教員養成における領域「表現」の音楽側面の検討(1) : 幼稚園及び小学校の教師の意識比較<教育科学>

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Observation of D_s1(2536)^+ → D^+π^-K^+ and angular decomposition of D_s1(2536)^+ →D^*+K_S^0

Using 462 fb^{-1} of e^+e^- annihilation data recorded by the Belle detector, we report the first observation of the decay D_s1(2536)^+　→　D+π^-K^+. The ratio of branching fractions \frac{B(D_s1(2536)^+ → D^+π^- K^+}{B(D_s1(2536)^+ → D+K^0}is measured to be (3.27±0.18±0.37)%. We also study the angular distributions in the D_s1(2536)^+　→D*+K_S^0 decay and measure the ratio of D- and S-wave amplitudes. The S-wave dominates, with a partial width of Γ_S/Γtotal=0.72±0.05±0.01.journal articl

Evidence for Direct CP Violation in B0→K+π-Decays

journal articl

Barnabae Brissonii ... De formulis et sollemnibus populi romani verbis, libri VIII.

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The Structure of Abl in an Intermediate Conformation Suggests a Path for the Transition between the Active and Src-Like Conformations

<div><p>(A) The intermediate structure of Abl (molecule E) is shown, with helix αC shown in blue, the activation loop in red, and the catalytic loop containing Arg 362 in orange.</p> <p>(B) The proposed pathway by which Abl makes the transition to the Src-like conformation.</p></div

The Helical Turn following the DFG motif in Src-Like Inactive Structures

<div><p>(A) The helical turn in the activation loop of molecule B that immediately follows the DFG motif is a characteristic feature of the Src-like conformation and is conserved in four different kinase families.</p> <p>(B and C) The side chain of Arg 386, presented by the helical turn, forms a hydrogen bond to a backbone carbonyl of Ile 360, a salt bridge with Glu 286, and an amino–aromatic interaction with Phe 359 that positions it for interacting with Asp 381 during the DFG flip.</p> <p>(D) An intermediate structure during one of the TMD simulations, showing the capture of Asp 381 by Arg 386.</p></div

Distinct States of the c-Abl and c-Src Kinase Domains

<div><p>Three key kinase domain conformations considered at length in the text are shown in (A–C). At the top, a schematic representation of each state and an enlarged schematic are shown, detailing the conformations of the DFG motif (red) and helix αC (blue). Below the schematics the crystal structure of each conformation is shown. The activation loop is colored red, helix αC blue, and the catalytic loop orange.</p> <p>(A) The conformation of inactive c-Abl, bound to imatinib (molecule A).</p> <p>(B) The conformation of the inactive Src family kinases. This conformation is now seen in Abl as well (molecule B, structure 1). Both the c-Src and Abl numbering are indicated.</p> <p>(C) Active Abl (molecule C, structure 2).</p> <p>(D) In cells the active conformation of Abl undergoes rapid autophosphorylation that is expected to trap the protein in the active conformation (indicated as C*). Similarly, imatinib only binds to Abl when the kinase domain adopts conformation A and forms a stable complex with the protein (A*). The interconversion between the different states of Abl is shown in the context of this competition.</p></div

Molecule B Helps Explain Mutations in the Kinase Domain of Abl That Confer Resistance to Imatinib

<div><p>(A) The side chains of residues implicated in imatinib resistance in the Azam et al. study [<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040144#pbio-0040144-b048" target="_blank">48</a>] are shown in blue in the context of molecule B. A large number of these mutations cluster in the interface between helix αC, the N-lobe, and the helical turn in the activation loop. </p> <p>(B–D) For three of these mutations we have shown the surface for all atoms within 6 Å of the mutated residue in the context of different structures. The Abl:imatinib complex is in green and the Src-like structure (molecule B) in yellow-orange. (B) Asp 276. (C) Leu 387. (D) Met 278.</p></div

Molecule B Closely Resembles the Structure of the Inactive Src Kinases

<div><p>(A) The kinase domain of Abl (molecule B) is shown as a cartoon with the bisubstrate analog inhibitor depicted as a stick model.</p> <p>(B) Structure of the ATP–peptide conjugate at the active site.</p> <p>(C) Comparison between molecule B (left) and the structure of a Src-family kinase (right).</p> <p>(D) Backbone torsion angles of Asp 381 of the DFG motif.</p> <p>(E) The backbone of Asp 381 can start to move from DFG-In to the DFG-Out conformations by three paths in torsion angle space [<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040144#pbio-0040144-b032" target="_blank">32</a>]. </p> <p>(F) Illustration of rotations about φ(Asp 381) and ψ(Asp 381) in the Src-like inactive versus the active structures of Abl.</p></div

Targeted Molecular Dynamics Simulations Suggest a Path for DFG Flipping

<div><p>(A) Coordination of Asp 381 during the DFG flip, shown in stereo, starting from the Src-like structure and following transition path A in backbone torsion angle space (see <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040144#pbio-0040144-g002" target="_blank">Figure 2</a>E). The coordination of Asp 381 is almost identical for transition path B, except that the carbonyl of Asp 381 flips in the other direction (see <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040144#sg003" target="_blank">Figure S3</a>). </p> <p>(B) The side chain of Phe 382 passing through a hydrophobic pocket in the Src-like inactive molecule B.</p> <p>(C) The paths of Asp 381 and Phe 382 in backbone torsion angle space for two trajectories starting with the Src-like inactive structure. Shown in red are the torsion angles seen in the first quarter of a TMD time series, in green, the second quarter of the time series, in blue, the third quarter, and in purple, the last quarter.</p> <p>(D) Unfavorable interactions between the backbone carbonyl of Phe 382 and the carboxylate group of Glu 286 during TMD simulations starting from the active structure, where the Glu 286-Lys 271 salt bridge is present.</p></div