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  • 1
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    Homeostatic replacement of CNS myeloid cells [Neuroscience] (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-10-31
    Description: Under most physiological circumstances, monocytes are excluded from parenchymal CNS tissues. When widespread monocyte entry occurs, their numbers decrease shortly after engraftment in the presence of microglia. However, some disease processes lead to focal and selective loss, or dysfunction, of microglia, and microglial senescence typifies the aged brain. In this...
    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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    Stratospheric sudden warmings in an idealized GCM (2014)
    Wiley
    Details
    Publication Date: 2014-08-31
    Description: An idealized general circulation model with an analytically described Newtonian cooling term is employed to study the occurrence rate of sudden stratospheric warmings (SSWs) over a wide range of parameters. In particular, the sensitivity of the SSW occurrence rates to orographic forcing and both relaxation temperature and damping rate is evaluated. The stronger the orographic forcing and the weaker radiative forcing (in both temperature and damping rate), the higher the SSW frequency. The separate effects of the damping rates at low and high latitudes are somewhat more complex. Generally, lower damping rates result in higher SSW frequency. However, if the low and high latitude damping rates are not the same, SSW frequency tends to be most sensitive to a fractional change in the lower of the two damping rates. In addition, the effect of the damping rates on the stratospheric residual circulation is investigated. It is found that higher high-latitude damping rate results in deeper but narrower circulation, whereas higher low-latitude damping rates cause strengthening of the streamfunction in the tropical mid to upper stratosphere. Finally, the relation between easily measured and compared climatological fields and the SSW occurrence rate is determined. The average stratospheric polar zonal mean zonal wind shows a strong anti-correlation with the SSW frequency. In the troposphere, there is a high correlation between the meridional temperature gradient and SSW frequency, suggesting that the strength of synoptic activity in the troposphere may be an important influence on SSW occurrence.
    Print ISSN: 0148-0227
    Topics: Geosciences , Physics
    Published by Wiley on behalf of American Geophysical Union (AGU).
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  • 3
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    Cerebral hemorrhage after passive anti-Abeta immunotherapy (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfeifer, M -- Boncristiano, S -- Bondolfi, L -- Stalder, A -- Deller, T -- Staufenbiel, M -- Mathews, P M -- Jucker, M -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1379.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Pathology, University of Basel, CH-4003 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12434053" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/pathology/therapy ; Amyloid beta-Peptides/analysis/*immunology ; Animals ; Antibodies, Monoclonal/immunology ; Capillary Permeability ; Cerebral Amyloid Angiopathy/metabolism/pathology/*therapy ; Cerebral Hemorrhage/*etiology ; Humans ; Immunization, Passive/*adverse effects ; Immunoglobulin G/immunology ; Male ; Mice ; Mice, Transgenic ; Neocortex/blood supply/chemistry/pathology ; Peptide Fragments/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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  • 4
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    Age-associated inclusions in normal and transgenic mouse brain (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jucker, M -- Walker, L C -- Martin, L J -- Kitt, C A -- Kleinman, H K -- Ingram, D K -- Price, D L -- New York, N.Y. -- Science. 1992 Mar 13;255(5050):1443-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1542796" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*metabolism ; Amyloid beta-Peptides/*metabolism ; Animals ; Brain/*metabolism ; Female ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic/*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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  • 5
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    gamma-Secretase heterogeneity in the Aph1 subunit: relevance for Alzheimer's disease (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-21
    Description: The gamma-secretase complex plays a role in Alzheimer's disease and cancer progression. The development of clinically useful inhibitors, however, is complicated by the role of the gamma-secretase complex in regulated intramembrane proteolysis of Notch and other essential proteins. Different gamma-secretase complexes containing different Presenilin or Aph1 protein subunits are present in various tissues. Here we show that these complexes have heterogeneous biochemical and physiological properties. Specific inactivation of the Aph1B gamma-secretase in a mouse Alzheimer's disease model led to improvements of Alzheimer's disease-relevant phenotypic features without any Notch-related side effects. The Aph1B complex contributes to total gamma-secretase activity in the human brain, and thus specific targeting of Aph1B-containing gamma-secretase complexes may help generate less toxic therapies for Alzheimer's disease.