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Alexander S. Arseniev
Researcher at Russian Academy of Sciences
Publications - 252
Citations - 8004
Alexander S. Arseniev is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: Transmembrane domain & Transmembrane protein. The author has an hindex of 51, co-authored 240 publications receiving 7331 citations. Previous affiliations of Alexander S. Arseniev include Moscow State University & Moscow Institute of Physics and Technology.
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Journal ArticleDOI
Three-dimensional structure of ectatomin from Ectatomma tuberculatum ant venom.
TL;DR: Two-dimensional 1H NMR techniques were used to determine the spatial structure of ectatomin, a toxin from the venom of the ant Ectatomma tuberculatum, and structures were refined by unrestrained energy minimization using the CHARMm program.
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Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state.
Eduard V. Bocharov,Konstantin S. Mineev,Pavel E. Volynsky,Yaroslav S. Ermolyuk,Elena N. Tkach,A.G. Sobol,Vladimir Chupin,Kirpichnikov Mp,Roman G. Efremov,Alexander S. Arseniev +9 more
TL;DR: The spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 embedded into lipid bicelles was obtained by solution NMR, followed by molecular dynamics relaxation in an explicit lipid bilayer, providing an explanation for the pathogenic power of some oncogenic mutations.
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Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy.
TL;DR: The observed conformational exchange behavior of alpha helices seems to be induced by the flickering helix-helix interaction and could be important for the functioning of bacteriorhodopsin.
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Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death trigger.
Eduard V. Bocharov,Yulia Pustovalova,Konstantin V. Pavlov,Pavel E. Volynsky,Marina V. Goncharuk,Yaroslav S. Ermolyuk,Dmitry V. Karpunin,Alexey A. Schulga,Kirpichnikov Mp,Roman G. Efremov,Innokenty V. Maslennikov,Alexander S. Arseniev +11 more
TL;DR: The right-handed parallel helix-helix structure of the transmembrane domain with a hydrogen bond-rich His-Ser node in the middle of the membrane, accessibility of the node for water, and continuous hydrophilic track across the membrane suggest that the domain can provide an ion-conducting pathway through the membrane.
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Spatial Structure of the Transmembrane Domain Heterodimer of ErbB1 and ErbB2 Receptor Tyrosine Kinases
Konstantin S. Mineev,Eduard V. Bocharov,Yulia Pustovalova,Olga V. Bocharova,Vladimir Chupin,Alexander S. Arseniev +5 more
TL;DR: The capability for multiple polar interactions, along with hydrogen bonding between TM segments, correlates with the observed highest affinity of the ErbB1/ErbB2 heterodimer, implying an important contribution of the TM helix-helix interaction to signal transduction.