일본어 학슥자의‘no’의 탈락에 괸한 일고

본　연구에서는　한･중･영3가지　언어런을　대상으로　한　오쿠노･유키코(2005)의　방법론을　채택하여　발화자료에　나타나는　‘no’의　탈락　오류를분석하였다．‘no'의　탈락　오류가　다연한　언어권의　작문자료에　나타나는　점은　이미　보고된　바　있으나　본　연구를　통해　추가적으로　발화　자료에　있어서도　다양한　학습레벨，다양한　모어화자에　있어　유사한　현상이　나타남으로써　‘no’의　탈락이　모어에　무관하게　나타나는　오류임이　규명되었다．그　요인으로　‘복합화’와　‘바꿔낳기　전략’이　제시되었으며，선행연구의　문제점을　보완하여　학습레벨을　통제한　결과　‘no’의　탈락오류가　상급에서는　영어권　학습가에　비해　중국어권　학습가와　한국어권　학습가에게　나타나기　쉬운　점과　대조연구의　관점에서　언어전이의　가능성을　배제하기　어려운　점이　제시되었다．departmental bulletin pape

Search for \bar{B}^0 →Λ_c^+\bar{Λ}_c^- decay at Belle

We search for the doubly charmed baryonic decay \bar{B}^0 →Λ_c^+\bar{Λ}_c^-, in a data sample of 520×106 B\bar{B} events accumulated at the Υ(4S) resonance with the Belle detector at the KEKB asymmetric-energy e^+e^- collider. We find no significant signal and set an upper limit of B(\bar{B}^0 →Λ_c^+\bar{Λ}_c^-)< 6.2×10^{-5} at 90% confidence level. The result is significantly below a naive extrapolation from B(B^-→　Ξ\begin0\c\end\bar{Λ}_c^-) assuming a simple Cabibbo-suppression factor of |V_cd/V_cs|^2. The small branching fraction may be attributed to a suppression due to the large momentum of the baryonic decay products, which has been observed in other charmed baryonic two-body B decays.journal articl

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

journal articl

Influence of substitutions at the conserved aromatic amino acid residues around the active site of ExoIII

<p><b>Copyright information:</b></p><p>Taken from "Role of the tryptophan residue in the vicinity of the catalytic center of exonuclease III family AP endonucleases: AP site recognition mechanism"</p><p>Nucleic Acids Research 2006;34(5):1552-1563.</p><p>Published online 15 Mar 2006</p><p>PMCID:PMC1408312.</p><p>© The Author 2006. Published by Oxford University Press. All rights reserved</p> () Detection of products of cleavage by ExoIII and its mutant proteins. Proteins used in each reaction are shown above each lane. The oligonucleotide containing an AP site (AP-ssDNA) was d-GCGATGACTAACGTACTAGGCTTCCGAGCC. AP-dsDNA was constructed by annealing AP-ssDNA and d-CGGAAGCCTAGTATCGTTAGTCATCGCCATG. The substrate DNA (4.4 pmol), in which the oligonucleotide containing an AP site was 5′ P-labeled, was incubated with the wild-type ExoIII or its mutant (0.04 pmol) in buffer containing 75 mM NaCl, 5 mM MgCl, 10 mM DTT and 65 mM Tris–HCl (pH 8.0) at 23°C. The DNA products were analyzed using a 20% denaturing (7 M urea) polyacrylamide gel. The product 1 was produced by AP endonucleolytic cleavage at the 5′ side of the AP site. The product 2 was produced by exonucleolytic cleavage from 3′ end of the product 1. The markers were 5′ P-labeled d-GCGATGACTAACG. () Abilities of ExoIII and its mutant proteins to bind the dsDNA containing an AP site. The proteins used in each reaction are shown above each lane. AP-dsDNA (0.45 pmol), in which the oligonucleotide containing an AP site was 5′ P-labeled, was incubated with the wild-type ExoIII or its mutant (4.5 pmol) in buffer containing 77 mM NaCl, 10 mM EDTA and 66 mM Tris–HCl (pH 8.3) at 4°C. The protein–DNA complex was analyzed by 15% native polyacrylamide gel electrophoresis

