[Venous gangrene of small intestine following coronavirus infection (SARS-COVID-19)].

The pandemic of a new coronavirus infection has made certain adjustments to modern emergency medicine. Systemic endothelial dysfunction following COVID-19 largely determines hemostatic disorders. Numerous studies revealed that intense platelet adhesion followed by platelet aggregates in COVID-19 patients and functional disorders of fibrinolysis system are combined with activation and severe endothelial dysfunction.

Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P.

RNA-based enzyme RNase P is a ribonucleoprotein complex responsible primarily for 5'-maturation of tRNAs. RNase P comprises a catalytic RNA component and nine proteins. The assembly and maturation of RNase P involves an abundant and catalytically active precursor form, which includes all components except for proteins Rpr2 and Pop3.

Novel LaCl(Ce)-based spectrometer for deuterium plasma neutron diagnostics.

This work studies in detail the application possibility of a chlorine-based cerium-doped scintillator crystal [LaCl(Ce)] to the task of D-D neutron spectrometry. We conducted an experimental campaign aimed at deriving the optimal setup parameters and energy calibration using a variety of available neutrons and γ-sources. The GEANT4 code was used for modeling the detector response to γ-ray irradiation.

Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP.

RNase MRP is an essential eukaryotic ribonucleoprotein complex involved in the maturation of rRNA and the regulation of the cell cycle. RNase MRP is related to the ribozyme-based RNase P, but it has evolved to have distinct cellular roles. We report a cryo-EM structure of the S.

[Infusion prevention of fat globulaemia during total hip arthroplasty].

Aim: To assess the effect of the modified infusion therapy regimen on the frequency of development of laboratory and clinical manifestations of fat embolism syndrome in patients after hip replacement.

Material And Methods: The study was conducted in 80 patients (70 men and 10 women) who were admitted for planned revision hip arthroplasty. The criteria for not inclusion in the study were the presence of a traumatic brain injury, episodes of acute disturbance of blood supply (stroke) and diabetes mellitus in history.

In vitro reconstitution and analysis of eukaryotic RNase P RNPs.

RNase P is a ubiquitous site-specific endoribonuclease primarily responsible for the maturation of tRNA. Throughout the three domains of life, the canonical form of RNase P is a ribonucleoprotein (RNP) built around a catalytic RNA. The core RNA is well conserved from bacteria to eukaryotes, whereas the protein parts vary significantly.

[Geriatria in the republic of Mari El, looking into the past, present and future.].

Population aging is the dominant demographic trend in the Republic of Mari El with the rapid growth of medical and social problems. This requires specific changes in the health care system and an increase in the effectiveness of medical care for the elderly, the most vulnerable category of the population.

Chance and necessity in the evolution of RNase P.

RNase P catalyzes 5'-maturation of tRNAs in all three domains of life. This primary function is accomplished by either a ribozyme-centered ribonucleoprotein (RNP) or a protein-only variant (with one to three polypeptides). The large, multicomponent archaeal and eukaryotic RNase P RNPs appear disproportionate to the simplicity of their role in tRNA 5'-maturation, prompting the question of why the seemingly gratuitously complex RNP forms of RNase P were not replaced with simpler protein counterparts.

[Multifocal motor neuropathy with conduction blocks].

The article describes a case of multifocal motor neuropathy with conduction blocks in a female patient, aged 27 years. The development of the disease, results of neurological, laboratory, instrumental examinations, including electroneuromyography, and their role for the diagnosis and differential diagnosis are presented.

Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP.

Telomerase is the ribonucleoprotein enzyme that replenishes telomeric DNA and maintains genome integrity. Minimally, telomerase activity requires a templating RNA and a catalytic protein. Additional proteins are required for activity on telomeres in vivo.

Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components.

Ribonuclease (RNase) P and RNase MRP are closely related catalytic ribonucleoproteins involved in the metabolism of a wide range of RNA molecules, including tRNA, rRNA, and some mRNAs. The catalytic RNA component of eukaryotic RNase P retains the core elements of the bacterial RNase P ribozyme; however, the peripheral RNA elements responsible for the stabilization of the global architecture are largely absent in the eukaryotic enzyme. At the same time, the protein makeup of eukaryotic RNase P is considerably more complex than that of the bacterial RNase P.

[Epidemiology of malignant tumors of the brain and other parts of the CNS in the North-West Federal District of Russia].

For the first time in Russia the dynamics of morbidity and mortality from malignant tumors of the brain and other parts of the CNS in the North-West Federal District of Russia is presented. A precise elaboration of data on cases is performed according to the database of the Population-based Cancer Registries of St. Petersburg and Arkhangelsk region.

Applying UV crosslinking to study RNA-protein interactions in multicomponent ribonucleoprotein complexes.

Ribonucleoprotein complexes (RNPs) play crucial roles in a wide range of biological processes. Here, we describe experimental approaches to the UV crosslinking-based identification of protein-binding sites on RNA, using multicomponent Saccharomyces cerevisiae RNPs of the RNase P/MRP family as an example. To identify the binding sites of a protein component of interest, a hexahistidine affinity tag was fused to that protein.

Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate.

Ribonuclease (RNase) MRP is a ubiquitous and essential site-specific eukaryotic endoribonuclease involved in the metabolism of a wide range of RNA molecules. RNase MRP is a ribonucleoprotein with a large catalytic RNA moiety that is closely related to the RNA component of RNase P, and multiple proteins, most of which are shared with RNase P. Here, we report the results of an ultraviolet-cross-linking analysis of interactions between a photoreactive RNase MRP substrate and the Saccharomyces cerevisiae RNase MRP holoenzyme.

