Correction by peptide bioregulators of micro- and ultramicroscopic changes in the pineal gland caused by stress under light deprivation

It has been established, that immobilizing stress causes decreasing of light cell's amount in pineal gland, which are the main source of melatonin production like under usual lighting and like under light deprivation. Light deprivation, that stimulates pineal gland function, also provides activation of pre-melatonin biosynthesis that increased production of endogenous melatonin

Dynamics of gene C-Fos activity in paraventricular nuclei of the hypothalamus of rats at light stress

Stress influence (light deprivation and stimulation) on gene c-fos state of early functional activity in subnuclei of paraventricular nucleus (PVN) of hypothalamus of rats in various periods of twenty-four hours (day and night) has been elucidated. Product expression of this gene - c-Fos protein - in animals which were hold under normal conditions of light and darkness alternations showed rather distinct circadian character. Simultaneously, change of duration of the light-darkness cycle results in evident desynchronization

Publicity Text is in a Religious Sphere

Статтю присвячено опису релігійного (культового) рекламного тексту. Виокремлено та описано загальні характеристики вербального компонента цього виду соціальної реклами, визначено особливості його структури та змісту, вербальні засоби передачі аксіологічних характеристик об’єкта пропозиції. The article is devoted description of religious (cult) publicity text. Selected and described general descriptions of verbal component of this type of the social advertising, the features of his structure and maintenance, verbal facilities of transmission of axiological descriptions of object of suggestion, are certain

UniPROBE, update 2011: expanded content and search tools in the online database of protein-binding microarray data on protein–DNA interactions

The Universal PBM Resource for Oligonucleotide-Binding Evaluation (UniPROBE) database is a centralized repository of information on the DNA-binding preferences of proteins as determined by universal protein-binding microarray (PBM) technology. Each entry for a protein (or protein complex) in UniPROBE provides the quantitative preferences for all possible nucleotide sequence variants (‘words’) of length k (‘k-mers’), as well as position weight matrix (PWM) and graphical sequence logo representations of the k-mer data. In this update, we describe >130% expansion of the database content, incorporation of a protein BLAST (blastp) tool for finding protein sequence matches in UniPROBE, the introduction of UniPROBE accession numbers and additional database enhancements. The UniPROBE database is available at http://uniprobe.org.National Institutes of Health (U.S.) (grant number R01 HG003985

UniPROBE, update 2011: expanded content and search tools in the online database of protein-binding microarray data on protein–DNA interactions

The Universal PBM Resource for Oligonucleotide-Binding Evaluation (UniPROBE) database is a centralized repository of information on the DNA-binding preferences of proteins as determined by universal protein-binding microarray (PBM) technology. Each entry for a protein (or protein complex) in UniPROBE provides the quantitative preferences for all possible nucleotide sequence variants (‘words’) of length k (‘k-mers’), as well as position weight matrix (PWM) and graphical sequence logo representations of the k-mer data. In this update, we describe >130% expansion of the database content, incorporation of a protein BLAST (blastp) tool for finding protein sequence matches in UniPROBE, the introduction of UniPROBE accession numbers and additional database enhancements. The UniPROBE database is available at http://uniprobe.org.National Institutes of Health (U.S.) (grant number R01 HG003985

UniPROBE, update 2015: new tools and content for the online database of protein-binding microarray data on protein-DNA interactions

The Universal PBM Resource for Oligonucleotide Binding Evaluation (UniPROBE) serves as a convenient source of information on published data generated using universal protein-binding microarray (PBM) technology, which provides in vitro data about the relative DNA-binding preferences of transcription factors for all possible sequence variants of a length k (‘k-mers’). The database displays important information about the proteins and displays their DNA-binding specificity data in terms of k-mers, position weight matrices and graphical sequence logos. This update to the database documents the growth of UniPROBE since the last update 4 years ago, and introduces a variety of new features and tools, including a new streamlined pipeline that facilitates data deposition by universal PBM data generators in the research community, a tool that generates putative nonbinding (i.e. negative control) DNA sequences for one or more proteins and novel motifs obtained by analyzing the PBM data using the BEEML-PBM algorithm for motif inference. The UniPROBE database is available at http://uniprobe.org.National Institutes of Health (U.S.) (R01 HG003985)National Science Foundation (U.S.). Graduate Research Fellowship Progra

DNA-Binding Specificity Changes in the Evolution of Forkhead Transcription Factors

The evolution of transcriptional regulatory networks entails the expansion and diversification of transcription factor (TF) families. The forkhead family of TFs, defined by a highly conserved winged helix DNA-binding domain (DBD), has diverged into dozens of subfamilies in animals, fungi, and related protists. We have used a combination of maximum-likelihood phylogenetic inference and independent, comprehensive functional assays of DNA-binding capacity to explore the evolution of DNA-binding specificity within the forkhead family. We present converging evidence that similar alternative sequence preferences have arisen repeatedly and independently in the course of forkhead evolution. The vast majority of DNA-binding specificity changes we observed are not explained by alterations in the known DNA-contacting amino acid residues conferring specificity for canonical forkhead binding sites. Intriguingly, we have found forkhead DBDs that retain the ability to bind very specifically to two completely distinct DNA sequence motifs.We propose an alternate specificity-determining mechanism whereby conformational rearrangements of the DBD broaden the spectrum of sequence motifs that a TF can recognize. DNA-binding bispecificity suggests a previously undescribed source of modularity and flexibility in gene regulation and may play an important role in the evolution of transcriptional regulatory networks.Organismic and Evolutionary Biolog