1920-30年代GMにおける成長戦略とマーケティング管理の確立 －管理会計とマーケティング管理の統合の視点から

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The effect of "Learning Science" in the teachers training for high school teachers

departmental bulletin pape

「出口調査、世論調査、まだ大丈夫だったか？」〔ディスカッション〕

p45-46 第2部パネルディスカッション表紙textapplication/pdfdepartmental bulletin pape

Observation of the DsJ(2317) and DsJ(2457) in B Decays

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Periodic solutions for evolution equations in Hilbert spaces

application/pdfWe consider the existence of periodic solutions of the problem ＄ g(t, u)￥in＄ ＄u^{￥prime}+Au＄ , where ＄A＄ is a maximal monotone operator defied in a Hilbert space and ＄g＄ : ＄R￥times H￥rightarrow H＄ is a Caratheodory function periodic with respect to the first variable.departmental bulletin pape

C-SBP2 forms highly stable complexes with RNAs containing an extended internal loop

<p><b>Copyright information:</b></p><p>Taken from "An improved definition of the RNA-binding specificity of SECIS-binding protein 2, an essential component of the selenocysteine incorporation machinery"</p><p></p><p>Nucleic Acids Research 2007;35(6):1868-1884.</p><p>Published online 1 Mar 2007</p><p>PMCID:PMC1874613.</p><p>© 2007 The Author(s)</p> The stabilities of the complexes formed between C-SBP2 and Snu13p and the Se1:Ins + loop () and SelN () RNAs were tested by competition experiments. RNA–protein complexes were formed by using 5 fmol of 5′-end labeled Se1:Ins + loop or SelN RNAs and C-SBP2 (300 nM) or Snu13p (1000 or 300 nM). The RNA–protein complexes were challenged with increasing concentrations of cold Se1:Ins + loop or SelN RNAs (10–100 000- and 10–40 000-fold molar excess, respectively, as indicated below the lanes). The remaining complexes were fractionated by gel electrophoresis. () Comparison of the relative stabilities of the Snu13p–SelN and C-SBP2–SelN complexes. RNP complexes formed with C-SBP2 at 300 nM were challenged by addition of an excess of Snu13p protein and vice versa. Complexes formed with Snu13p at 300 nM were challenged by addition of an excess of C-SBP2. The remaining complexes were fractionated by gel electrophoresis. The identities and concentrations of the protein competitors used in the assays are indicated below the lanes

Sequences of the RNAs recovered from the SELEX experiment and test of their affinities for C-SBP2

<p><b>Copyright information:</b></p><p>Taken from "An improved definition of the RNA-binding specificity of SECIS-binding protein 2, an essential component of the selenocysteine incorporation machinery"</p><p></p><p>Nucleic Acids Research 2007;35(6):1868-1884.</p><p>Published online 1 Mar 2007</p><p>PMCID:PMC1874613.</p><p>© 2007 The Author(s)</p> () Alignment of the WT yU3B/C RNA sequence with the degenerated N18 RNA and the selected Se1-Se7 RNAs sequences. Nucleotides in Se1-Se7 RNA, are numbered according to the positions of the homolog nucleotides in the WT yU3B/C RNA. The number of sequenced plasmids encoding each selected RNA is indicated in brackets on the right of the sequences. The nucleotides corresponding to the constant sequence are shown in gray, nucleotides in the degenerated sequence and nucleotides mutated during the RT-PCR cycles are shown in black. The GA dinucleotides are underlined. () The nucleotide sequences of a series of SECIS motifs from various genes and species (,) were aligned with the Se1 RNA sequence taking as references the UGA and GA conserved nucleotides of the K-turn structure (bold characters). A consensus sequence of the SECIS K-turn motifs is deduced from the alignment and indicated below. The positions of the conserved nucleotides in the two strands of helix II are indicated () Estimation of the affinity of C-SBP2 for the Se1, Se2, Se3, Se5 and Se7 RNAs by gel-shift assays. RNA–protein complexes formed with 5 fmol of labeled RNA and increasing concentrations of C-SBP2 (as indicated below the lanes) were fractionated by gel electrophoresis as in . The apparent values are indicated above the autoradiograms

Mutations in helix II of RNA Se1 are more deleterious for C-SBP2 than for Snu13p binding

<p><b>Copyright information:</b></p><p>Taken from "An improved definition of the RNA-binding specificity of SECIS-binding protein 2, an essential component of the selenocysteine incorporation machinery"</p><p></p><p>Nucleic Acids Research 2007;35(6):1868-1884.</p><p>Published online 1 Mar 2007</p><p>PMCID:PMC1874613.</p><p>© 2007 The Author(s)</p> () Positions of base substitutions in the Se1 RNA are represented in gray on the proposed secondary structure. The nature of the mutations in the variant Se1 RNAs is shown on the right of helix II. () The affinities of C-SBP2 and Snu13p for Se1 RNA and its variants were estimated by gel-shift assays using 5′-end labeled RNAs and protein concentrations ranging from 0 to 4000 nM. The apparent values obtained for each of the RNA–protein complexes are indicated

A K-turn motif with an extended internal loop increases C-SBP2 affinity

<p><b>Copyright information:</b></p><p>Taken from "An improved definition of the RNA-binding specificity of SECIS-binding protein 2, an essential component of the selenocysteine incorporation machinery"</p><p></p><p>Nucleic Acids Research 2007;35(6):1868-1884.</p><p>Published online 1 Mar 2007</p><p>PMCID:PMC1874613.</p><p>© 2007 The Author(s)</p> The variant Se1:Ins () and Se1:Ins + loop RNAs ( and ) are shown. The additional residues in these variant RNAs compared to Se1 RNA are shown in gray. The affinities of C-SBP2 and Snu13p for Se1:Ins (A) and Se1:Ins + loop (B) were tested by gel-shift assays. Complex formation was performed as described in , using 5 fmol of 5′-end labeled RNA and increasing concentrations of C-SBP2 or Snu13p proteins. In Panels A and B, the apparent s are indicated above the autoradiograms. () The base substitutions generated at positions 2 and 3 in the internal loop of the Se1:Ins + loop RNA are indicated in gray. The table gives the apparent values established by gel-shift assays for complexes formed between C-SBP2 and the variant Se1:Ins + loop RNAs

The sequence and stability of helix II are important for C-SBP2 binding onto SelN RNA

<p><b>Copyright information:</b></p><p>Taken from "An improved definition of the RNA-binding specificity of SECIS-binding protein 2, an essential component of the selenocysteine incorporation machinery"</p><p></p><p>Nucleic Acids Research 2007;35(6):1868-1884.</p><p>Published online 1 Mar 2007</p><p>PMCID:PMC1874613.</p><p>© 2007 The Author(s)</p> () The base-pair substitutions generated at positions 5, 6 and 7 in helix II of the SelN RNA are shown. (B) Complexes were formed with 5 fmol of radiolabeled WT or mutated SelN RNA and increasing concentrations of the C-SBP2 protein (from 50 to 2000 nM). The RNP complexes were fractionated on 6% polyacrylamide 8–M urea gel and apparent dissociation constants were determined by measuring the radioactivity in the bands of gel corresponding to free RNA and the RNP. The determined s are indicated above each autoradiogram