ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    facet.materialart.
    Unknown
    Dynamin-related protein 1 is required for normal mitochondrial bioenergetic and synaptic function in CA1 hippocampal neurons (2015)
    Springer Nature
    Details
    Publication Date: 2015-04-17
    Description: Dynamin-related protein 1 is required for normal mitochondrial bioenergetic and synaptic function in CA1 hippocampal neurons Cell Death and Disease 6, e1725 (April 2015). doi:10.1038/cddis.2015.94 Authors: L Y Shields, H Kim, L Zhu, D Haddad, A Berthet, D Pathak, M Lam, R Ponnusamy, L G Diaz-Ramirez, T M Gill, H Sesaki, L Mucke & K Nakamura
    Electronic ISSN: 2041-4889
    Topics: Biology , Medicine
    Published by Springer Nature
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-26
    Description: To elucidate the role of the synaptic protein alpha-synuclein in neurodegenerative disorders, transgenic mice expressing wild-type human alpha-synuclein were generated. Neuronal expression of human alpha-synuclein resulted in progressive accumulation of alpha-synuclein-and ubiquitin-immunoreactive inclusions in neurons in the neocortex, hippocampus, and substantia nigra. Ultrastructural analysis revealed both electron-dense intranuclear deposits and cytoplasmic inclusions. These alterations were associated with loss of dopaminergic terminals in the basal ganglia and with motor impairments. These results suggest that accumulation of wild-type alpha-synuclein may play a causal role in Parkinson's disease and related conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Masliah, E -- Rockenstein, E -- Veinbergs, I -- Mallory, M -- Hashimoto, M -- Takeda, A -- Sagara, Y -- Sisk, A -- Mucke, L -- AG10689/AG/NIA NIH HHS/ -- AG11385/AG/NIA NIH HHS/ -- AG5131/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2000 Feb 18;287(5456):1265-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurosciences, Department of Pathology, University of California San Diego, La Jolla, CA 92093-0624, USA. emasliah@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10678833" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*metabolism/ultrastructure ; Dopamine/*physiology ; Humans ; Inclusion Bodies/*metabolism/ultrastructure ; Lewy Bodies/ultrastructure ; Lewy Body Disease/metabolism/pathology ; Mice ; Mice, Inbred C57BL ; Mice, Inbred DBA ; Mice, Transgenic ; Microscopy, Electron ; Motor Activity ; Nerve Tissue Proteins/genetics/immunology/*metabolism ; Neurodegenerative Diseases/*metabolism/pathology ; Neurons/*metabolism/ultrastructure ; Substantia Nigra/metabolism/ultrastructure ; Synucleins ; Tyrosine 3-Monooxygenase/immunology/metabolism ; Ubiquitins/metabolism ; alpha-Synuclein
    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
  • 3
    facet.materialart.
    Unknown
    Neuroscience: Alzheimer's disease (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-10-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mucke, Lennart -- England -- Nature. 2009 Oct 15;461(7266):895-7. doi: 10.1038/461895a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19829367" target="_blank"〉PubMed〈/a〉
    Keywords: Age of Onset ; Aging ; *Alzheimer Disease/diagnosis/epidemiology/etiology/physiopathology/therapy ; Amyloid beta-Peptides/metabolism ; Animals ; Controlled Clinical Trials as Topic ; Genetic Testing ; Humans ; Mice ; Stem Cell Transplantation ; Treatment Failure ; United States/epidemiology
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 4
    facet.materialart.
    Unknown
    Alzheimer's disease: A prion protein connection (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-02-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cisse, Moustapha -- Mucke, Lennart -- England -- Nature. 2009 Feb 26;457(7233):1090-1. doi: 10.1038/4571090a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19242462" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*metabolism/*pathology/physiopathology ; Amyloid Precursor Protein Secretases/metabolism ; Amyloid beta-Peptides/*chemistry/*metabolism ; Animals ; Hippocampus/cytology/metabolism ; Humans ; Long-Term Potentiation/physiology ; Mice ; Neuronal Plasticity/physiology ; Neurons/metabolism ; Prions/genetics/*metabolism ; Receptors, Cell Surface/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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 5
    facet.materialart.
