Study of the electronic structure of NixTiSe2 by EMF method.

The electron structure of the NixTiSe2 system has been studied by the electromotive force (EMF) method in Cu|Cu+|NixTiSe2 and Na|Na+|NixTiSe2 electrochemical cells. Two critical transitions have been found in this system at x = 0.25 and x = 0.

Computational and experimental mapping of the allosteric network of two manganese ABC transporters.

Transition metals (e.g., Fe, Zn, Mn) are essential enzymatic cofactors in all organisms.

The features of Tat protein of human immunodeficiency virus type 1 (Retroviridae: ) non-A6 variants, characteristic for the Russian Federation.

Introduction: Tat protein is a trans-activator of HIV-1 genome transcription, with additional functions including the ability to induce the chronic inflammatory process. Natural amino acid polymorphisms in Tat may affect its functional properties and the course of HIV infection. The aim of this work is to analyze the marks of Tat consensus sequences in non-A6 HIV-1 variants characteristic of the Russian Federation, as well as study natural polymorphisms in Tat CRF63_02A6 and subtype B variants circulating in Russia.

Comparative evaluation of ACetic - MEthanol high salt dissociation approach for single-cell transcriptomics of frozen human tissues.

Current dissociation methods for solid tissues in scRNA-seq studies do not guarantee intact single-cell isolation, especially for sensitive and complex human endocrine tissues. Most studies rely on enzymatic dissociation of fresh samples or nuclei isolation from frozen samples. Dissociating whole intact cells from fresh-frozen samples, commonly collected by biobanks, remains a challenge.

Characterization and PCR Application of Family B DNA Polymerases from .

DNA polymerases from the hyperthermophilic Archaea have attracted considerable attention as PCR enzymes due to their high thermal stability and proofreading 3' → 5' exonuclease activity. This study is the first to report data concerning the purification and biochemical characteristics of the Tst DNA polymerase from . Both the wild type Tst(wt) DNA polymerase and its chimeric form containing the P36H substitution-which reduces the enzyme's affinity for the U-containing template and dUTP-and the DNA-binding domain Sso7d from were obtained and analyzed.