archive-com.com » COM » C » CELL-RESEARCH.COM

Total: 1754

Choose link from "Titles, links and description words view":

Or switch to "Titles and links view".
  • Cell Research
    2 Ming Pei 4 and Mo Fang Liu 1 2 1 Center for RNA Research State Key Laboratory of Molecular Biology University of Chinese Academy of Sciences Shanghai 200031 China 2 Shanghai Key Laboratory of Molecular Andrology Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences Shanghai 200031 China 3 Department of General Surgery Zhongshan Hospital Fudan University Shanghai 200032 China 4 Shanghai Qibao

    Original URL path: http://www.cell-research.com/arts.asp?id=1889 (2016-02-14)
    Open archived version from archive


  • Cell Research

    (No additional info available in detailed archive for this subpage)
    Original URL path: /artsmore1.asp?id=166 (2016-02-14)


  • Cell Research
    University Munich 82152 Planegg Martinsried Germany 2 Molecular Biology Unit Adolf Butenandt Institute Center for Integrated Protein Science Munich CIPSM Ludwig Maximilians University Munich 80336 Munich Germany Correspondence Heinrich Leonhardt Tel 49 89 2180 74232 Fax 49 89 2180 74236 E mail h leonhardt lmu de Sandra B Hake Tel 49 89 2180 75435 Fax 49 89 2180 75425 E mail sandra hake med uni muenchen de Chemical modifications of

    Original URL path: http://www.cell-research.com/arts.asp?id=1891 (2016-02-14)
    Open archived version from archive

  • Cell Research
    2014 263 264 Where long noncoding RNAs meet DNA methylation FREE Fan Lai 1 and Ramin Shiekhattar 1 1 Wistar Institute Philadelphia PA 19104 USA Correspondence Ramin Shiekhattar E mail Shiekhattar wistar org DNA methylation is a fundamental epigenetic mechanism governing regulation of gene expression during mammalian development A recent study published in Nature shows a novel long noncoding RNA lncRNA arising from the CEBPA gene locus termed ecCEBPA that

    Original URL path: http://www.cell-research.com/arts.asp?id=1892 (2016-02-14)
    Open archived version from archive

  • Cell Research
    to be or not to be FREE Felix Wertek 1 2 and Chenqi Xu 1 1 National Center for Protein Science Shanghai State Key Laboratory of Molecular Biology Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences Shanghai 200031 China 2 University of Heidelberg Institute of Pharmacy and Molecular Biotechnology 69120 Heidelberg Germany Correspondence Chenqi Xu E mail cqxu sibcb ac cn A recent

    Original URL path: http://www.cell-research.com/arts.asp?id=1893 (2016-02-14)
    Open archived version from archive

  • Cell Research
    University Beijing 100084 China 2 Department of Pharmacology and Pharmaceutical Sciences School of Medicine Tsinghua University Beijing 100084 China 3 Humboldt Universität zu Berlin Institut für Biologie Mikrobiologie 10115 Berlin Germany 4 Department of Chemistry Tsinghua University Beijing 100084 China 5 Shanghai Synchrotron Radiation Facilities Shanghai Institute of Applied Physics Chinese Academy of Sciences Shanghai 201204 China Correspondence Maojun Yang E mail maojunyang tsinghua edu cn Tel 86 10 6278 9400 Fax 86 10 6279 2736 Thomas Eitinger E mail thomas eitinger cms hu berlin de Tel 49 30 2093 8103 Fax 49 30 2093 8102 Jun Li Tel 86 10 6279 5381 Fax E mail junli tsinghua edu cn The energy coupling factor ECF transporters are multi subunit protein complexes that mediate uptake of transition metal ions and vitamins in about 50 of the prokaryotes including bacteria and archaea Biological and structural studies have been focused on ECF transporters for vitamins but the molecular mechanism by which ECF systems transport metal ions from the environment remains unknown Here we report the first crystal structure of a NikM TtNikM2 the substrate binding component S component of an ECF type nickel transporter from Thermoanaerobacter tengcongensis In contrast to the structures of the vitamin specific S proteins with six transmembrane segments TSs TtNikM2 possesses an additional TS at its N terminal region resulting in an extracellular N terminus The highly conserved N terminal loop inserts into the center of TtNikM2 and occludes a region corresponding to the substrate binding sites of the vitamin specific S components Nickel binds to NikM via its coordination to four nitrogen atoms which are derived from Met1 His2 and His67 residues These nitrogen atoms form an approximately square planar geometry similar to that of the metal ion binding sites in the amino terminal Cu2 and Ni2 binding