    Unknown
    Viral persistence in neurons explained by lack of major histocompatibility class I expression (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-13
    Description: Viruses frequently persist in neurons, suggesting that these cells can evade immune surveillance. In a mouse model, 5 x 10(6) cytotoxic T lymphocytes (CTLs), specific for lymphocytic choriomeningitis virus (LCMV), did not lyse infected neurons or cause immunopathologic injury. In contrast, intracerebral injection of less than 10(3) CTL caused disease and death when viral antigens were expressed on leptomeningeal and choroid plexus cells of the nervous system. The neuronal cell line OBL21 expresses little or no major histocompatibility (MHC) class I surface glycoproteins and when infected with LCMV, resisted lysis by virus-specific CTLs. Expression of MHC heavy chain messenger RNA was limited, but beta 2-microglobulin messenger RNA and protein was made normally. OBL21 cells were made sensitive to CTL lysis by transfection with a fusion gene encoding another MHC class I molecule. Hence, neuronal cells probably evade immune surveillance by failing to express MHC class I molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joly, E -- Mucke, L -- Oldstone, M B -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1283-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuropharmacology, Scripps Clinic and Research Foundation, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1891717" target="_blank"〉PubMed〈/a〉
    Keywords: Acute Disease ; Animals ; Brain/immunology/*microbiology ; Cell Line ; Chronic Disease ; Gene Expression ; *Genes, MHC Class I ; Histocompatibility Antigens Class I/analysis ; Lymphocytic Choriomeningitis/*immunology ; Lymphocytic choriomeningitis virus/immunology/*pathogenicity ; Mice ; Mice, Inbred Strains ; Neurons/immunology/*microbiology ; T-Lymphocytes, Cytotoxic/*immunology
    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
  • 6
    facet.materialart.
    Unknown
    Reversing EphB2 depletion rescues cognitive functions in Alzheimer model (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-11-30
    Description: Amyloid-beta oligomers may cause cognitive deficits in Alzheimer's disease by impairing neuronal NMDA-type glutamate receptors, whose function is regulated by the receptor tyrosine kinase EphB2. Here we show that amyloid-beta oligomers bind to the fibronectin repeats domain of EphB2 and trigger EphB2 degradation in the proteasome. To determine the pathogenic importance of EphB2 depletions in Alzheimer's disease and related models, we used lentiviral constructs to reduce or increase neuronal expression of EphB2 in memory centres of the mouse brain. In nontransgenic mice, knockdown of EphB2 mediated by short hairpin RNA reduced NMDA receptor currents and impaired long-term potentiation in the dentate gyrus, which are important for memory formation. Increasing EphB2 expression in the dentate gyrus of human amyloid precursor protein transgenic mice reversed deficits in NMDA receptor-dependent long-term potentiation and memory impairments. Thus, depletion of EphB2 is critical in amyloid-beta-induced neuronal dysfunction. Increasing EphB2 levels or function could be beneficial in Alzheimer's disease.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3030448/" 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/PMC3030448/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cisse, Moustapha -- Halabisky, Brian -- Harris, Julie -- Devidze, Nino -- Dubal, Dena B -- Sun, Binggui -- Orr, Anna -- Lotz, Gregor -- Kim, Daniel H -- Hamto, Patricia -- Ho, Kaitlyn -- Yu, Gui-Qiu -- Mucke, Lennart -- AG011385/AG/NIA NIH HHS/ -- AG022074/AG/NIA NIH HHS/ -- K08 AG034531/AG/NIA NIH HHS/ -- NS041787/NS/NINDS NIH HHS/ -- P01 AG022074/AG/NIA NIH HHS/ -- P01 AG022074-09/AG/NIA NIH HHS/ -- R01 AG011385/AG/NIA NIH HHS/ -- R01 AG011385-08/AG/NIA NIH HHS/ -- R01 NS041787/NS/NINDS NIH HHS/ -- R01 NS041787-09/NS/NINDS NIH HHS/ -- RR18928-01/RR/NCRR NIH HHS/ -- England -- Nature. 2011 Jan 6;469(7328):47-52. doi: 10.1038/nature09635. Epub 2010 Nov 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Institute of Neurological Disease, San Francisco, California 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21113149" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*physiopathology/*therapy ; Amyloid beta-Peptides/metabolism ; Animals ; Cell Line ; Cells, Cultured ; Cognition/*physiology ; Dentate Gyrus/metabolism ; Disease Models, Animal ; Humans ; Long-Term Potentiation ; Memory/physiology ; Mice ; Mice, Transgenic ; Neuronal Plasticity ; Proteasome Endopeptidase Complex/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Rats ; Receptor, EphB2/chemistry/*deficiency/genetics/*metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Synapses/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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 7
    facet.materialart.