Effects of translocating the tryptophan residue protruding from the surface of the APE1 active site

<p><b>Copyright information:</b></p><p>Taken from "Role of the tryptophan residue in the vicinity of the catalytic center of exonuclease III family AP endonucleases: AP site recognition mechanism"</p><p>Nucleic Acids Research 2006;34(5):1552-1563.</p><p>Published online 15 Mar 2006</p><p>PMCID:PMC1408312.</p><p>© The Author 2006. Published by Oxford University Press. All rights reserved</p> () Detection of AP endonucleolytic activity of APE1 mutants. DNA substrate (AP-dsDNA: 4.4 pmol), in which the oligonucleotide containing an AP site was 5′ P-labeled, was incubated with the wild-type APE1 or its mutant (0.04 pmol). The DNA products were analyzed using a 20% denaturing polyacrylamide gel. () Ability of APE1 mutants to form a complex with the dsDNA containing an AP site. AP-dsDNA (0.45 pmol) was incubated with the wild-type APE1 or its mutant (4.5 pmol). The protein–DNA complexes were analyzed using a 15% native polyacrylamide gel

Effect of tryptophan residues on interaction between peptides and double-stranded oligonucleotides containing AP sites or not

<p><b>Copyright information:</b></p><p>Taken from "Role of the tryptophan residue in the vicinity of the catalytic center of exonuclease III family AP endonucleases: AP site recognition mechanism"</p><p>Nucleic Acids Research 2006;34(5):1552-1563.</p><p>Published online 15 Mar 2006</p><p>PMCID:PMC1408312.</p><p>© The Author 2006. Published by Oxford University Press. All rights reserved</p> () SPR analyses of the interaction between a peptide containing a tryptophan residue (11KWK, solid line) or not (11KAK, dashed line) and dsDNA not containing an AP site. The amount of immobilized oligonucleotides not containing AP sites (3Native-dsDNA) was 1515 RU. For all the sensorgrams, the injection point was set as the zero time and the baseline prior to the injection was set to zero RU. The 11KWK and 11KAK oligopeptides were KSRGKKGRSA and KSRGKKGRSK, respectively. () SPR analyses of the interaction between a peptide containing a tryptophan residue (11KWK, solid line) or not (11KAK, dashed line) and dsDNA containing three AP sites. The amount of immobilized oligonucleotide containing three AP sites (3AP-dsDNA) was 1500 RU. This analysis was carried out under the same experimental conditions as in (A), except for the immobilized oligonucleotide. () Fluorescence spectra of the peptide containing a tryptophan residue in the presence or absence of dsDNA containing an AP site. AP-dsDNA was the substrate used in the AP endonuclease assay (). The DNA sequences of AP-dsDNA and Native-dsDNA were the same excluding the presence of an AP site. Peptide and dsDNA were mixed at a molar ratio of 1:10. The excitation wavelength was 275 nm

Sensorgrams for the binding of APE1 and its mutants to single- or double-stranded DNA containing AP sites

<p><b>Copyright information:</b></p><p>Taken from "Role of the tryptophan residue in the vicinity of the catalytic center of exonuclease III family AP endonucleases: AP site recognition mechanism"</p><p>Nucleic Acids Research 2006;34(5):1552-1563.</p><p>Published online 15 Mar 2006</p><p>PMCID:PMC1408312.</p><p>© The Author 2006. Published by Oxford University Press. All rights reserved</p> The Overlay of sensorgrams represents interactions of the wild-type APE1 and mutant proteins with immobilized dsDNA (1620 RU) containing AP sites (), and immobilized ssDNA (989 RU) containing AP sites (). There were three AP sites in the immobilized single-stranded oligonucleotide (3AP-ssDNA). The immobilized double-stranded oligonucleotide containing three AP sites (3AP-dsDNA) was prepared by annealing 3AP-ssDNA and its complementary strand. The flow rate of the enzyme solution was 20 µl/min. Association and dissociation phases were both taken as 120 s each. For all the sensorgrams, the injection point was set as the zero time and the baseline prior to the injection was set to zero RU

