Publications by authors named "N A Barinov"

Introduction: WhiA is a conserved protein found in numerous bacteria. It consists of an HTH DNA-binding domain linked with a homing endonuclease (HEN) domain. WhiA is one of the most conserved transcription factors in reduced bacteria of the class Mollicutes.

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Abnormal intracellular phase transitions in mutant hnRNP A1 may underlie the development of several neurodegenerative diseases. The risk of these diseases increases upon repeat expansion and the accumulation of the corresponding G-quadruplex (G4)-forming RNA, but the link between this RNA and the disruption of hnRNP A1 homeostasis has not been fully explored so far. Our aim was to clarify the mutual effects of hnRNP A1 and C9Orf72 G4 in vitro.

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Multi-responsive polymeric nanocontainers attract significant attention for their potential applications in biotechnology, drug delivery, catalysis, and other fields. By incorporating a liquid-crystalline (LC) mesogenic ligand with an alkyl tail length ranging from 8-12 carbons, ionically linked to the polymer backbone, we generate vesicles with walls significantly thinner than those of conventional polymersomes, approaching the thickness of a lipid bilayer. These LC vesicles, ranging in size from 50-120 nm, are designed to be mechanically robust due to the alignment of the hydrophilic polymer backbone within the plane of the vesicle wall.

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Understanding of DNA interaction with carbonaceous surfaces (including graphite, graphene and carbon nanotubes) is important for the development of DNA-based biosensors and other biotechnological devices. Though many issues related to DNA adsorption on graphitic surfaces have been studied, some important aspects of DNA interaction with graphite remain unclear. In this work, we use atomic force microscopy (AFM) equipped with super-sharp cantilevers to analyze the morphology and conformation of relatively long DNA molecule adsorbed on a highly oriented pyrolytic graphite (HOPG) surface.

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Article Synopsis
  • Self-assembling nanoparticles (saNP) and nanofibers were identified from SARS-CoV-2 proteins, showing various sizes and consistent solid structures rather than hollow vesicles.
  • The stability of these saNP was confirmed over two years, maintaining their integrity even under multiple freeze-thaw cycles.
  • Interactions with specific cell receptors indicated efficient entry of S1 and RBD saNP into certain cells, and their amyloid-like characteristics raise concerns about potential impacts on protein health and vaccine stability in patients.
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