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  • 1
    Electronic Resource
    Electronic Resource
    Immunohistochemical demonstration of tissue transglutaminase in amyloid plaques (1998)
    Springer
    Acta neuropathologica 96 (1998), S. 395-400 
    Details
    ISSN: 1432-0533
    Keywords: Key words Amyloid β-peptide ; Alzheimer’s disease ; Amyloid deposits ; Tissue transglutaminase ; Protein polymerization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The brain of Alzheimer’s disease patients contains deposits of the 39–42-amino acid (∼ 4 kDa) amyloid β-peptide, which is derived from the β-amyloid precursor protein. These pathological deposits have been shown to consist in part of insoluble 8- and 16-kDa aggregates of the amyloid β-peptide. This report confirms that the amyloid β-peptide is a substrate for tissue transglutaminase (TGase) and demonstrates that human brain preparations from Alzheimer’s disease patients and control patients form cross-linked dimers from added iodinated amyloid β-peptide. Immunohistochemical staining for TGase revealed its presence in tissue sections and isolated amyloid plaque cores obtained from brains of patients diagnosed as having Alzheimer’s disease. These results provide evidence that the previously described insoluble amyloid deposits in Alzheimer’s disease may involve TGase-mediated cross-linked amyloid β-peptide polymers, and suggest a potential role for TGase in the pathogenesis of this disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004010050910
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  • 2
    Electronic Resource
    Electronic Resource
    Transition structures and exo/endo stereoselectivities of concerted [6 + 4] cycloadditions with density functional theory (1999)
    Springer
    Theoretical chemistry accounts 103 (1999), S. 81-84 
    Details
    ISSN: 1432-2234
    Keywords: Key words: Secondary orbital interactions ; B3LYP ; Diels ; Alder reaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract. Density functional theory transition structures were located for three concerted [6 + 4] cycloaddition reactions involving cis-hexatriene and butadiene, cyclopentadiene and cycloheptatriene, and cyclopentadiene and tropone. Geometries, energies, and entropies were computed at the Becke3LYP/6-31G* level. The activation energy of the concerted [6 + 4] cycloaddition of hexatriene and butadiene is 33.3 kcal/mol, about 8 kcal/mol above the activation energy of the butadiene plus ethylene [4 + 2] cycloaddition. The endo concerted [6 + 4] transition state is 1.1 kcal/mol higher than the exo. The [6 + 4] reaction of cyclopentadiene and cycloheptatriene has a barrier of 25.9 kcal/mol, while the cyclopentadiene–tropone barrier drops to 20.7 kcal/mol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002140050517
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    Paper (German National Licenses)
    Fulltext
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