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  • 1
    Electronic Resource
    Electronic Resource
    Effect of tissue transglutaminase on the solubility of proteins containing expanded polyglutamine repeats (2004)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 88 (2004), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The expansion of a polyglutamine (polyQ) domain in neuronal proteins is the molecular genetic cause of at least eight neurodegenerative diseases. Proteins with a polyQ domain that is greater than 40 Q (Q40) residues form insoluble intranuclear and cytoplasmic inclusions. Expanded polyQ proteins self-associate by non-covalent interactions and become insoluble. They can also be covalently cross-linked by tissue transglutaminase (TTG), a calcium-dependent enzyme present in cells throughout the nervous system. However, it remains unclear whether TTG cross-linking directly contributes to the insolubility of the expanded polyQ proteins. Using an in vitro solubility assay, we found TTG cross-linked Q62 monomers into high molecular weight soluble complexes in a calcium-dependent reaction. Inhibition of TTG cross-linking by primary amine substrates including putrescine and biotinylated pentylamine antagonized TTG's ability to form soluble complexes. In contrast, primary amines (histamine and lysine) that were less effective inhibitors of TTG cross-linking did not inhibit Q62 from becoming insoluble. In summary, TTG can increase the solubility of expanded polyQ proteins by catalyzing intermolecular cross-links. This demonstrates directly that TTG will reduce the ability of expanded polyQ proteins from becoming insoluble. Furthermore, the effectiveness of a primary amine substrate at inhibiting formation of insoluble inclusions may be related to their ability to inhibit intermolecular cross-linking by TTG.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2003.02249.x
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  • 2
    Electronic Resource
    Electronic Resource
    Sequestration of Amyloid β-Peptide (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 695 (1993), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Notes: Amyloid β-protein, or β/A4, is a 4-kilodalton peptide that forms poorly soluble extracellular depositions of amyloid in brains and leptomeninges of patients with Alzheimer's disease (AD), Down's syndrome (DS), and hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D). β/A4 peptide is a derivative of a large transmembrane glycoprotein (APP) and is found in the extracellular space, i.e., in the cerebrospinal fluid and serum of individuals with and without AD and in the conditioned media of many different cells grown in culture.1 The mechanism by which normally produced amyloid β peptide forms extracellular aggregates in patients is unknown. One possible explanation is a failure of a mechanism for removal of the β/A4 peptide that prevents this highly aggregating peptide from forming extracellular amyloid depositions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1993.tb23042.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of Human T Cells that Require Zinc for Growth (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 36 (1992), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Zinc is an essential trace clement required for normal tunction of Ihe immune system. Deficiency of zinc results in marked thymic atrophy in experimental animals, and in man immunodeficiency is a recognized complication of zinc deprivation. Althoug numerous proteins require zinc as a cofactor, its precise functions in the immune system remain unknown. The mechanism by which metals stimulate lymphocytes, whether all T cells are responsive, and the relationship to zinc requirements have not been determined. We unexpectedly isolated a number of human T-cell lines that have a highly specific requirement for zinc. The ability to respond to zinc resides in only a subset of T cells since antigen-specific clones are not stimulated by zinc. Although proliferation requires the presence of antigen-presenting cells and is restricted by class II MHC antigens, antigen-presenting cells could not be pulsed with zinc to induce T-cell activation. Our results suggest that zinc-dependent T cells are a subset of CD4+ cells present in all normal individuals and that zinc stimulates their growth by novel mechanisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1992.tb03099.x
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Apolipoprotein E and Alzheimer's Disease (1996)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Neuroscience 19 (1996), S. 53-77 
    Details
    ISSN: 0147-006X
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ne.19.030196.000413
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Protective effect of apolipoprotein E type 2 allele for late onset Alzheimer disease (1994)
    [s.l.] : Nature Publishing Group
    Nature genetics 7 (1994), S. 180-184 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Gene dosage of the apolipoprotein E (APOE) ε4 allele is a major risk factor for familial Alzheimer disease (AD) of late onset (after age 60). Here we studied a large series of 115 AD case subjects and 243 controls as well as 150 affected and 197 unaffected members of 66 AD families. Our data ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng0694-180
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    Paper (German National Licenses)
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