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Localization of the influenza virus nucleoprotein: cell-associated and extracellular non-virion forms.
Both the supernatant of influenza virus-infected chick embryo cells and allantoic fluid containing influenza virus were shown to contain non-virion nucleoprotein (NP), which reacted readily withExpand
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Bimane Fluorescence Scanning Suggests Secondary Structure near the S3-S4 Linker of BK Channels*
Gating of large conductance Ca2+-activated K+ channels (BK or maxi-K channels) is controlled by a Ca2+-sensor, formed by the channel cytoplasmic C-terminal domain, and a voltage sensor, formed by itsExpand
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Intracellular oligomerization of influenza virus nucleoprotein.
It has previously been shown that the purified influenza virus nucleoprotein (NP) forms the oligomers in vitro in NP preparations obtained from virions (Wiley et al., 1977, Virology, 79, 446-448;Expand
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Stability of intracellular influenza virus nucleocapsid protein oligomers
Summary.Stability of A/Duck/Ukrainae/63 (H3N8) influenza virus intracellular NP oligomers was studied using reducing agents, denaturants, detergents, salts, various pH and a range of temperatures.Expand
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[Effect of the antiviral drug Ingaviruin on intracellular transformations and import into the nucleus of influenza A virus nucleocapsid protein].
The paper presents the results of studying the effect of the antiviral drug Ingavirin on different stages of intracellular transformations of influenza A virus nucleocapsid protein (NP). IngavirinExpand
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Extracellular truncated influenza virus nucleoprotein.
In the culture medium of MDCK cells infected with influenza A/Duck/Ukraine/1/63(H3N8) virus two kinds of virus nucleoprotein (NP) are detected: full-length 56 kDa NP and truncated 53 kDa NP. However,Expand
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[Antigenic variability of avian influenza virus A/H13, isolated in the USSR].
The antigenic structure of influenza H13 viruses isolated from wild birds in the USSR in 1976-1985 was studied. Antiserum against the reference A/gull/Maryland/704/77 (H13N6) strain was used toExpand
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Non-compact nucleocapsid protein multimers in influenza-virus-infected cells
Summary.We have previously shown that protease-resistant and highly immunoreactive compact NP oligomers, dissociating at +80 °C and possessing properties of folded proteins, are post-translationallyExpand
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[Use of the plaque method to reveal the phenomenon of autointerference in influenza virus].
The paper describes a simple and convenient method for qualitative and quantitative evaluation of the capacity of influenza virus for autointerference consisting in the lack or considerable reductionExpand
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Transient disulfide bonds formation in conformational maturation of influenza virus nucleocapsid protein (NP).
It has been previously shown that influenza virus nucleocapsid protein (NP) forms homooligomers in vivo. Our analyses revealed that the reducing agent dithiothreitol (DTT) introduced in pulseExpand
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