43 research outputs found

    Multifrequency VLBI Observations of the Broad Absorption Line Quasar J1020+4320: Recently Restarted Jet Activity?

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    This paper reports very-long-baseline interferometry observations of the radio-loud broad absorption line (BAL) quasar J1020+4320 at 1.7, 2.3, 6.7, and 8.4 GHz using the Japanese VLBI network (JVN) and European VLBI network (EVN). The radio morphology is compact with a size of ~10 pc. The convex radio spectrum is stable over the last decade; an observed peak frequency of 3.2 GHz is equivalent to 9.5 GHz in the rest frame, suggesting an age of the order of ~100 years as a radio source, according to an observed correlation between linear size and peak frequency of compact steep spectrum (CSS) and giga-hertz peaked spectrum (GPS) radio sources. A low-frequency radio excess suggests relic of past jet activity. J1020+4320 may be one of the quasars with recurrent and short-lived jet activity during a BAL-outflowing phase.Comment: 7 pages, 2 figures, 2 tables, accepted for publication in PAS

    A novel histone exchange factor, protein phosphatase 2Cγ, mediates the exchange and dephosphorylation of H2A–H2B

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    In eukaryotic nuclei, DNA is wrapped around a protein octamer composed of the core histones H2A, H2B, H3, and H4, forming nucleosomes as the fundamental units of chromatin. The modification and deposition of specific histone variants play key roles in chromatin function. In this study, we established an in vitro system based on permeabilized cells that allows the assembly and exchange of histones in situ. H2A and H2B, each tagged with green fluorescent protein (GFP), are incorporated into euchromatin by exchange independently of DNA replication, and H3.1-GFP is assembled into replicated chromatin, as found in living cells. By purifying the cellular factors that assist in the incorporation of H2A–H2B, we identified protein phosphatase (PP) 2C γ subtype (PP2Cγ/PPM1G) as a histone chaperone that binds to and dephosphorylates H2A–H2B. The disruption of PP2Cγ in chicken DT40 cells increased the sensitivity to caffeine, a reagent that disturbs DNA replication and damage checkpoints, suggesting the involvement of PP2Cγ-mediated histone dephosphorylation and exchange in damage response or checkpoint recovery in higher eukaryotes

    障害を持つ子どもときょうだいを育てる父親の思い

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    【目的】本研究では、障害を持つ子どもときょうだいを育てるにあたっての父親の思いを明らかにすることを目 的とした。 【方法】障害を持つ子どもを含めて2人以上の子どもを持つ父親16名を対象に、自由記述形式の自記式質問紙調 査を行い、Berelson, Bの内容分析を用いて分析した。 【結果】障害を持つ子どもときょうだいを育てる父親の思いとして、「障害を持つ子どもとの関わり方」「子ども を育てる上での教育方針」「「障害をもつ子どもに対して感じること」「きょうだい間に対して感じること」「きょ うだいに対して感じること」「障害を持つ子どもを育てるにあたっての苦労」「障害を持つ子どもの将来への心配」 の7カテゴリが形成された。 【考察】父親の思いは、先行研究に示されている母親の思いと共通する面もあるが、母親に比べ「きょうだい同 じように育てている」という思いが見られるという相違点もあった。また、健常児と同様の期待をしてしまう一 方甘やかしてしまうという葛藤を抱いていることも明らかとなった

    Differences in transient outward currents of feline endocardial and epicardial myocytes.

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    Whole-cell voltage-clamp experiments were performed on enzymatically dissociated single ventricular myocytes harvested from feline endocardial and epicardial surfaces. The studies were designed to test the hypothesis that the differences in the amplitude of transient outward current (Ito) contribute to the difference in action potential configuration between endocardial and epicardial myocytes. In the control state, action potentials recorded from epicardial cells demonstrated a prominent notch between phases 1 and 2, and membrane current recordings displayed a prominent Ito, whereas in endocardial cells the notch in action potentials and Ito were small. External application of 4-aminopyridine (2 mM) reduced the amplitudes of notch and Ito in epicardial cells but not in endocardial cells. After application of 4-aminopyridine (2 mM) and caffeine (5 mM), the notch and Ito were abolished completely in both endocardial and epicardial cells. The first component of Ito (Ito1) was present in all epicardial cells studied (n=20); it was absent in 12 of the 20 endocardial cells, and a small 1to1 was present in the remaining eight endocardial cells. The mean amplitude of Ito1 was significantly greater in epicardial than in endocardial cells. At a test voltage of +80 mV, the amplitude of Ito1 was 102.0±47.7 pA/pF in epicardial cells and 3.3±3.3 pA/pF in endocardial cells (p<0.01). The second component of Ito (Ito2) was present in all endocardial (n=30) and epicardial (n=30) cells studied. The amplitude of Ito2 was significantly greater in epicardial than in endocardial cells. At a test voltage of +60 mV, the amplitude of Ito2 was 10.8±4.1 pA/pF in epicardial cells and 8.1±4.9 pA/pF in endocardial cells (p<0.05). The differential distribution of Ito in endocardial and epicardial myocytes may relate to regional heterogeneity of electrical properties of the heart
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