Synthesis, Photo- and Electroluminescence of New Polyfluorene Copolymers Containing Dicyanostilbene and 9,10-Dicyanophenanthrene in the Main Chain.

Using palladium-catalyzed Suzuki polycondensation, we synthesized new light-emitting fluorene copolymers containing the dicyano derivatives of stilbene and phenanthrene and characterized them by gel permeation chromatography, UV-vis absorption spectroscopy, spectrofluorimetry, and cyclic voltammetry. The photoluminescence spectra of the synthesized polymers show significant energy transfer from the fluorene segments to the dicyanostilbene and 9,10-dicyanophenanthrene units, which is in agreement with the data of theoretical calculations. OLEDs based on these polymers were fabricated with an ITO/PEDOT-PSS (35 nm)/p-TPD (30 nm)/PVK (5 nm)/light emitting layer (70-75 nm)/PF-PO (20 nm)/LiF (1 nm)/Al (80 nm) configuration.

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.

Plant transcripts with long or structured upstream open reading frames in the NDL2 5' UTR can escape nonsense-mediated mRNA decay in a reinitiation-independent manner.

Many eukaryotic transcripts contain upstream open reading frames (uORFs). Translated uORFs can inhibit the translation of main ORFs by imposing the need for reinitiation of translation. Translated uORFs can also lead to transcript degradation by the nonsense-mediated mRNA decay (NMD) pathway.

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.

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.

[Galectin-3, Markers of Oxidative Stress and Renal Dysfunction in Patients With Chronic Heart Failure].

Objective: to determine levels of galectin-3, markers of renal dysfunction, and plasma oxidative stress; to assess their correlation in patients with chronic heart failure (CHF) of various severity.

Material And Methods: We included in this study 157 CHF patients (with documented prior myocardial infarction. Patients were divided into 3 groups according to their NYHA functional class (group 1 - class II n=60, group 2 - class III n=52, group 3 - class IV n=45).

The NMD Factor UPF3 Is Feedback-Regulated at Multiple Levels and Plays a Role in Plant Response to Salt Stress.

Nonsense-mediated mRNA decay (NMD) is a eukaryotic RNA surveillance mechanism that degrades aberrant transcripts and controls the levels of many normal mRNAs. It was shown that balanced expression of the NMD factor UPF3 is essential for the maintenance of proper NMD homeostasis in . expression is controlled by a negative feedback loop that exposes transcript to NMD.

Galectin-3 in patients with chronic heart failure: association with oxidative stress, inflammation, renal dysfunction and prognosis.

Background: Galectin-3 is a recently developed biomarker of fibrosis, which may play a role in cardiac remodeling and associated with both the progression and severity of heart failure (HF).

Methods: A prospective cohort study of 190 patients with documented prior myocardial infarction and chronic HF (NYHA class II-IV) was conducted. Patients were divided into 3 groups based on their NYHA functional class.

[STATE OF THE SOIL IN THE TERRITORY OF THE CITY WITH THE DEVELOPED PETROLEUM-REFINING INDUSTRY].

In 2013-2014, there was performed the study of the soil in the territory of the city of Novokuibyshevsk. The concentrations of heavy metals and petroleum products on the territory of the industrial zone of the city of Novokuibyshevsk were determined. The evaluation of concentrations ofanthropogenic toxicants was carried out in Novokuibyshevsk by means of laboratory monitoring of environmental pollution.

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.

The feedback control of UPF3 is crucial for RNA surveillance in plants.

Nonsense-mediated-decay (NMD) is a eukaryotic RNA surveillance mechanism that controls the levels of both aberrant and normal transcripts. The regulation of this process is not well understood. The Arabidopsis NMD factor UPF3 is regulated by a negative feedback-loop that targets its own transcript for NMD.

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.

Phylogeny and a structural model of plant MHX transporters.

Background: The Arabidopsis thaliana MHX gene (AtMHX) encodes a Mg²⁺/H⁺ exchanger. Among non-plant proteins, AtMHX showed the highest similarity to mammalian Na⁺/Ca²⁺ exchanger (NCX) transporters, which are part of the Ca²⁺/cation (CaCA) exchanger superfamily.

