Стилистический эффект разговорной речи и его составляющие

В обучении русскому языку как иностранному на современном этапе большое внимание уделяется особенностям русской разговорной речи. Это обусловлено целым рядом причин, среди которых, на наш взгляд, можно выделить следующие: во-первых, разговорная речь всегда отличается активностью проникновения во все сферы жизнедеятельности людей и функционирует как в повседневном общении, так и в различных сферах (литературе, кино, политике и т.д.). Во-вторых, разговорная речь носит многожанровый характер, что зачастую затрудняет ее понимание иностранными студентами. В-третьих, в разговорную речь помимо слов нейтрального стиля все активнее стала проникать арготическая лексика. Именно в связи с этим особый интерес у нас вызывает разговорный стиль речи в преломлении на инофонную аудиторию

Proteins commonly identified in all conditions.

<p>Protein and gene names, molecular weight in daltons, cellular localization, function/structure, Uniprot accession number, protein identification probability from iProphet and unique number of identified peptides for each individual protein are shown.</p

Uniquely identified proteins in anti-CD4 co-immunoprecipitations in induced CD4 internalization and degradation in Mφ (Condition 2).

<p>Protein and gene names, molecular weight in Daltons, cellular localization, function/structure, Uniprot accession number, protein identification probability from iProphet and unique number of identified peptides for each individual protein are shown.</p

Uniquely identified proteins in anti-CD4 co-immunoprecipitations in induced CD4 internalization and blocked degradation in Mφ (Condition 3).

<p>Protein and gene names, molecular weight in Daltons, cellular localization, function/structure, Uniprot accession number, protein identification probability from iProphet and unique number of identified peptides for each individual protein are shown.</p

Western blot analysis of CD4 co-immunoprecipitates in Mφ.

<p>A total of 1×10⁷ Mφ were left untreated (Condition 1, blue), treated for 18 hours with supernatants from activated T cells (Condition 2, red), treated for 18 hours with supernatants from activated T cells in the presence of 5 µM MG132 and 100 nM BafA1 (Condition 3, green), lysed and anti-CD4 immunoprecipitation reactions were carried out. Isotype control immunoprecipitations were also performed to show background protein binding. Immunoisolates were resuspended in Laemmli sample buffer under reducing and denaturing conditions and resolved on a SDS-PAGE gel. Membranes were incubated with antibodies against CD4, clathrin heavy chain (HC) 1, E3 Ubiquitin (Ub) ligase Itch, CD9 and CCR5. Primary antibodies were detected and scanned using the quantitative western blotting imaging Odyssey System. A representative blot of three different blood donors is shown (n = 3).</p

Gene Ontology (GO) annotations of the uniquely identified proteins in anti-CD4 immunoprecipitations in Mφ.

<p>Protein identifications from the three different conditions were exported from the in-house developed Central Proteomics Facilities data analysis pipeline (CPFP) and uploaded to ProteinCenter software. <b>A</b> illustrates the percentage of protein identifications versus protein cellular localizations (GO cellular annotations); <b>B</b> illustrates the percentage of protein identifications versus protein molecular functions (GO molecular annotations) and <b>C</b> illustrates the percentage of protein identifications versus protein biological functions (GO biological annotations). Blue bars represent the percentage of unique proteins identified in condition 1 (Resting macrophages); Red bars represent the percentage of unique proteins identified in condition 2 (Induced CD4 internalization and degradation); Green bars represent the percentage of unique proteins identified in condition 3 (Induced CD4 internalization and blocked degradation).</p

CD4 is internalized and degraded after treatment with conditioned media from activated T cells.

<p>Mφ were treated with conditioned media from activated T cells for 18 hours or left untreated, followed by flow cytometry staining with directly conjugated mAb to CD4. <b>A</b> Black histogram represents the appropriate isotype control. Histograms show the intensity of the signal on the X-axis with a log₁₀-scale and the percentage of maximum expression on the Y-axis. Representative staining of more than five donors tested (n>5). <b>B</b> Bars represent the mean percentage of Mφ expressing surface CD4 with SD error bars from ten independent donors (n = 10). <b>C</b> Total CD4 expression levels (surface + intracellular) were determined by dividing the geometrical MFI of the antibody staining over the MFI of the isotype control. Bars represent the mean values of five independent donors (n = 5) with SD error bars. In <b>B</b> and <b>C</b>, black bar corresponds to untreated Mφ and white bar corresponds to conditioned media treated Mφ (T cell Sup).</p

Alternate reading frame-encoded amino acids in circulating viral sequences.

<p>A) Distribution of known mutant origins across viral ARF sequences attributable to a particular cause based on information associated with the sequence accession the NCBI nr protein database presented in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0039311#pone.0039311.s002" target="_blank">Table S2</a>. B) Composition of viral coding sequence computed as a percentage assigned to the coding sequence for the Env, Gag, Pol poly-proteins based on nucleotide base counts for a particular gene region compared to the total nucleotide count for the structural genes of the virus. Gag comprises 1,503 nt of the total of 6,878 nt of structural gene sequence; Pol comprises 3,139 nt of the total; Env comprises of 2,571 nt of the total. This is the distribution of origins within the genome that would be expected if originating events for the incorporation of ARF and their detection in circulating HIV-1 viral sequences were distributed randomly throughout the genome. C) The distribution of ARF incorporated into circulating viral sequences that was observed in our searches of NCBI nr protein database for ARF sequences in circulating HIV-1 viral sequences. The percentages were computed by dividing the number of BLAST hits with ARF sequence incorporated into a given gene region by the 123 total hits examined. D) A three-way alignment between the HXB-2 reference sequence for the Env region, the accession AAL78125.1 and the alternate reading frame encoded ORF 67. E) A three-way alignment between the HXB-2 reference sequence for the Gag region, the accession AEQ21252.1 and the alternate reading frame encoded ORF 3. F) A three-way alignment between the HXB-2 reference sequence for the Pol region, the accession CAF29000.1 and the alternate reading frame encoded ORF 23. All three-way alignments were generated by combining two pair-wise alignments created in Geneious, followed by manual editing. Note each accession is similar to both the HXB-2 reference sequence for the structural proteins and the alternate reading frame encoded sequence, but not to both sequences simultaneously within the same region of the sequence.</p

HIV-1 genome (HXB-2 strain), and localization of the 47 alternative reading frames (ARF).

<p>Figure depicts all 199 ARF-tested peptides. These include 13 forward ARF within frames 1, 2 or 3 (in green) and 34 reverse ARF within frames -1, -2 or -3 (in purple). HIV-1 classically defined encoding genes are shown in blue.</p

ARF responses in one HIV-1 chronically infected patients before and on HAART.

<p>In the pie charts each color represents a pool of immune response that the patient mounted against. Numbers inside the pie charts correspond to the magnitude of the response against the pool in SFU/million PBMC.</p