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2740474/" 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/PMC2740474/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Serneels, Lutgarde -- Van Biervliet, Jerome -- Craessaerts, Katleen -- Dejaegere, Tim -- Horre, Katrien -- Van Houtvin, Tine -- Esselmann, Hermann -- Paul, Sabine -- Schafer, Martin K -- Berezovska, Oksana -- Hyman, Bradley T -- Sprangers, Ben -- Sciot, Raf -- Moons, Lieve -- Jucker, Mathias -- Yang, Zhixiang -- May, Patrick C -- Karran, Eric -- Wiltfang, Jens -- D'Hooge, Rudi -- De Strooper, Bart -- AG 13579/AG/NIA NIH HHS/ -- AG026593/AG/NIA NIH HHS/ -- P01 AG015379/AG/NIA NIH HHS/ -- P01 AG015379-110009/AG/NIA NIH HHS/ -- P01AG015379/AG/NIA NIH HHS/ -- R01 AG026593/AG/NIA NIH HHS/ -- R01 AG026593-01A1/AG/NIA NIH HHS/ -- R01AG026593/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2009 May 1;324(5927):639-42. doi: 10.1126/science.1171176. Epub 2009 Mar 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department for Molecular and Developmental Genetics, VIB, KULeuven, Herestraat 49, 3000 Leuven, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19299585" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/drug therapy/*metabolism ; Amyloid Precursor Protein Secretases/antagonists & ; inhibitors/*chemistry/genetics/*metabolism ; Amyloid beta-Peptides/analysis/chemistry/*metabolism ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Brain/*metabolism ; Disease Models, Animal ; Endopeptidases/chemistry/genetics/*metabolism ; Female ; Humans ; Maze Learning ; Membrane Proteins/metabolism ; Memory ; Mice ; Neurons/metabolism ; Peptide Fragments/analysis/metabolism ; Peptide Hydrolases/metabolism ; Presenilin-1/chemistry/genetics/metabolism ; Protein Subunits/chemistry/metabolism ; Receptor, Notch1/metabolism ; Signal Transduction
    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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    Peripherally applied Abeta-containing inoculates induce cerebral beta-amyloidosis (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-10-23
    Description: The intracerebral injection of beta-amyloid-containing brain extracts can induce cerebral beta-amyloidosis and associated pathologies in susceptible hosts. We found that intraperitoneal inoculation with beta-amyloid-rich extracts induced beta-amyloidosis in the brains of beta-amyloid precursor protein transgenic mice after prolonged incubation times.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3233904/" 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/PMC3233904/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisele, Yvonne S -- Obermuller, Ulrike -- Heilbronner, Gotz -- Baumann, Frank -- Kaeser, Stephan A -- Wolburg, Hartwig -- Walker, Lary C -- Staufenbiel, Matthias -- Heikenwalder, Mathias -- Jucker, Mathias -- P51 RR000165/RR/NCRR NIH HHS/ -- P51 RR000165-51/RR/NCRR NIH HHS/ -- RR-00165/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2010 Nov 12;330(6006):980-2. doi: 10.1126/science.1194516. Epub 2010 Oct 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Neurology, Hertie-Institute for Clinical Brain Research, University of Tubingen, D-72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20966215" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/metabolism/pathology ; Amyloid beta-Peptides/administration & dosage/*chemistry/metabolism ; Animals ; Brain/blood supply/*pathology ; Brain Chemistry ; Cerebral Amyloid Angiopathy/metabolism/pathology ; Female ; Injections, Intraperitoneal ; Mice ; Mice, Transgenic ; Plaque, Amyloid/pathology ; Prions/chemistry/metabolism ; Protein Folding ; 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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  • 7
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    Comment on "ApoE-directed therapeutics rapidly clear beta-amyloid and reverse deficits in AD mouse models" (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-05-25
    Description: Cramer et al. (Reports, 23 March 2012, p. 1503; published online 9 February 2012) reported that bexarotene rapidly reduces beta-amyloid (Abeta) levels and plaque burden in two mouse models of Abeta deposition in Alzheimer's disease (AD). We now report that, although bexarotene reduces soluble Abeta40 levels in one of the mouse models, the drug has no impact on plaque burden in three strains that exhibit Abeta amyloidosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Veeraraghavalu, Karthikeyan -- Zhang, Can -- Miller, Sean -- Hefendehl, Jasmin K -- Rajapaksha, Tharinda W -- Ulrich, Jason -- Jucker, Mathias -- Holtzman, David M -- Tanzi, Rudolph E -- Vassar, Robert -- Sisodia, Sangram S -- New York, N.Y. -- Science. 2013 May 24;340(6135):924-f. doi: 10.1126/science.1235505.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23704555" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*drug therapy/*metabolism ; Amyloid beta-Peptides/*metabolism ; Animals ; Apolipoproteins E/*metabolism ; Brain/*metabolism ; Male ; Tetrahydronaphthalenes/*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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    Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-09-23