    Unknown
    100 years and counting: prospects for defeating Alzheimer's disease (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-11-04
    Description: This week marks a century since the first description of Alzheimer's disease (AD). Despite approval of several drugs for AD, the disease continues to rob millions of their memories and their lives. Fortunately, many new therapies directly targeting the mechanisms underlying AD are now in the pipeline. Among the investigative AD therapies in clinical trials are several strategies to block pathogenic amyloid-beta peptides and to rescue vulnerable neurons from degeneration. Complementary but less mature strategies aim to prevent the copathogenic effects of apolipoprotein E and the microtubule-associated protein tau. New insights into selective neuronal vulnerability and the link between aging and AD may provide additional entry points for therapeutic interventions. The predicted increase in AD cases over the next few decades makes the development of better treatments a matter of utmost importance and urgency.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3544944/" 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/PMC3544944/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberson, Erik D -- Mucke, Lennart -- AG011385/AG/NIA NIH HHS/ -- AG022074/AG/NIA NIH HHS/ -- K08 NS054811/NS/NINDS NIH HHS/ -- K08 NS054811-01/NS/NINDS NIH HHS/ -- NS054811/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2006 Nov 3;314(5800):781-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Institute of Neurological Disease and Department of Neurology, University of California, San Francisco, CA 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17082448" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/pathology/physiopathology/*therapy ; Amyloid beta-Peptides/immunology/metabolism ; Animals ; Clinical Trials as Topic ; Enzyme Inhibitors/therapeutic use ; Humans ; Immunization, Passive ; Nootropic Agents/therapeutic use ; Vaccination
    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
  • 8
    facet.materialart.
    Unknown
    Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-05-05
    Description: Many potential treatments for Alzheimer's disease target amyloid-beta peptides (Abeta), which are widely presumed to cause the disease. The microtubule-associated protein tau is also involved in the disease, but it is unclear whether treatments aimed at tau could block Abeta-induced cognitive impairments. Here, we found that reducing endogenous tau levels prevented behavioral deficits in transgenic mice expressing human amyloid precursor protein, without altering their high Abeta levels. Tau reduction also protected both transgenic and nontransgenic mice against excitotoxicity. Thus, tau reduction can block Abeta- and excitotoxin-induced neuronal dysfunction and may represent an effective strategy for treating Alzheimer's disease and related conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberson, Erik D -- Scearce-Levie, Kimberly -- Palop, Jorge J -- Yan, Fengrong -- Cheng, Irene H -- Wu, Tiffany -- Gerstein, Hilary -- Yu, Gui-Qiu -- Mucke, Lennart -- AG011385/AG/NIA NIH HHS/ -- AG022074/AG/NIA NIH HHS/ -- K08 NS054811/NS/NINDS NIH HHS/ -- K08 NS054811-02/NS/NINDS NIH HHS/ -- MH070588/MH/NIMH NIH HHS/ -- NS054811/NS/NINDS NIH HHS/ -- RR18928-01/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2007 May 4;316(5825):750-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Institute of Neurological Disease, San Francisco, CA 94158, USA. eroberson@gladstone.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17478722" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*metabolism/pathology/physiopathology/*therapy ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics/metabolism ; Animals ; Axons/ultrastructure ; Convulsants/pharmacology ; *Disease Models, Animal ; Excitatory Amino Acid Agonists/pharmacology ; Exploratory Behavior ; Hippocampus/pathology ; Humans ; Kainic Acid/pharmacology ; Maze Learning ; Memory ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Motor Activity ; Pentylenetetrazole/pharmacology ; Phosphorylation ; Seizures/prevention & control ; tau Proteins/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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 9
    facet.materialart.
