ЕА

Е. А. Смирнова

Lomonosov Moscow State University

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ГЕ

Г. Е. Онищенко

Lomonosov Moscow State University

Ekaterina N. Baranova

Russian Academy of Sciences

ЕМ

Е. М. Лазарева

Lomonosov Moscow State University

M. S. Vildanova

Lomonosov Moscow State University

A. Bajer

Jagiellonian University

НВ

Н. В. Кононенко

All-Russian Scientific Research Institute of Food Biotechnology

Tatiana N. Bocharova

Kurchatov Institute

Alexander A. Volodin

Joint Institute for Nuclear Research

I. A. Chaban

Russian State Agrarian University - Moscow Timiryazev Agricultural Academy

НТ

Н. Т. Райхлин

Ministry of Health of the Russian Federation

Cooperative Institutions

Russian Academy of Sciences

Lomonosov Moscow State University

Moscow State University

Ministry of Health of the Russian Federation

Academy of Medical Sciences

All-Russian Scientific Research Institute of Food Biotechnology

A.V. Shubnikov Institute of Crystallography

Institute of Bioorganic Chemistry

National Institutes of Health

Russian State Agrarian University - Moscow Timiryazev Agricultural Academy

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Apoptosis-inducing and apoptosis-preventing functions of poliovirus

Journal of Virology (1995)

Elena A. Tolskaya Lyudmila I. Romanova Marina S. Kolesnikova T A Ivannikova Е. А. Смирнова

Data showing that an apoptotic reaction (the exit into the cytoplasm and nucleolytic internucleosomal degradation of chromosomal DNA, compaction and fragmentation of chromatin, cellular shrinkage, and cytoplasmic blebbing) developed in a subline of HeLa-S3 cells upon nonpermissive poliovirus infection with either a guanidine-sensitive poliovirus in the presence of guanidine, a guanidine-dependent mutant in the absence of guanidine, or certain temperature-sensitive mutants at a restrictive temperature are presented. Essentially, no apoptotic reaction occurred upon permissive infection of these cells. Both permissive and nonpermissive infections resulted in the inhibition of host protein synthesis. Actinomycin D or cycloheximide also elicited a rapid apoptotic reaction in uninfected cells. However, preinfection or coinfection with poliovirus prevented the apoptotic response to the addition of actinomycin D, and preinfection blocked cycloheximide-induced apoptosis as well. These data fit a model in which the cells used are prepared to develop apoptosis, with their viability due to the presence of certain short-lived mRNA and protein species. Poliovirus infection turns on two oppositely directed sets of reactions. On the one hand, the balance is driven toward apoptosis, probably via the shutoff of host macromolecular synthesis. On the other hand, viral protein exhibits antiapoptotic activity, thereby preventing premature cell death. To our knowledge, this is the first description of an antiapoptotic function for an RNA virus.

HeLa

Fragmentation

Guanidine

10.1128/jvi.69.2.1181-1189.1995

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Citations (198)

Protein crystal growth on the Russian segment of the International Space Station

Crystallography Reports (2009)

Е. А. Смирнова Yu. A. Kislitsyn N. I. Sosfenov A. V. Lyashenko А. Н. Попов

Protein crystallization

Crystal (programming language)

Random hexamer

10.1134/s106377450905023x

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Citations (14)

СТРЕСС ЭНДОПЛАЗМАТИЧЕСКОГО РЕТИКУЛУМА, ИНДУЦИРОВАННЫЙ ЖАСМОНОВОЙ КИСЛОТОЙ, ВЫЗЫВАЕТ СЕЛЕКТИВНЫЙ ОТВЕТ В КУЛЬТИВИРУЕМЫХ НОРМАЛЬНЫХ И ОПУХОЛЕВЫХ КЛЕТКАХ ЭПИДЕРМАЛЬНОГО ПРОИСХОЖДЕНИЯ

Биохимия (2019)

M. S. Vildanova А.А. Саидова А.И. Фокин Д.М. Поташникова Г. Е. Онищенко

10.1134/s0320972519090070

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Citations (1)

Влияние характеристик поверхности и генезиса гематита на его активность в процессах его микробиологического восстановления

Башкирский химический журнал (2012)

В. Ю. Орлов Е. М. Волков Н. Ю. Пухова Е. А. Смирнова

The Fe 2O 3 (hematite) reduction with using a pure bacterial culture Georgenia ferrireducens in a nutrient medium with fructose as the sole source of carbon and energy has been investigated. The samples of hematite, which used for reduction and differed from each other by obtaining method and, consequently, by its structure, has been shown different activity in the studied process. It was assumed, that different activity shows due to the peculiarities of the fine crystalline structure of the samples.

