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  • 1
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    Extremely long-lived nuclear pore proteins in the rat brain (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-02-04
    Description: To combat the functional decline of the proteome, cells use the process of protein turnover to replace potentially impaired polypeptides with new functional copies. We found that extremely long-lived proteins (ELLPs) did not turn over in postmitotic cells of the rat central nervous system. These ELLPs were associated with chromatin and the nuclear pore complex, the central transport channels that mediate all molecular trafficking in and out of the nucleus. The longevity of these proteins would be expected to expose them to potentially harmful metabolites, putting them at risk of accumulating damage over extended periods of time. Thus, it is possible that failure to maintain proper levels and functional integrity of ELLPs in nonproliferative cells might contribute to age-related deterioration in cell and tissue function.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3296478/" 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/PMC3296478/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Savas, Jeffrey N -- Toyama, Brandon H -- Xu, Tao -- Yates, John R 3rd -- Hetzer, Martin W -- F32 AG039127/AG/NIA NIH HHS/ -- F32 AG039127-01A1/AG/NIA NIH HHS/ -- F32AG039127/AG/NIA NIH HHS/ -- HHSN268201000035C/PHS HHS/ -- P01 AG031097/AG/NIA NIH HHS/ -- P01 AG031097-03/AG/NIA NIH HHS/ -- P30 CA014195/CA/NCI NIH HHS/ -- P30 CA014195-35/CA/NCI NIH HHS/ -- P41 RR011823/RR/NCRR NIH HHS/ -- P41 RR011823-14/RR/NCRR NIH HHS/ -- R01 MH067880/MH/NIMH NIH HHS/ -- R01 MH067880-08/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2012 Feb 24;335(6071):942. doi: 10.1126/science.1217421. Epub 2012 Feb 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22300851" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/cytology/*metabolism ; Cell Aging ; Chromatin/metabolism ; Female ; Half-Life ; Liver/metabolism ; Mitosis ; Nuclear Pore/*metabolism ; Nuclear Pore Complex Proteins/*metabolism ; Proteome/metabolism ; Rats ; Rats, Sprague-Dawley ; Time Factors
    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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    Nuclear pores form de novo from both sides of the nuclear envelope (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-04-22
    Description: Nuclear pore complexes are multiprotein channels that span the double lipid bilayer of the nuclear envelope. How new pores are inserted into the intact nuclear envelope of proliferating and differentiating eukaryotic cells is unknown. We found that the Nup107-160 complex was incorporated into assembly sites in the nuclear envelope from both the nucleoplasmic and the cytoplasmic sides. Nuclear pore insertion required the generation of Ran guanosine triphosphate in the nuclear and cytoplasmic compartments. Newly formed nuclear pore complexes did not contain structural components of preexisting pores, suggesting that they can form de novo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉D'Angelo, Maximiliano A -- Anderson, Daniel J -- Richard, Erin -- Hetzer, Martin W -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):440-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute for Biological Studies, Molecular and Cell Biology Laboratory, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16627745" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Cell-Free System ; Cytoplasm/metabolism ; Egtazic Acid/analogs & derivatives/pharmacology ; Fluorescent Antibody Technique ; Guanosine Triphosphate/metabolism ; HeLa Cells ; Humans ; Image Processing, Computer-Assisted ; Microscopy, Confocal ; Nuclear Envelope/*metabolism/*ultrastructure ; Nuclear Pore/*metabolism/*ultrastructure ; Nuclear Pore Complex Proteins/*metabolism ; Recombinant Proteins/metabolism ; Wheat Germ Agglutinins/metabolism/pharmacology ; Xenopus ; beta Karyopherins/metabolism/pharmacology ; ran GTP-Binding Protein/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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  • 3
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    The role of the nuclear envelope in cellular organization (2006)
    Springer
    Details
    Publication Date: 2006-01-02
    Print ISSN: 1420-682X
    Electronic ISSN: 1420-9071
    Topics: Biology , Medicine
    Published by Springer
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