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  • 1
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    ALS-linked TDP-43 mutations produce aberrant RNA [Neuroscience] (2013)
    National Academy of Sciences
    Details
    Publication Date: 2013-02-20
    Description: Transactivating response region DNA binding protein (TDP-43) is the major protein component of ubiquitinated inclusions found in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD) with ubiquitinated inclusions. Two ALS-causing mutants (TDP-43Q331K and TDP-43M337V), but not wild-type human TDP-43, are shown here to provoke age-dependent, mutant-dependent, progressive motor axon...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 2
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    Toxicity of ALS-linked SOD1 mutants (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williamson, T L -- Corson, L B -- Huang, L -- Burlingame, A -- Liu, J -- Bruijn, L I -- Cleveland, D W -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):399.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, University of California at San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10798964" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/*enzymology/genetics/pathology ; Animals ; Apoptosis ; Cells, Cultured ; Copper/metabolism ; Humans ; Mice ; Motor Neurons/metabolism/*pathology ; Mutation ; Neurofilament Proteins/metabolism ; Nitrates/metabolism ; Superoxide Dismutase/*genetics/*metabolism ; Yeasts/cytology/metabolism ; Zinc/*metabolism/toxicity
    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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    Cell cycle. Some importin news about spindle assembly (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kahana, J A -- Cleveland, D W -- New York, N.Y. -- Science. 2001 Mar 2;291(5509):1718-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, University of California at San Diego, La Jolla, CA 92093-0670, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11253198" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Cell Compartmentation ; *Cell Cycle Proteins ; Cell Nucleus/*metabolism ; Centrosome/metabolism ; Chromatin/metabolism ; Cytoplasm/metabolism ; DNA-Binding Proteins/metabolism ; *Guanine Nucleotide Exchange Factors ; Interphase ; Karyopherins ; Meiosis ; Microtubule-Associated Proteins/metabolism ; Microtubules/*metabolism ; Mitosis ; *Neoplasm Proteins ; Nuclear Envelope/metabolism ; Nuclear Proteins/*metabolism ; *Phosphoproteins ; Spindle Apparatus/*metabolism ; Xenopus ; *Xenopus Proteins ; 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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  • 4
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    Motor neuron disease: The curious ways of ALS (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-07-18
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3625042/" 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/PMC3625042/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Polymenidou, Magdalini -- Cleveland, Don W -- R37 NS027036/NS/NINDS NIH HHS/ -- England -- Nature. 2008 Jul 17;454(7202):284-5. doi: 10.1038/454284a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18633404" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/enzymology/genetics/*physiopathology ; Animals ; Humans ; Membrane Proteins/metabolism ; Mice ; Mitochondria/metabolism ; Motor Neurons/pathology ; Mutation ; Superoxide Dismutase/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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  • 5
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    Forensic DNA typing (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-02-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cleveland, D W -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1052; author reply 1052-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546301" target="_blank"〉PubMed〈/a〉
    Keywords: DNA Fingerprinting/*methods ; Forensic Medicine/*methods ; Humans ; Publishing/standards
    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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  • 6
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    Comment on "A centrosome-independent role for gamma-TuRC proteins in the spindle assembly checkpoint" (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-05-19
    Description: Muller et al. (Reports, 27 October 2006, p. 654) proposed a role for microtubule nucleation in mitotic checkpoint signaling. However, their observations of spindle defects and mitotic delay after depletion of gamma-tubulin ring complex (gamma-TuRC) components are fully consistent with activation of the established pathway of checkpoint signaling in response to incomplete or unstable interactions between kinetochores of mitotic chromosomes and spindle microtubules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weaver, Beth A A -- Cleveland, Don W -- New York, N.Y. -- Science. 2007 May 18;316(5827):982; author reply 982.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research and Department of Cellular and Molecular Medicine, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0670, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17510348" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Kinetochores/*physiology ; Microtubule-Associated Proteins/*metabolism ; Microtubules/*metabolism/ultrastructure ; *Mitosis ; Signal Transduction ; Spindle Apparatus/*metabolism ; Tubulin/*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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  • 7
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    Medicine. Treating neurodegenerative diseases with antibiotics (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Timothy M -- Cleveland, Don W -- R37 NS027036/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):361-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research and the Department of Medicine and Neurosciences, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15661995" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/*drug therapy ; Animals ; Anti-Bacterial Agents/pharmacology/*therapeutic use ; Brain/metabolism ; Ceftriaxone/pharmacology/*therapeutic use ; Clinical Trials as Topic ; Drug Evaluation, Preclinical ; Excitatory Amino Acid Transporter 2/genetics/metabolism ; Glutamic Acid/metabolism ; Humans ; Mice ; Motor Neurons/physiology ; Neurodegenerative Diseases/*drug therapy ; Spinal Cord/metabolism ; Synapses/physiology ; Synaptic Transmission ; beta-Lactams/pharmacology/*therapeutic use
