Search Results - "Arseniev, A.S"

Towards universal approach for bacterial production of three-finger Ly6/uPAR proteins: Case study of cytotoxin I from cobra N. oxiana by Shulepko, M.A., Lyukmanova, E.N., Shenkarev, Z.O., Dubovskii, P.V., Astapova, M.V., Feofanov, A.V., Arseniev, A.S., Utkin, Y.N., Kirpichnikov, M.P., Dolgikh, D.A.

“…Cytotoxins or cardiotoxins is a group of polycationic toxins from cobra venom belonging to the ‘three-finger’ protein superfamily (Ly6/uPAR family) which…”
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NMR studies of Brownian tumbling and internal motions in proteins by Korzhnev, D.M., Billeter, M., Arseniev, A.S., Orekhov, V.Y.

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Spatial Structure of Zervamicin IIB Bound to DPC Micelles: Implications for Voltage-Gating by Shenkarev, Z.O., Balashova, T.A., Efremov, R.G., Yakimenko, Z.A., Ovchinnikova, T.V., Raap, J., Arseniev, A.S.

“…Zervamicin IIB is a 16-amino acid peptaibol that forms voltage-dependent ion channels with multilevel conductance states in planar lipid bilayers and vesicular…”
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Expression, purification and characterization of SORCS2 intracellular domain for structural studies by Artemieva, L.E., Mineev, K.S., Arseniev, A.S., Goncharuk, S.A.

“…Neurotrophin signaling pathways are one of the major cascades in neuronal development and involved in many key processes including proliferation,…”
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Lipid–protein nanodiscs for cell-free production of integral membrane proteins in a soluble and folded state: Comparison with detergent micelles, bicelles and liposomes by Lyukmanova, E.N., Shenkarev, Z.O., Khabibullina, N.F., Kopeina, G.S., Shulepko, M.A., Paramonov, A.S., Mineev, K.S., Tikhonov, R.V., Shingarova, L.N., Petrovskaya, L.E., Dolgikh, D.A., Arseniev, A.S., Kirpichnikov, M.P.

“…Production of integral membrane proteins (IMPs) in a folded state is a key prerequisite for their functional and structural studies. In cell-free (CF)…”
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Probing the effect of membrane contents on transmembrane protein-protein interaction using solution NMR and computer simulations by Bragin, P.E., Kuznetsov, A.S., Bocharova, O.V., Volynsky, P.E., Arseniev, A.S., Efremov, R.G., Mineev, K.S.

“…The interaction between the secondary structure elements is the key process, determining the spatial structure and activity of a membrane protein…”
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Medicinal leech antimicrobial peptides lacking toxicity represent a promising alternative strategy to combat antibiotic-resistant pathogens by Grafskaia, E.N., Nadezhdin, K.D., Talyzina, I.A., Polina, N.F., Podgorny, O.V., Pavlova, E.R., Bashkirov, P.V., Kharlampieva, D.D., Bobrovsky, P.A., Latsis, I.A., Manuvera, V.A., Babenko, V.V., Trukhan, V.M., Arseniev, A.S., Klinov, D.V., Lazarev, V.N.

“…The rise of antibiotic resistance has necessitated the development of alternative strategies for the treatment of infectious diseases. Antimicrobial peptides…”
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NMR investigation of the isolated second voltage-sensing domain of human Nav1.4 channel by Paramonov, A.S., Lyukmanova, E.N., Myshkin, M.Yu, Shulepko, M.A., Kulbatskii, D.S., Petrosian, N.S., Chugunov, A.O., Dolgikh, D.A., Kirpichnikov, M.P., Arseniev, A.S., Shenkarev, Z.O.

“…Voltage-gated Na+ channels are essential for the functioning of cardiovascular, muscular, and nervous systems. The α-subunit of eukaryotic Na+ channel consists…”
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Spatial structure and dimer–monomer equilibrium of the ErbB3 transmembrane domain in DPC micelles by Mineev, K.S., Khabibullina, N.F., Lyukmanova, E.N., Dolgikh, D.A., Kirpichnikov, M.P., Arseniev, A.S.