    Unknown
    Tau reduction prevents Abeta-induced defects in axonal transport (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-09-11
    Description: Amyloid-beta (Abeta) peptides, derived from the amyloid precursor protein, and the microtubule-associated protein tau are key pathogenic factors in Alzheimer's disease (AD). How exactly they impair cognitive functions is unknown. We assessed the effects of Abeta and tau on axonal transport of mitochondria and the neurotrophin receptor TrkA, cargoes that are critical for neuronal function and survival and whose distributions are altered in AD. Abeta oligomers rapidly inhibited axonal transport of these cargoes in wild-type neurons. Lowering tau levels prevented these defects without affecting baseline axonal transport. Thus, Abeta requires tau to impair axonal transport, and tau reduction protects against Abeta-induced axonal transport defects.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3024010/" 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/PMC3024010/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vossel, Keith A -- Zhang, Kai -- Brodbeck, Jens -- Daub, Aaron C -- Sharma, Punita -- Finkbeiner, Steven -- Cui, Bianxiao -- Mucke, Lennart -- AG011385/AG/NIA NIH HHS/ -- C06 RR018928/RR/NCRR NIH HHS/ -- NS041787/NS/NINDS NIH HHS/ -- NS057906/NS/NINDS NIH HHS/ -- R00 NS057906/NS/NINDS NIH HHS/ -- R00 NS057906-05/NS/NINDS NIH HHS/ -- R01 AG011385/AG/NIA NIH HHS/ -- R01 AG011385-07/AG/NIA NIH HHS/ -- R01 NS041787/NS/NINDS NIH HHS/ -- R01 NS041787-09/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2010 Oct 8;330(6001):198. doi: 10.1126/science.1194653. Epub 2010 Sep 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Institute of Neurological Disease, San Francisco, CA 94158, USA. kvossel@gladstone.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20829454" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid beta-Peptides/*metabolism/pharmacology ; Animals ; *Axonal Transport ; Cells, Cultured ; Hippocampus/cytology ; Mice ; Mitochondria/metabolism ; Neurons/*metabolism ; Peptide Fragments/*metabolism/pharmacology ; Receptor, trkA/metabolism ; tau 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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 10
    Electronic Resource
    Electronic Resource
    Neurotrophic and Neuroprotective Effects of hAPP in Transgenic Mice (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 777 (1996), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Notes: To better understand the role the human amyloid precursor protein (hAPP) plays in Alzheimer's disease (AD), it is essential to define its primary function(s). Here we expressed different hAPPs in neurons of transgenic (tg) mice to characterize their effects on the intact central nervous system (CNS). Immunolabeled brain sections of tg and non-tg mice were compared quantitatively by microdensitometry and computer-aided analysis of laser scanning confocal digitized images. Compared with non-tg mice, tg mice overexpressing hAPPs showed an increase in the number of synaptophysin immunoreactive presynaptic terminals as well as in the expression of the growth-associated marker GAP-43. While non-tg controls and tg mice expressing hAPP751 at moderate levels displayed a normal pattern of reinnervation of the dentate gyrus following perforant pathway transection, tg mice expressing hAPP695 at severalfold higher levels showed an accentuation of the synaptic loss and no sprouting reaction. In addition, expression of hAPP751 at moderate levels effectively protected neurons against excitotoxic injury induced either acutely by systemic injection of kainic acid or chronically by transgene-driven glial production of the soluble HIV-1 protein gp120. Neuronal expression of hAPP695 at higher levels provided less excitoprotection. Our findings are consistent with the postulate that APP plays a role in the formation/maintenance of synapses and that processes which affect this function could contribute to the synaptic pathology seen in AD. Our study also revealed that hAPPs can exert important excitoprotective functions in vivo and that the efficiency of this protection may depend on the hAPP isoform expressed as well as on the level of neuronal hAPP expression. Neuronal overexpression of hAPP beyond a certain level may have detrimental effects on the CNS, particularly in the context of secondary neural injuries.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1996.tb34405.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...