Crystallization of RNA-protein complexes: from synthesis and purification of individual components to crystals.

A broad range of biological processes relies on complexes between RNA and proteins. Crystallization of RNA-protein complexes can yield invaluable information on structural organizations of key elements of cellular machinery. However, crystallization of RNA-protein complexes is often challenging and requires special approaches.

Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA-protein interactions.

Eukaryotic ribonuclease (RNase) P and RNase MRP are closely related ribonucleoprotein complexes involved in the metabolism of various RNA molecules including tRNA, rRNA, and some mRNAs. While evolutionarily related to bacterial RNase P, eukaryotic enzymes of the RNase P/MRP family are much more complex. Saccharomyces cerevisiae RNase P consists of a catalytic RNA component and nine essential proteins; yeast RNase MRP has an RNA component resembling that in RNase P and 10 essential proteins, most of which are shared with RNase P.

Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP.

Ribonuclease (RNase) MRP is a multicomponent ribonucleoprotein complex closely related to RNase P. RNase MRP and eukaryotic RNase P share most of their protein components, as well as multiple features of their catalytic RNA moieties, but have distinct substrate specificities. While RNase P is practically universally found in all three domains of life, RNase MRP is essential in eukaryotes.

Substrate recognition by ribonucleoprotein ribonuclease MRP.

The ribonucleoprotein complex ribonuclease (RNase) MRP is a site-specific endoribonuclease essential for the survival of the eukaryotic cell. RNase MRP closely resembles RNase P (a universal endoribonuclease responsible for the maturation of the 5' ends of tRNA) but recognizes distinct substrates including pre-rRNA and mRNA. Here we report the results of an in vitro selection of Saccharomyces cerevisiae RNase MRP substrates starting from a pool of random sequences.

Of proteins and RNA: the RNase P/MRP family.

Nuclear ribonuclease (RNase) P is a ubiquitous essential ribonucleoprotein complex, one of only two known RNA-based enzymes found in all three domains of life. The RNA component is the catalytic moiety of RNases P across all phylogenetic domains; it contains a well-conserved core, whereas peripheral structural elements are diverse. RNA components of eukaryotic RNases P tend to be less complex than their bacterial counterparts, a simplification that is accompanied by a dramatic reduction of their catalytic ability in the absence of protein.

The P3 domain of eukaryotic RNases P/MRP: making a protein-rich RNA-based enzyme.

Nuclear Ribonuclease (RNase) P is a universal essential RNA-based enzyme made of a catalytic RNA component and a protein part; eukaryotic RNase P is closely related to a universal eukaryotic ribonucleoprotein RNase MRP. The protein part of the eukaryotic RNases P/MRP is dramatically more complex than that in bacterial and archaeal RNases P. The increase in the complexity of the protein part in eukaryotic RNases P/MRP was accompanied by the appearance of a novel structural element in the RNA component: an essential and phylogenetically conserved helix-loop-helix P3 RNA domain.

Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components.

RNase MRP is a ribonucleoprotein endoribonuclease found in three cellular locations where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm. Cytoplasmic RNase MRP is the nucleolar enzyme that is transiently relocalized during mitosis. Nucleolar RNase MRP (NuMRP) was purified to homogeneity, and we extensively purified the mitochondrial RNase MRP (MtMRP) to a single RNA component identical to the NuMRP RNA.

Eukaryotic ribonucleases P/MRP: the crystal structure of the P3 domain.

Ribonuclease (RNase) P is a site-specific endoribonuclease found in all kingdoms of life. Typical RNase P consists of a catalytic RNA component and a protein moiety. In the eukaryotes, the RNase P lineage has split into two, giving rise to a closely related enzyme, RNase MRP, which has similar components but has evolved to have different specificities.

Crystallization and preliminary X-ray diffraction analysis of the P3 RNA domain of yeast ribonuclease MRP in a complex with RNase P/MRP protein components Pop6 and Pop7.

Eukaryotic ribonucleases P and MRP are closely related RNA-based enzymes which contain a catalytic RNA component and several protein subunits. The roles of the protein subunits in the structure and function of eukaryotic ribonucleases P and MRP are not clear. Crystals of a complex that included a circularly permuted 46-nucleotide-long P3 domain of the RNA component of Saccharomyces cerevisiae ribonuclease MRP and selenomethionine derivatives of the shared ribonuclease P/MRP protein components Pop6 (18.

[Problem in the rehabilitation of patients with acute chemical poisonings in the toxicological hospital].

Follow-ups of 693 patients treated at the rehabilitation toxicological department for poisonings with psychopharmacological agents (n=549), cauterants (n=72), and opium narcotics (n=72) were summarized. Moreover, factors, such as the development of complications and the prehospitalization psychosomatic status of patients, influenced the length stay in a unit. Treatment of such patients should be aimed at eliminating at once a few causes that negatively affect the course of recovery for which it is expedient to use the methods of physicochemical hemotherapy, mesodiencephalic modulation, intestinal lavage, and hyperbaric oxygenation.

Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes.

Eukaryotic ribonuclease (RNase) P and RNase MRP are evolutionary related RNA-based enzymes involved in metabolism of various RNA molecules, including tRNA and rRNA. In contrast to the closely related eubacterial RNase P, which is comprised of an RNA component and a single small protein, these enzymes contain multiple protein components. Here we report the results of footprinting studies performed on purified Saccharomyces cerevisiae RNase MRP and RNase P holoenzymes.