“…In present work the interaction of two TM α-helices of the ErbB3 receptor tyrosine kinase from the ErbB or HER family (residues 639–670) was studied by means…”
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Isolation and structure analysis of components from venom of the spider Argiope lobata by Grishin, E V, Volkova, T M, Arseniev, A S

“…Homologous low molecular weight compounds, blocking postsynaptic glutamate receptors, were isolated from the venom of the spider Argiope lobata by ion exchange…”
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Bacterial and cell-free production of APP671-726 containing amyloid precursor protein transmembrane and metal-binding domains by Bocharova, O. V., Urban, A. S., Nadezhdin, K. D., Bocharov, E. V., Arseniev, A. S.

“…More than half of the mutations associated with familiar Alzheimer’s disease have been found in the transmembrane domain of amyloid precursor protein (APP)…”
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Structural and dynamic study of the transmembrane domain of the amyloid precursor protein by Nadezhdin, K D, Bocharova, O V, Bocharov, E V, Arseniev, A S

“…Alzheimer's disease affects people all over the world, regardless of nationality, gender or social status. An adequate study of the disease requires essential…”
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Expression of G-protein coupled receptors in Escherichia coli for structural studies by Petrovskaya, L. E., Shulga, A. A., Bocharova, O. V., Ermolyuk, Ya. S., Kryukova, E. A., Chupin, V. V., Blommers, M. J. J., Arseniev, A. S., Kirpichnikov, M. P.

“…To elaborate a high-performance system for expression of genes of G-protein coupled receptors (GPCR), methods of direct and hybrid expression of 17 GPCR genes…”
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1H‐NMR study of gramicidin A transmembrane ion channel by Arseniev, A.S., Barsukov, I.L., Bystrov, V.F., Lomize, A.L., Ovchinnikov, Yu.A.

“…The structure of[Val1]gramicidin A incorporated into sodium dodecyl‐d 25 sulphate micelles has been studied by two‐dimensional proton NMR spectroscopy…”
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Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments by Mineev, K S, Bocharov, E V, Volynsky, P E, Goncharuk, M V, Tkach, E N, Ermolyuk, Ya S, Schulga, A A, Chupin, V V, Maslennikov, I V, Efremov, R G, Arseniev, A S

“…Specific interactions between transmembrane α-helices, to a large extent, determine the biological function of integral membrane proteins upon normal…”
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N-terminal fusion tags for effective production of g-protein-coupled receptors in bacterial cell-free systems by Lyukmanova, E N, Shenkarev, Z O, Khabibullina, N F, Kulbatskiy, D S, Shulepko, M A, Petrovskaya, L E, Arseniev, A S, Dolgikh, D A, Kirpichnikov, M P

“…G-protein-coupled receptors (GPCR) constitute one of the biggest families of membrane proteins. In spite of the fact that they are highly relevant to pharmacy,…”
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Bacterial Synthesis and Purification of Normal and Mutant Forms of Human FGFR3 Transmembrane Segment by Goncharuk, S A, Goncharuk, M V, Mayzel, M L, Lesovoy, D M, Chupin, V V, Bocharov, E V, Arseniev, A S, Kirpichnikov, M P

“…The fibroblast growth factor receptor 3 (FGFR3) is a protein belonging to the family of receptor tyrosine kinases. FGFR3 plays an important role in human…”
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Peptaibol Zervamicin IIB Structure and Dynamics Refinement from Transhydrogen Bond J Couplings by Shenkarev, Z.O., Balashova, T.A., Yakimenko, Z.A., Ovchinnikova, T.V., Arseniev, A.S.

“…Zervamicin IIB (Zrv-IIB) is a channel-forming peptaibol antibiotic of fungal origin. The measured transhydrogen bond 3h J NC′ couplings in methanol solution…”
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NMR structure of the channel-former zervamicin IIB in isotropic solvents by Balashova, T.A., Shenkarev, Z.O., Tagaev, A.A., Ovchinnikova, T.V., Raap, J., Arseniev, A.S.

“…Spatial structure of the membrane channel-forming hexadecapeptide, zervamicin IIB, was studied by NMR spectroscopy in mixed solvents of different polarity…”
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Cell-free Production of the Extracellular Domain of the Nicotinic Acetylcholine Receptor by Lyukmanova, E N, Kopeina, G S, Shulepko, M A, Shenkarev, Z O, Arseniev, A S, Dolgikh, D A, Kirpichnikov, M P

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