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  • 1
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    Phonon drag effect on Seebeck coefficient of ultrathin P-doped Si-on-insulator layers (2014)
    American Institute of Physics (AIP)
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    Publication Date: 2014-09-10
    Description: The contribution of the phonon drag effect to the Seebeck coefficient of P-doped ultrathin Si-on-insulator (SOI) layers with a thickness of 9–100 nm is investigated for near-room-temperature applications. The contribution is found to be significant in the lightly doped region and to depend on the carrier concentration with increasing carrier concentration above ∼5 × 10 18  cm −3 . Moreover, the contribution is not influenced by SOI thickness above 9 nm. On the basis of phonon mean-free-path calculations considering phonon scattering processes, the phonon drag part of the SOI Seebeck coefficient in the lightly doped region is mainly governed by phonon-phonon scattering. Furthermore, in higher concentration regions, the dependence of phonon drag can be qualitatively explained by the interaction between phonons and doped impurities.
    Print ISSN: 0003-6951
    Electronic ISSN: 1077-3118
    Topics: Physics
    Published by American Institute of Physics (AIP)
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  • 2
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    Crystal structure of the human centromeric nucleosome containing CENP-A (2011)
    Nature Publishing Group (NPG)
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    Publication Date: 2011-07-12
    Description: In eukaryotes, accurate chromosome segregation during mitosis and meiosis is coordinated by kinetochores, which are unique chromosomal sites for microtubule attachment. Centromeres specify the kinetochore formation sites on individual chromosomes, and are epigenetically marked by the assembly of nucleosomes containing the centromere-specific histone H3 variant, CENP-A. Although the underlying mechanism is unclear, centromere inheritance is probably dictated by the architecture of the centromeric nucleosome. Here we report the crystal structure of the human centromeric nucleosome containing CENP-A and its cognate alpha-satellite DNA derivative (147 base pairs). In the human CENP-A nucleosome, the DNA is wrapped around the histone octamer, consisting of two each of histones H2A, H2B, H4 and CENP-A, in a left-handed orientation. However, unlike the canonical H3 nucleosome, only the central 121 base pairs of the DNA are visible. The thirteen base pairs from both ends of the DNA are invisible in the crystal structure, and the alphaN helix of CENP-A is shorter than that of H3, which is known to be important for the orientation of the DNA ends in the canonical H3 nucleosome. A structural comparison of the CENP-A and H3 nucleosomes revealed that CENP-A contains two extra amino acid residues (Arg 80 and Gly 81) in the loop 1 region, which is completely exposed to the solvent. Mutations of the CENP-A loop 1 residues reduced CENP-A retention at the centromeres in human cells. Therefore, the CENP-A loop 1 may function in stabilizing the centromeric chromatin containing CENP-A, possibly by providing a binding site for trans-acting factors. The structure provides the first atomic-resolution picture of the centromere-specific nucleosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tachiwana, Hiroaki -- Kagawa, Wataru -- Shiga, Tatsuya -- Osakabe, Akihisa -- Miya, Yuta -- Saito, Kengo -- Hayashi-Takanaka, Yoko -- Oda, Takashi -- Sato, Mamoru -- Park, Sam-Yong -- Kimura, Hiroshi -- Kurumizaka, Hitoshi -- England -- Nature. 2011 Jul 10;476(7359):232-5. doi: 10.1038/nature10258.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21743476" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Autoantigens/*chemistry/metabolism ; Base Sequence ; Chromosomal Proteins, Non-Histone/*chemistry/metabolism ; Crystallography, X-Ray ; DNA/*chemistry/genetics/metabolism ; Histones/*chemistry/metabolism ; Humans ; Models, Molecular ; Molecular Conformation ; Molecular Sequence Data ; Nucleosomes/*chemistry/genetics/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Pathogenic exon-trapping by SVA retrotransposon and rescue in Fukuyama muscular dystrophy (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-10-08
    Description: Fukuyama muscular dystrophy (FCMD; MIM253800), one of the most common autosomal recessive disorders in Japan, was the first human disease found to result from ancestral insertion of a SINE-VNTR-Alu (SVA) retrotransposon into a causative gene. In FCMD, the SVA insertion occurs in the 3' untranslated region (UTR) of the fukutin gene. The pathogenic mechanism for FCMD is unknown, and no effective clinical treatments exist. Here we show that aberrant messenger RNA (mRNA) splicing, induced by SVA exon-trapping, underlies the molecular pathogenesis of FCMD. Quantitative mRNA analysis pinpointed a region that was missing from transcripts in patients with FCMD. This region spans part of the 3' end of the fukutin coding region, a proximal part of the 3' UTR and the SVA insertion. Correspondingly, fukutin mRNA transcripts in patients with FCMD and SVA knock-in model mice were shorter than the expected length. Sequence analysis revealed an abnormal splicing event, provoked by a strong acceptor site in SVA and a rare alternative donor site in fukutin exon 10. The resulting product truncates the fukutin carboxy (C) terminus and adds 129 amino acids encoded by the SVA. Introduction of antisense oligonucleotides (AONs) targeting the splice acceptor, the predicted exonic splicing enhancer and the intronic splicing enhancer prevented pathogenic exon-trapping by SVA in cells of patients with FCMD and model mice, rescuing normal fukutin mRNA expression and protein production. AON treatment also restored fukutin functions, including O-glycosylation of alpha-dystroglycan (alpha-DG) and laminin binding by alpha-DG. Moreover, we observe exon-trapping in other SVA insertions associated with disease (hypercholesterolemia, neutral lipid storage disease) and human-specific SVA insertion in a novel gene. Thus, although splicing into SVA is known, we have discovered in human disease a role for SVA-mediated exon-trapping and demonstrated the promise of splicing modulation therapy as the first radical clinical treatment for FCMD and other SVA-mediated diseases.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3412178/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3412178/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taniguchi-Ikeda, Mariko -- Kobayashi, Kazuhiro -- Kanagawa, Motoi -- Yu, Chih-chieh -- Mori, Kouhei -- Oda, Tetsuya -- Kuga, Atsushi -- Kurahashi, Hiroki -- Akman, Hasan O -- DiMauro, Salvatore -- Kaji, Ryuji -- Yokota, Toshifumi -- Takeda, Shin'ichi -- Toda, Tatsushi -- T32 AR056993/AR/NIAMS NIH HHS/ -- England -- Nature. 2011 Oct 5;478(7367):127-31. doi: 10.1038/nature10456.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neurology/Molecular Brain Science, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21979053" target="_blank"〉PubMed〈/a〉
    Keywords: 3' Untranslated Regions/genetics ; Alternative Splicing/drug effects/*genetics ; Animals ; Disease Models, Animal ; Dystroglycans/metabolism ; Exons/*genetics ; Gene Knock-In Techniques ; Glycosylation ; Humans ; Introns/genetics ; Japan ; Laminin/metabolism ; Membrane Proteins/genetics/metabolism ; Mice ; Molecular Sequence Data ; Mutagenesis, Insertional/drug effects/genetics ; Oligonucleotides, Antisense/genetics/pharmacology/therapeutic use ; RNA Isoforms/genetics ; RNA Splice Sites/genetics ; Retroelements/*genetics ; Walker-Warburg Syndrome/*genetics/*pathology/therapy
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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