Carbon fibers

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Crystal structure of Pu5Ru3, Pu5Rh3, Pu5Os3, Pu5Ir3, Pu5Pt3

Soviet Atomic Energy (1974)

A. V. Beznosikova Н.Т. Чеботарев Alexey Lukyanov A. V. Chernyi Е. А. Смирнова

10.1007/bf01125637

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Microtubule Converging Centers: Implications for Microtubule Dynamics in Higher Plants

Springer eBooks (1994)

A. Bajer Е. А. Смирнова Kolja Wawrowsky Rainer Wolf Jadwiga Molè-Bajer

Microtubule nucleation

Microtubule organizing center

Spindle pole body

Astral microtubules

10.1007/978-3-642-78975-5_20

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Citations (2)

Trifluralin-induced disorganization of microtubular cytoskeleton alters the development of roots inHordeum vulgareL.

Acta Biologica Hungarica (2008)

Eugene V. Sheval Yu. Kazhura Nina Poleshuk Е. М. Лазарева Е. А. Смирнова

Trifluralin

Multinucleate

Plant cell

10.1556/abiol.59.2008.4.7

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Citations (10)

A Model for Dynamin Self-assembly Based on Binding Between Three Different Protein Domains

Journal of Biological Chemistry (1999)

Е. А. Смирнова Dixie‐Lee Shurland Erin Newman‐Smith Babak Pishvaee Alexander M. van der Bliek

Dynamin is a 100-kDa GTPase that assembles into multimeric spirals at the necks of budding clathrin-coated vesicles. We describe three different intramolecular binding interactions that may account for the process of dynamin self-assembly. The first binding interaction is the dimerization of a 100-amino acid segment in the C-terminal half of dynamin. We call this segment the assembly domain, because it appears to be critical for multimerization. The second binding interaction occurs between the assembly domain and the N-terminal GTPase domain. The strength of this interaction is controlled by the nucleotide-bound state of the GTPase domain, as shown with mutations in GTP binding motifs and in vitro binding experiments. The third binding interaction occurs between the assembly domain and a segment that we call the middle domain. This is the segment between the N-terminal GTPase domain and the pleckstrin homology domain. The three different binding interactions suggest a model in which dynamin molecules first dimerize. The dimers are then linked into a chain by a second binding reaction. The third binding interaction might connect adjacent rungs of the spiral.

Pleckstrin homology domain

10.1074/jbc.274.21.14942

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Citations (133)

Glyprolines and Semax Prevent Stress-Induced Microcirculatory Disturbances in the Mesentery

Bulletin of Experimental Biology and Medicine (2003)

Г. Н. Копылова Е. А. Смирнова L. Ts. Sanzhieva Б. А. Умарова T. V. Lelekova

10.1023/b:bebm.0000017087.90585.a9

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Citations (4)

Molecular Biology of the Cell (2001)

Е. А. Смирнова Lorena Griparić Dixie‐Lee Shurland Alexander M. van der Bliek

Mutations in the human dynamin-related protein Drp1 cause mitochondria to form perinuclear clusters. We show here that these mitochondrial clusters consist of highly interconnected mitochondrial tubules. The increased connectivity between mitochondria indicates that the balance between mitochondrial division and fusion is shifted toward fusion. Such a shift is consistent with a block in mitochondrial division. Immunofluorescence and subcellular fractionation show that endogenous Drp1 is localized to mitochondria, which is also consistent with a role in mitochondrial division. A direct role in mitochondrial division is suggested by time-lapse photography of transfected cells, in which green fluorescent protein fused to Drp1 is concentrated in spots that mark actual mitochondrial division events. We find that purified human Drp1 can self-assemble into multimeric ring-like structures with dimensions similar to those of dynamin multimers. The structural and functional similarities between dynamin and Drp1 suggest that Drp1 wraps around the constriction points of dividing mitochondria, analogous to dynamin collars at the necks of budding vesicles. We conclude that Drp1 contributes to mitochondrial division in mammalian cells.

DNM1L

Mitochondrial apoptosis-induced channel

10.1091/mbc.12.8.2245

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Citations (1,762)