Results: Sequences showing similarity to AtMHX were searched in the databases or sequenced from cDNA clones.

CsrA activates flhDC expression by protecting flhDC mRNA from RNase E-mediated cleavage.

Csr is a conserved global regulatory system that controls expression of several hundred Escherichia coli genes. CsrA protein represses translation of numerous genes by binding to mRNA and inhibiting ribosome access. CsrA also activates gene expression, although an activation mechanism has not been reported.

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.

CsrA represses translation of sdiA, which encodes the N-acylhomoserine-L-lactone receptor of Escherichia coli, by binding exclusively within the coding region of sdiA mRNA.

The RNA binding protein CsrA is the central component of a conserved global regulatory system that activates or represses gene expression posttranscriptionally. In every known example of CsrA-mediated translational control, CsrA binds to the 5' untranslated region of target transcripts, thereby repressing translation initiation and/or altering the stability of the RNA. Furthermore, with few exceptions, repression by CsrA involves binding directly to the Shine-Dalgarno sequence and blocking ribosome binding.

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.

Complex regulation of the global regulatory gene csrA: CsrA-mediated translational repression, transcription from five promoters by Eσ⁷⁰ and Eσ(S), and indirect transcriptional activation by CsrA.

CsrA of Escherichia coli is an RNA-binding protein that globally regulates gene expression by repressing translation and/or altering the stability of target transcripts. Here we explored mechanisms that control csrA expression. Four CsrA binding sites were predicted upstream of the csrA initiation codon, one of which overlapped its Shine-Dalgarno sequence.

[Substantiation of the program of realization of bases of the state policy of a healthy nutrition of population of the Samara Region for the period till 2020 year].

Substantiate the need for long-term program of sanitation the diet of the population of the Samara Region. A systemic analysis of actual nutrition of different population groups in the region showed an excessive consumption of fats and added sugar--the main risk factors of obesity, cardiovascular diseases and diabetes mellitus. The risks of inadequate consumption of vitamins B, calcium, iron, caused by the irrational combination of the foodstuff use, are revealed.

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.

[Comparative assessment of educational conditions in various secondary educational institutions in Samara].

The educational medium in varying secondary educational establishments of Samara was comparatively analyzed in accordance with the sanitary regulations SanPiN 2.4.2.

The leader intron of AtMHX can elicit, in the absence of splicing, low-level intron-mediated enhancement that depends on the internal intron sequence.

Background: Introns stimulate gene expression in a wide range of organisms by increasing the levels of mature mRNA, without affecting mRNA stability. Although introns sometimes function as transcriptional enhancers, they usually stimulate expression by a process termed intron-mediated enhancement (IME). The mechanism of IME is largely unknown.

The upstream open reading frame of the Arabidopsis AtMHX gene has a strong impact on transcript accumulation through the nonsense-mediated mRNA decay pathway.

Approximately 20% of plant genes possess upstream open-reading frames (uORFs). The effect of uORFs on gene expression has mainly been studied at the translational level. Very little is known about the impact of plant uORFs on transcript content through the nonsense-mediated mRNA decay (NMD) pathway, which degrades transcripts bearing premature termination codons (PTCs).

[Unbalanced nutrition is a universal factor in the occurrence of visceral diseases].

Nutrition is one of the most important determinants of human health. The investigation has determined the pattern of actual nutrition of the Samara Region, its influence on the occurrence of cardiovascular, endocrine, urogenital, and musculoskeletal, and digestive diseases. Emphasis is placed on unbalanced diets excluding meat, by increasing the consumption of bread and cereals, which is a universal factor for the development of visceral diseases.

Overexpression of AtMHX in tobacco causes increased sensitivity to Mg2+, Zn2+, and Cd2+ ions, induction of V-ATPase expression, and a reduction in plant size.

AtMHX is a vacuolar transporter encoded by a single gene in Arabidopsis. Electrophysiological analysis showed that it exchanges protons with Mg(2+), Zn(2+), and Fe(2+) ions. The physiological impact of AtMHX was examined so far only in tissue-culture grown seedlings of tobacco plants overexpressing this transporter.