    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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  • 8
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    Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-04
    Description: The most common inherited [correct] form of amyotrophic lateral sclerosis (ALS), a neurodegenerative disease affecting adult motor neurons, is caused by dominant mutations in the ubiquitously expressed Cu-Zn superoxide dismutase (SOD1). In chimeric mice that are mixtures of normal and SOD1 mutant-expressing cells, toxicity to motor neurons is shown to require damage from mutant SOD1 acting within nonneuronal cells. Normal motor neurons in SOD1 mutant chimeras develop aspects of ALS pathology. Most important, nonneuronal cells that do not express mutant SOD1 delay degeneration and significantly extend survival of mutant-expressing motor neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clement, A M -- Nguyen, M D -- Roberts, E A -- Garcia, M L -- Boillee, S -- Rule, M -- McMahon, A P -- Doucette, W -- Siwek, D -- Ferrante, R J -- Brown, R H Jr -- Julien, J-P -- Goldstein, L S B -- Cleveland, D W -- AG 12992/AG/NIA NIH HHS/ -- AG 13846/AG/NIA NIH HHS/ -- HD 30249/HD/NICHD NIH HHS/ -- NS 27036/NS/NINDS NIH HHS/ -- NS 31248/NS/NINDS NIH HHS/ -- NS 37912/NS/NINDS NIH HHS/ -- R37 NS027036/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 3;302(5642):113-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, University of California, 9500 Gilman Drive, La Jolla, CA 92093-0670, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14526083" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/*pathology ; Animals ; Axons/pathology ; Cell Survival ; Chimera ; Humans ; Mice ; Mice, Inbred C57BL ; Mice, Inbred Strains ; Mice, Transgenic ; Motor Neurons/metabolism/pathology/*physiology ; Mutation ; Nerve Degeneration ; Neurofilament Proteins/metabolism ; Spinal Cord/metabolism/*pathology ; Superoxide Dismutase/*genetics/metabolism ; Survival Rate ; Ubiquitin/analysis
    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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  • 9
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    Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-22
    Description: Analysis of transgenic mice expressing familial amyotrophic lateral sclerosis (ALS)-linked mutations in the enzyme superoxide dismutase (SOD1) have shown that motor neuron death arises from a mutant-mediated toxic property or properties. In testing the disease mechanism, both elimination and elevation of wild-type SOD1 were found to have no effect on mutant-mediated disease, which demonstrates that the use of SOD mimetics is unlikely to be an effective therapy and raises the question of whether toxicity arises from superoxide-mediated oxidative stress. Aggregates containing SOD1 were common to disease caused by different mutants, implying that coaggregation of an unidentified essential component or components or aberrant catalysis by misfolded mutants underlies a portion of mutant-mediated toxicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bruijn, L I -- Houseweart, M K -- Kato, S -- Anderson, K L -- Anderson, S D -- Ohama, E -- Reaume, A G -- Scott, R W -- Cleveland, D W -- NS 27036/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 18;281(5384):1851-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research and Departments of Medicine and Neuroscience, University of California, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9743498" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/*enzymology/genetics/pathology ; Animals ; Astrocytes/enzymology/ultrastructure ; Disease Progression ; Female ; Humans ; Hydrogen Peroxide/metabolism ; Inclusion Bodies/enzymology/ultrastructure ; Male ; Mice ; Mice, Transgenic ; Motor Neurons/enzymology/*pathology ; Mutation ; *Nerve Degeneration ; Oxidative Stress ; Superoxide Dismutase/genetics/*metabolism ; Superoxides/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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  • 10
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    A structural scaffolding of intermediate filaments in health and disease (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: The cytoplasm of animal cells is structured by a scaffolding composed of actin microfilaments, microtubules, and intermediate filaments. Intermediate filaments, so named because their 10-nanometer diameter is intermediate between that of microfilaments (6 nanometers) and microtubules (23 nanometers), assemble into an anastomosed network within the cytoplasm. In combination with a recently identified class of cross-linking proteins that mediate interactions between intermediate filaments and the other cytoskeletal networks, evidence is reviewed here that intermediate filaments provide a flexible intracellular scaffolding whose function is to structure cytoplasm and to resist stresses externally applied to the cell. Mutations that weaken this structural framework increase the risk of cell rupture and cause a variety of human disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fuchs, E -- Cleveland, D W -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):514-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9438837" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/physiology/ultrastructure ; Cytoplasm/physiology/ultrastructure ; Cytoskeletal Proteins/*metabolism ; *Disease ; Genetic Diseases, Inborn/*etiology/pathology ; Humans ; Intermediate Filament Proteins/*metabolism ; Intermediate Filaments/*physiology/ultrastructure ; Keratinocytes/physiology/ultrastructure ; Keratins/genetics/physiology ; Microtubules/metabolism/ultrastructure ; Mutation ; Neurons/physiology/ultrastructure
    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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