Effects of translocating the tryptophan residue protruding from the surface of the ExoIII active site

<p><b>Copyright information:</b></p><p>Taken from "Role of the tryptophan residue in the vicinity of the catalytic center of exonuclease III family AP endonucleases: AP site recognition mechanism"</p><p>Nucleic Acids Research 2006;34(5):1552-1563.</p><p>Published online 15 Mar 2006</p><p>PMCID:PMC1408312.</p><p>© The Author 2006. Published by Oxford University Press. All rights reserved</p> () Detection of AP endonucleolytic activity of ExoIII mutants. DNA substrate (AP-dsDNA: 4.4 pmol), in which the oligonucleotide containing an AP site was 5′ P-labeled, was incubated with the wild-type ExoIII or its mutant (0.04 pmol). The DNA products were analyzed using a 20% denaturing polyacrylamide gel. () Binding of ExoIII mutants to the dsDNA containing an AP site (AP-dsDNA). AP-dsDNA (0.45 pmol) was incubated with the wild-type ExoIII or its mutants (4.5 pmol). The protein–DNA complex was analyzed using a 15% polyacrylamide gel

Influence of substitutions of the aromatic amino acid residues around the active site of human APE1

<p><b>Copyright information:</b></p><p>Taken from "Role of the tryptophan residue in the vicinity of the catalytic center of exonuclease III family AP endonucleases: AP site recognition mechanism"</p><p>Nucleic Acids Research 2006;34(5):1552-1563.</p><p>Published online 15 Mar 2006</p><p>PMCID:PMC1408312.</p><p>© The Author 2006. Published by Oxford University Press. All rights reserved</p> () Detection of products of cleavage by wild-type APE1 and its mutant proteins. Substrate DNA (AP-dsDNA: 4.4 pmol), in which the oligonucleotide containing an AP site was 5′ P-labeled, was incubated with the wild-type APE1 or its mutant (0.04 pmol). The DNA products were analyzed by 20% denaturing polyacrylamide gel electrophoresis. () Binding of APE1 and its mutant proteins to the dsDNA containing an AP site (AP-dsDNA). AP-dsDNA (0.45 pmol) was incubated with the wild-type APE1 or its mutants (4.5 pmol). Protein–DNA complex was analyzed by 15% native polyacrylamide gel electrophoresis

The interaction of double-stranded DNA and ExoIII family AP endonuclease

<p><b>Copyright information:</b></p><p>Taken from "Role of the tryptophan residue in the vicinity of the catalytic center of exonuclease III family AP endonucleases: AP site recognition mechanism"</p><p>Nucleic Acids Research 2006;34(5):1552-1563.</p><p>Published online 15 Mar 2006</p><p>PMCID:PMC1408312.</p><p>© The Author 2006. Published by Oxford University Press. All rights reserved</p> A model for recognition of an AP site by the ExoIII family AP endonuclease. () Unbound forms of dsDNA containing an AP site (PDB ID: 1A9I) and human APE1 (PDB ID: 1BIX). The negative charge of the substrate DNA attracts the positively charged region of the enzyme. () An AP site recognition complex. When AP endonuclease encounters an AP site, the tryptophan residue in the vicinity of the catalytic site intercalates into an AP site pocket as an AP site ‘recognizer’. This recognition complex would immediately change into a reaction complex. () A cleavage reaction complex (PDB ID: 1DEW). To cleave on the 5′ side of the AP site, an abasic ribose ring is flipped out from the duplex interior and accommodated into a catalytic pocket with DNA kinking at the AP site