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  • Articles  (2)
  • American Association for the Advancement of Science (AAAS)  (2)
  • American Geophysical Union
  • Institute of Physics (IOP)
  • International Union of Crystallography (IUCr)
  • 2005-2009  (2)
  • 1
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    Synaptic protein degradation underlies destabilization of retrieved fear memory (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-02-09
    Description: Reactivated memory undergoes a rebuilding process that depends on de novo protein synthesis. This suggests that retrieval is dynamic and serves to incorporate new information into preexisting memories. However, little is known about whether or not protein degradation is involved in the reorganization of retrieved memory. We found that postsynaptic proteins were degraded in the hippocampus by polyubiquitination after retrieval of contextual fear memory. Moreover, the infusion of proteasome inhibitor into the CA1 region immediately after retrieval prevented anisomycin-induced memory impairment, as well as the extinction of fear memory. This suggests that ubiquitin- and proteasome-dependent protein degradation underlies destabilization processes after fear memory retrieval. It also provides strong evidence for the existence of reorganization processes whereby preexisting memory is disrupted by protein degradation, and updated memory is reconsolidated by protein synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Sue-Hyun -- Choi, Jun-Hyeok -- Lee, Nuribalhae -- Lee, Hye-Ryeon -- Kim, Jae-Ick -- Yu, Nam-Kyung -- Choi, Sun-Lim -- Lee, Seung-Hee -- Kim, Hyoung -- Kaang, Bong-Kiun -- New York, N.Y. -- Science. 2008 Feb 29;319(5867):1253-6. doi: 10.1126/science.1150541. Epub 2008 Feb 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Creative Research Initiative Center for Memory, Department of Biological Sciences, College of Natural Sciences, Seoul National University, San 56-1 Silim-dong, Gwanak-gu, Seoul 151-747, Korea.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18258863" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anisomycin/pharmacology ; Conditioning (Psychology) ; Extinction, Psychological ; *Fear ; Hippocampus/drug effects/*metabolism ; Lactones/pharmacology ; Male ; *Memory ; *Mental Recall ; Mice ; Mice, Inbred C57BL ; Nerve Tissue Proteins/*metabolism ; Proteasome Endopeptidase Complex/metabolism ; Protein Synthesis Inhibitors/pharmacology ; Synapses/*metabolism ; Ubiquitination
    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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    Itinerant ferromagnetism in a Fermi gas of ultracold atoms (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-09-19
    Description: Can a gas of spin-up and spin-down fermions become ferromagnetic because of repulsive interactions? We addressed this question, for which there is not yet a definitive theoretical answer, in an experiment with an ultracold two-component Fermi gas. The observation of nonmonotonic behavior of lifetime, kinetic energy, and size for increasing repulsive interactions provides strong evidence for a phase transition to a ferromagnetic state. Our observations imply that itinerant ferromagnetism of delocalized fermions is possible without lattice and band structure, and our data validate the most basic model for ferromagnetism introduced by Stoner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jo, Gyu-Boong -- Lee, Ye-Ryoung -- Choi, Jae-Hoon -- Christensen, Caleb A -- Kim, Tony H -- Thywissen, Joseph H -- Pritchard, David E -- Ketterle, Wolfgang -- New York, N.Y. -- Science. 2009 Sep 18;325(5947):1521-4. doi: 10.1126/science.1177112.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Massachusetts Institute of Technology-Harvard Center for Ultracold Atoms, Research Laboratory of Electronics, Department of Physics, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. gyuboong@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19762638" target="_blank"〉PubMed〈/a〉
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
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