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  • Mutation  (4)
  • American Association for the Advancement of Science (AAAS)  (4)
  • American Geophysical Union (AGU)
  • 2000-2004  (4)
  • 2004  (4)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (4)
  • American Geophysical Union (AGU)
Years
  • 2000-2004  (4)
Year
  • 1
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    Nucleosome arrays reveal the two-start organization of the chromatin fiber (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-30
    Description: Chromatin folding determines the accessibility of DNA constituting eukaryotic genomes and consequently is profoundly important in the mechanisms of nuclear processes such as gene regulation. Nucleosome arrays compact to form a 30-nanometer chromatin fiber of hitherto disputed structure. Two competing classes of models have been proposed in which nucleosomes are either arranged linearly in a one-start higher order helix or zigzag back and forth in a two-start helix. We analyzed compacted nucleosome arrays stabilized by introduction of disulfide cross-links and show that the chromatin fiber comprises two stacks of nucleosomes in accord with the two-start model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dorigo, Benedetta -- Schalch, Thomas -- Kulangara, Alexandra -- Duda, Sylwia -- Schroeder, Rasmus R -- Richmond, Timothy J -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1571-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eidgenossische Technische Hochschule (ETH) Zurich, Institute for Molecular Biology and Biophysics, ETH-Honggerberg, CH-8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15567867" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatin/*chemistry/ultrastructure ; DNA/chemistry/metabolism ; Electrophoresis, Polyacrylamide Gel ; Histones/chemistry/genetics/metabolism ; Microscopy, Electron ; Models, Biological ; Models, Molecular ; Multiprotein Complexes/chemistry ; Mutation ; Nucleosomes/*chemistry/ultrastructure ; Protein Folding ; Xenopus laevis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Structural basis of mitochondrial tethering by mitofusin complexes (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-07
    Description: Vesicle fusion involves vesicle tethering, docking, and membrane merger. We show that mitofusin, an integral mitochondrial membrane protein, is required on adjacent mitochondria to mediate fusion, which indicates that mitofusin complexes act in trans (that is, between adjacent mitochondria). A heptad repeat region (HR2) mediates mitofusin oligomerization by assembling a dimeric, antiparallel coiled coil. The transmembrane segments are located at opposite ends of the 95 angstrom coiled coil and provide a mechanism for organelle tethering. Consistent with this proposal, truncated mitofusin, in an HR2-dependent manner, causes mitochondria to become apposed with a uniform gap. Our results suggest that HR2 functions as a mitochondrial tether before fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koshiba, Takumi -- Detmer, Scott A -- Kaiser, Jens T -- Chen, Hsiuchen -- McCaffery, J Michael -- Chan, David C -- R01 GM62967/GM/NIGMS NIH HHS/ -- S10 RR019409-01/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2004 Aug 6;305(5685):858-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, 1200 East California Boulevard, MC114-96, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15297672" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cell Line ; Crystallography, X-Ray ; Dimerization ; GTP Phosphohydrolases/*chemistry/*metabolism ; Humans ; Hybrid Cells ; Hydrophobic and Hydrophilic Interactions ; Intracellular Membranes/physiology/ultrastructure ; Membrane Fusion ; Mice ; Mitochondria/*metabolism/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Structure, Secondary ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Biomedicine. Parkinson's--divergent causes, convergent mechanisms (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greenamyre, J Timothy -- Hastings, Teresa G -- New York, N.Y. -- Science. 2004 May 21;304(5674):1120-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Emory University School of Medicine, Atlanta, GA 30322, USA. jgreena@emory.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15155938" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Dopamine/metabolism ; Electron Transport Complex I/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins ; Mitochondria/enzymology/*metabolism ; Mutation ; Nerve Tissue Proteins/genetics/metabolism ; Neurons/metabolism ; Oncogene Proteins/genetics/metabolism ; Oxidative Stress ; Parkinson Disease/*etiology/*genetics/metabolism ; Phosphorylation ; Protein Kinases/*genetics/*metabolism ; Reactive Oxygen Species/metabolism ; Synucleins ; Ubiquitin Thiolesterase/genetics/metabolism ; Ubiquitin-Protein Ligases/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Comment on "Uracil DNA glycosylase activity is dispensable for immunoglobulin class switch" (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stivers, James T -- GM56834-09/GM/NIGMS NIH HHS/ -- R01 GM056834/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2042; author reply 2042.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Johns Hopkins Medical School, 725 North Wolfe Street, Baltimore, MD 21205, USA. jstivers@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604391" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/enzymology/immunology/*physiology ; Catalysis ; DNA/*metabolism ; DNA Damage ; DNA Glycosylases/*metabolism ; DNA Repair ; Humans ; *Immunoglobulin Class Switching ; Mice ; Mutation ; Recombination, Genetic ; Uracil/metabolism ; Uracil-DNA Glycosidase ; Viral Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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