    Description: Protein aggregation is an established pathogenic mechanism in Alzheimer's disease, but little is known about the initiation of this process in vivo. Intracerebral injection of dilute, amyloid-beta (Abeta)-containing brain extracts from humans with Alzheimer's disease or beta-amyloid precursor protein (APP) transgenic mice induced cerebral beta-amyloidosis and associated pathology in APP transgenic mice in a time- and concentration-dependent manner. The seeding activity of brain extracts was reduced or abolished by Abeta immunodepletion, protein denaturation, or by Abeta immunization of the host. The phenotype of the exogenously induced amyloidosis depended on both the host and the source of the agent, suggesting the existence of polymorphic Abeta strains with varying biological activities reminiscent of prion strains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meyer-Luehmann, Melanie -- Coomaraswamy, Janaky -- Bolmont, Tristan -- Kaeser, Stephan -- Schaefer, Claudia -- Kilger, Ellen -- Neuenschwander, Anton -- Abramowski, Dorothee -- Frey, Peter -- Jaton, Anneliese L -- Vigouret, Jean-Marie -- Paganetti, Paolo -- Walsh, Dominic M -- Mathews, Paul M -- Ghiso, Jorge -- Staufenbiel, Matthias -- Walker, Lary C -- Jucker, Mathias -- NS45357/NS/NINDS NIH HHS/ -- RR-00165/RR/NCRR NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2006 Sep 22;313(5794):1781-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Neurology, Hertie-Institute for Clinical Brain Research, University of Tubingen, D-72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16990547" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Aged, 80 and over ; Aging ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/*administration & dosage/*analysis/chemistry/pharmacology ; Amyloid beta-Protein Precursor/*administration & dosage/pharmacology ; Amyloidosis/*metabolism/pathology ; Animals ; Brain/pathology ; Brain Chemistry ; Brain Diseases/*metabolism/pathology ; Female ; Hippocampus/*chemistry/pathology ; Humans ; Male ; Mice ; Mice, Transgenic ; Protein Denaturation ; Time Factors ; Tissue Extracts
    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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    Self-propagation of pathogenic protein aggregates in neurodegenerative diseases (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-09-06
    Description: For several decades scientists have speculated that the key to understanding age-related neurodegenerative disorders may be found in the unusual biology of the prion diseases. Recently, owing largely to the advent of new disease models, this hypothesis has gained experimental momentum. In a remarkable variety of diseases, specific proteins have been found to misfold and aggregate into seeds that structurally corrupt like proteins, causing them to aggregate and form pathogenic assemblies ranging from small oligomers to large masses of amyloid. Proteinaceous seeds can therefore serve as self-propagating agents for the instigation and progression of disease. Alzheimer's disease and other cerebral proteopathies seem to arise from the de novo misfolding and sustained corruption of endogenous proteins, whereas prion diseases can also be infectious in origin. However, the outcome in all cases is the functional compromise of the nervous system, because the aggregated proteins gain a toxic function and/or lose their normal function. As a unifying pathogenic principle, the prion paradigm suggests broadly relevant therapeutic directions for a large class of currently intractable diseases.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3963807/" 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/PMC3963807/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jucker, Mathias -- Walker, Lary C -- P51 OD011132/OD/NIH HHS/ -- P51 RR000165/RR/NCRR NIH HHS/ -- P51OD11132/OD/NIH HHS/ -- P51RR165/RR/NCRR NIH HHS/ -- R21 AG040589/AG/NIA NIH HHS/ -- R21AG040589/AG/NIA NIH HHS/ -- England -- Nature. 2013 Sep 5;501(7465):45-51. doi: 10.1038/nature12481.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Neurology, Hertie Institute for Clinical Brain Research, University of Tubingen, D-72076 Tubingen, Germany. mathias.jucker@uni-tuebingen.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24005412" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/metabolism/pathology ; Amyloid/chemistry/*metabolism ; Animals ; Humans ; Neurodegenerative Diseases/drug therapy/*metabolism/*pathology ; Prion Diseases/drug therapy/metabolism/pathology ; Prions/chemistry/classification/*metabolism ; alpha-Synuclein/chemistry/metabolism ; tau Proteins/chemistry/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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  • 10
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    Neurodegeneration: Amyloid-beta pathology induced in humans (2015)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2015-09-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jucker, Mathias -- Walker, Lary C -- England -- Nature. 2015 Sep 10;525(7568):193-4. doi: 10.1038/525193a.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hertie Institute for Clinical Brain Research, University of Tubingen, and at the German Center for Neurodegenerative Diseases (DZNE), D-72076 Tubingen, Germany. ; Yerkes National Primate Research Center and Department of Neurology, Emory University, Atlanta, Georgia 30322, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26354478" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*etiology ; Amyloid beta-Peptides/*metabolism ; Cerebral Amyloid Angiopathy/*etiology ; Creutzfeldt-Jakob Syndrome/*etiology ; *Drug Contamination ; Human Growth Hormone/*administration & dosage ; Humans ; *Iatrogenic Disease
    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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