Survey on use of personal pronoun "imo" in Manyoshu

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マンヨウシュウ アキ ノ オオキミ ノ ウタ カン4 534 オ メグル モンダイ : ツマ ト イモ ガ ヘイゾン スル アリカタ

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Effect of encapsulated atoms on the electronic structure of the fullerene cage: A case study on La2@C78 and Ti2C2@C78 via ultraviolet photoelectron spectroscopy

Ultraviolet photoelectron spectra (UPS) of metallofullerene, La2@C78 were measured using a synchrotronradiation light source. Its spectral onset energy was 0.70 eV below the Fermi level, indicating the semiconductive nature of this metallofullerene. The UPS consisted of numerous crests and troughs. Further, a change in intensity upon tuning the excitation energy was observed; however, the intensity of the change was not as large as those observed for other fullerenes. The UPS of La2@C78 differ considerably from those of Ti2C2@C78, although they are thought to have the same cage structure. Herein, this difference is explored using density-functional theory, and the origin of this difference was determined to be the hybridization of the π-electron wave functions.journal articl

'uchiwaezukushi'

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当科でのシスプラチン十タキソテール併用化学療法の経験

当科では平成10年5月から約4年間に臨床病期Ⅲ、Ⅳ期の非小細胞肺癌11例(平均58歳、組織型:腺癌6例、肩平上皮癌4例、未分癌1例)にシスプラチン+タキソテール併用化学療法を合計18コース施行した。ⅢA、ⅢB期の4例は根治照射を併用した。11例の奏効率は25%、生存期間中央値45週、1年生存率40%、2年生存率11%であった。化学療法単独の7例では生存期間中央値19週、1年生存率28%、2年生存率14%であった。有害事象ではGrade3の食欲不振が6%、白血球減少、好中球減少が22%に認められた。journal articl

Rod-derived Cone Viability Factor-2 is a novel bifunctional-thioredoxin-like protein with therapeutic potential-0

<p><b>Copyright information:</b></p><p>Taken from "Rod-derived Cone Viability Factor-2 is a novel bifunctional-thioredoxin-like protein with therapeutic potential"</p><p>http://www.biomedcentral.com/1471-2199/8/74</p><p>BMC Molecular Biology 2007;8():74-74.</p><p>Published online 31 Aug 2007</p><p>PMCID:PMC2064930.</p><p></p>romosome 8, minus strand, from 70'033'763 to 70'027'717) is composed of three exons (1–3) of 348, 687 and 1751 bp. The RdCVF-S mRNA (BC017153, from 70'033'785 to 70'032'615) is composed of one exon (1172 bp). The RdCVF2-L mRNA (AK015847, mouse chromosome 13, plus strand, from 50'202'630 to 50'206'797) is composed of two exons (1–2) of 603 and 564 bp. The RdCVF2-S mRNA (BC016199, from 50'202'667 to 50'205'571) is composed of one exon (2904 bp). Coding and non-coding regions are depicted in dark grey) and light grey respectively. At middle, panels a and b, the genomic region surrounding the stop codon at the end of the first coding exon and the corresponding orthologous sequences in 12 other vertebrate genomes are aligned. The black triangles indicate the end of the first RdCVF(2)-L coding exon. Conserved stop codons are colored in red. At bottom, panels a and b, lengths of the coding (CDS) and terminal untranslated regions (UTR) are given

Improving Learners' Communicative Competence : Towards Continuity between Elementary School Foreign Language Activities and Junior High School English Classes

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Rod-derived Cone Viability Factor-2 is a novel bifunctional-thioredoxin-like protein with therapeutic potential-1

<p><b>Copyright information:</b></p><p>Taken from "Rod-derived Cone Viability Factor-2 is a novel bifunctional-thioredoxin-like protein with therapeutic potential"</p><p>http://www.biomedcentral.com/1471-2199/8/74</p><p>BMC Molecular Biology 2007;8():74-74.</p><p>Published online 31 Aug 2007</p><p>PMCID:PMC2064930.</p><p></p> and the existing and predicted RdCVF and RdCVF2 proteins. The name, organism and accession number (in brackets) of each protein sequence are given (left). Identical (white text on black) small (A, D, G, P, S, T ; white text on green) hydrophobic (A, C, F, G, I, L, M, S, T, V, W, Y ; black text on yellow) polar (D, E, H, K, N, Q, R, S ; blue text) and charged (D, E, K, R ; white text on red) conserved residues are shown according to a conservation threshold of 85%. A consensus sequence is given below the multiple alignment in which s, h, p and c correspond to small, hydrophobic, polar and charged residues respectively. The secondary structures (β sheet and α helix) of the Crithidia fasciculata tryparedoxin I structure (1EWX) are given below the consensus sequence. The blue dashed rectangles indicate the three RdCVF(2) specific insertions. The green dashed rectangle shows the "cap" region absent in RdCVF(2)-S. The position of the human thioredoxin cleavage product (TRX80) is indicated (red triangle). Panel b displays the structure of the TRYX-I (1EWX) (left) mouse RdCVF-L (center) and mouse RdCVF2-L (right) models. Regions of TRYX-I backbone conserved in RdCVF(2)-L are colored in red. The "cap" region and the three specific insertions are depicted in green and blue respectively. The putative catalytic site (CXXC) is shown in yellow with a space-filling representation

P23H mutated mouse transgene variations.

<p>P23H mutated mouse transgene variations.</p