceptors at the Frog Neuromuscular Junction: an Immunohistochemical Study. // BioNanoScience. 2016. doi: 10.1007/s12668-016-0319-5. 
15. Peters, J. Dynamics of human acetylcholinesterase bound to non-covalent and covalent inhibitors shedding light on changes to the water network structure / J. Peters, N. Martinez, M. Trovaslet, K. Scannapieco, M.M. Koza, P. Masson, F. Nachon // Phys. Chem. Chem. Phys. – 2016. - V18. -№ 18.- P. 12992-13001. DOI: 10.1039/c6cp00280c., ISSN: 14639076
16. Povysheva T.V., Rezvyakov P.N., Shaimardanova G.F., Nikolskii E.E., Islamov R.R., Chelyshev Y.A., Grygoryev A.I., Myelinated fibers of the mouse spinal cord after a 30-day space flight, Doklady Biological Sciences
17. Samigullin D.,Khaziev E, Zhilyakov N, Sudakov I, Bukharaeva E., Nikolsky E. Calcium transient registration in response to single stimulation and during train of pulses in mouse neuromuscular junction.// .BioNanoScience, doi:: 10.1007/s12668-016-0318-6
18. Strelnik AD, Petukhov AS, Zueva IV, Zobov VV, Petrov KA, Nikolsky EE, Balakin KV, Bachurin SO, Shtyrlin YG. Novel potent pyridoxine-based inhibitors of AChE and BChE, structural analogs of pyridostigmine, with improved in vivo safety profile.// Bioorganic & Medicinal Chemistry Letters. 2016. V. 26, № 16. P. 4092-4094. doi: 10.1016/j.bmcl.2016.06.070.
19. Shakirzyanova A, Valeeva G, Giniatullin A, Naumenko N, Fulle S, Akulov A, Atalay M, Nikolsky E, Giniatullin R. Age-dependent action of reactive oxygen species on transmitter release in mammalian neuromuscular junctions. // Neurobiology of Aging.  2016.  V.38. P. 73-81. doi: 10.1016/j.neurobiolaging.
20. Tsentsevitsky A, Nurullin L, Nikolsky E, Malomouzh A. Metabotropic and ionotropic glutamate receptors mediate the modulation of acetylcholine release at the frog neuromuscular junction.// Journal Neuroscience Research. 2016. Oct 22. doi: 10.1002/jnr.23977.

2015 год:

1. Tokhtaeva E. Septin dynamics are essential for exocytosis / Tokhtaeva E., Capri J., Marcus E.A., Whitelegge J.P., Khuzakhmetova V., Bukharaeva E., Deiss-Yehiely N., Dada L.A., Sachs G., Fernandez-Salas E., Vagin O. // Journal of Biological Chemistry.-2015.-V. 290.-P.5280-5297.
2.    Marion J. Pressure-induced molten globule state of human acetylcholinesterase: Structural and dynamical changes monitored by neutron scattering / Marion J., Trovaslet M., Martinez N., Masson P., Schweins R., Nachon F., Trapp M., Peters J. //  Physical Chemistry Chemical Physics.-2015.-V.17.-P.3157-3163.
3. Saveliev A. Bayesian analysis of the kinetics of quantal transmitter secretion at the neuromuscular junction. / Saveliev A., Khuzakhmetova V., Samigullin D., Skorinkin A., Kovyazina I., Nikolsky E., Bukharaeva E. // Journal Computational Neuroscience.-2015.-V.39.- P.119-129.
4. Samigullin D. Estimation of presynaptic calcium currents and endogenous calcium buffers at the frog neuromuscular junction with two different calcium fluorescent dyes. / Samigullin D, Fatikhov N, Khaziev E, Skorinkin A, Nikolsky E, Bukharaeva E. // Frontiers in Synaptic Neuroscience.-2015.-V.6.-Р.1-10.
5. Semenov V.E. 6-Methyluracil derivatives as bifunctional acetylcholinesterase inhibitors for the treatment of Alzheimer's Disease. / Semenov V.E., Zueva I.V., Mukhamedyarov M.A., Lushchekina S.V., Kharlamova A.D., Petukhova E.O., Mikhailov A.S., Podyachev S.N., Saifina L.F., Petrov K.A., Minnekhanova O.A., Zobov V.V., Nikolsky E.E., Masson P., Reznik V.S. // ChemMedChem.-2015.-V.10.-P.1863-1874.
6. Terekhov S. 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. Jr., Ponomarenko N., Blackburn G.M., Masson P., Gabibov A. // Biochimie.-2015.-V.118.-P.51-59.
7. Malomouzh A.I. Metabotropic GABAB receptors mediate GABA inhibition of acetylcholine release in the rat neuromuscular junction. /  Malomouzh A.I., Petrov K.A., Nurullin L.F., Nikolsky E.E. // J. Neurochem.-2015.-Sep 25. doi: 10.1111/jnc.13373.
8. Исламов Р.Р. Синтез мембранного белка слияния синаптических везикул snap25 в двигательном нервном окончании мыши. / Исламов Р.Р., Самигуллин Д.В., Ризванов А.А, Бондаренко Н.И., Никольский Е.Е. // Доклады Академии наук.-2015.-Т.464.-№1.-С.108–110.
9. Маломуж А.И. Иммуногистохимическое доказательство наличия метаботропных рецепторов к гамма-аминомасляной кислоте в нервно-мышечных синапсах крысы. / Маломуж А.И., Нуруллин Л.Ф., Никольский Е.Е. // Доклады академии наук.-2015.-Т.463.-№4.-С.483–486.
10. Ковязина И.В. Идентификация подтипов М-холинорецепторов, участвующих в ауторегуляции освобождения квантов медиатора из двигательных нервных окончаний. / Ковязина И.В., Ценцевицкий А.Н., Никольский Е.Е. // Доклады Академии наук.-2015.-Т.460.-№3.-С.356–358.
11. Выштакалюк А.Б. Влияние лекарственного препарата «Ксимедон» на восстановление печени крыс при токсическом повреждении четыреххлористым углеродом / А.Б. Выштакалюк, Н.Г. Назаров, А.Г. Порфирьев, И.В. Зуева, О.А. Миннеханова, О.В. Маятина, В.С. Резник, В.В. Зобов, Е.Е. Никольский // Доклады Академии наук.-2015.–Т.462.-№1.-С.103-106.
12. Ценцевицкий А.Н. Особенности кальциевой регуляции кинетики секреции медиатора в нервно-мышечных синапсах холоднокровных и теплокровных. / Ценцевицкий А.Н., Хузахметова В.Ф., Васин А.Л., Самигуллин Д.В., Бухараева Э.А. // Биологические мембраны.-2015.-Т.32.-№5–6.-C.310-318.
13. Бухараева Э.А. Синхронное и асинхронное освобождение квантов медиатора в синаптическом контакте. / Бухараева Э.А. // Биологические мембраны.-2015.-Т.32.-№5–6.-С.302-309.