The Exosome-Mediated Epigenome: Non-Coding RNA and mRNA-Coding Networks in Microbiome-Cellular Communication, Inflammation, and Tumorigenesis Along the Oral-Gut-Lung Axis. [PDF]
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A novel accessory gene product of tick-borne Dhori-Orthomyxovirus, encoded by overlooked spliced transcripts of RNA segment 6. [PDF]
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Adsorption of viral matrix protein M1 in acidic medium
Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology, 2013Adsorption of viral matrix protein M1 on the self-assembled monolayer of carboxyhexadecanthiol molecules simulating the surface of the cell membrane was studied by surface plasmon resonance refractometry technique. It was shown that in the acidic medium (pH 4.0) the fraction of irreversibly adsorbed protein increases with time.
V. V. Brevnov +2 more
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The matrix (M) protein of vesicular stomatitis virus has been shown to induce the rounding of cells. Experiments were performed in order to define the mechanism by which M protein could cause this cytopathic effect (CPE). Immunofluorescence experiments performed on infected cells indicate that cellular rounding coincides with the disruption of the ...
R, Melki, Y, Gaudin, D, Blondel
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Numerous studies have shown that viruses can utilize or manipulate ribosomal proteins to achieve viral protein biosynthesis and replication. In our recent studies using proteomics analysis of virus-infected cells, we found that ribosomal protein L18 (RPL18) was the highest up-regulated differentially expressed protein, along with the increasingly ...
Zhiqiang Duan +5 more
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Effects of pH on the adsorption of the viral matrix protein M1
Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology, 2015Adsorption of the viral matrix protein M1 on a substrate simulating the lipid membrane surface of the influenza virus was studied by surface plasmon resonance (SPR). It was found that a decrease of pH leads to an increase of the time to reach the saturated level of adsorption, despite the growth of its initial rate.
V. V. Brevnov +2 more
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A novel nuclear export activity in HIV-1 matrix protein required for viral replication
Nature, 1999An important aspect of the pathophysiology of human immunodeficiency virus type-1 (HIV-1) infection is the ability of the virus to replicate in non-dividing cells. HIV-1 matrix (MA), the amino-terminal domain of the Pr55 gag polyprotein (Pr55), bears a nuclear localization signal that promotes localization of the viral preintegration complex to the ...
Dupont, Stefan A. +7 more
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