    Original URL path: http://www.cell-research.com/arts.asp?id=1894 (2016-02-14)
    Open archived version from archive

  • Cell Research
    Sciences Icahn School of Medicine at Mount Sinai One Gustave L Levy Place Box 1040 New York NY 10029 USA 2 Institute for Genomics and Multiscale Biology Icahn School of Medicine at Mount Sinai One Gustave L Levy Place New York NY 10029 USA 3 Cardiovascular Institute Icahn School of Medicine at Mount Sinai One Gustave L Levy Place New York NY 10029 USA 4 Pharmacology and Systems Therapeutics Icahn School of Medicine at Mount Sinai One Gustave L Levy Place New York NY 10029 USA 5 Current address College of Life Sciences Peking University Beijing 100871 China Correspondence Yong Zhao Tel 1 212 824 8916 Fax 1 212 241 3310 E mail yong zhao mssm edu miRNAs are an important class of regulators that play roles in cellular homeostasis and disease Muscle specific miRNAs miR 1 1 and miR 1 2 have been found to play important roles in regulating cell proliferation and cardiac function Redundancy between miR 1 1 and miR 1 2 has previously impeded a full understanding of their roles in vivo To determine how miR 1s regulate cardiac function in vivo we generated mice lacking miR 1 1 and miR 1 2 without affecting nearby genes miR 1 double knockout miR 1 dKO mice were viable and not significantly different from wild type controls at postnatal day 2 5 Thereafter all miR 1 dKO mice developed dilated cardiomyopathy DCM and died before P17 Massively parallel sequencing showed that a large portion of upregulated genes after deletion of miR 1s is associated with the cardiac fetal gene program including cell proliferation glycolysis glycogenesis and fetal sarcomere associated genes Consistent with gene profiling glycogen content and glycolytic rates were significantly increased in miR 1 dKO mice Estrogen related Receptor β Errβ was identified as a direct target

    Original URL path: http://www.cell-research.com/arts.asp?id=1895 (2016-02-14)
    Open archived version from archive

  • Cell Research
    Tan 1 Tao Cheng 3 Tao Cai 2 Shaorong Gao 2 and Jianhui Tian 1 1 Ministry of Agriculture Key Laboratory of Animal Genetics Breeding and Reproduction National Engineering Laboratory for Animal Breeding College of Animal Sciences and Technology China Agricultural University 2 Yuanmingyuan West Road Haidian District Beijing 100193 China 2 National Institute of Biological Sciences 7 Science Park Road Zhongguancun Life Science Park Beijing 102206 China 3 State Key Laboratory of Experimental Hematology Institute of Hematology and Blood Diseases Hospital Chinese Academy of Medical Sciences and Peking Union Medical College Nanjing Road Tianjin 300020 China Correspondence Jianhui Tian Tel 86 10 62896057 Fax 86 10 62733856 E mail tianjh cau edu cn Shaorong Gao Tel 86 10 80728967 Fax 86 10 80727535 E mail gaoshaorong nibs ac cn It remains controversial whether the abnormal epigenetic modifications accumulated in the induced pluripotent stem cells iPSCs can ultimately affect iPSC pluripotency To probe this question iPSC lines with the same genetic background and proviral integration sites were established and the pluripotency state of each iPSC line was characterized using tetraploid 4N complementation assay Subsequently gene expression and global epigenetic modifications of 4N ON and the corresponding 4N OFF iPSC lines

    Original URL path: http://www.cell-research.com/arts.asp?id=1896 (2016-02-14)
    Open archived version from archive



  •