Search Results - (Author, Cooperation:H. Kaphzan)

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  1. 1
    E. Santini ; T. N. Huynh ; A. F. MacAskill ; A. G. Carter ; P. Pierre ; D. Ruggero ; H. Kaphzan ; E. Klann
    Nature Publishing Group (NPG)
    Published 2012
    Staff View
    Publication Date:
    2012-12-25
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Animals ; Autistic Disorder/drug therapy/*genetics/pathology/*physiopathology ; Behavior, Animal/drug effects ; Dendrites/metabolism/pathology ; Eukaryotic Initiation Factor-4E/genetics/*metabolism ; Eukaryotic Initiation Factor-4G/metabolism ; Female ; Hippocampus/metabolism ; Hydrazones ; Infusions, Intraventricular ; Male ; Mice ; Mice, Transgenic ; Neostriatum/metabolism ; Neuronal Plasticity ; Nitro Compounds/administration & dosage/pharmacology/therapeutic use ; Prefrontal Cortex/metabolism ; *Protein Biosynthesis/drug effects/genetics ; RNA Caps/metabolism ; Synapses/*metabolism/*pathology ; Thiazoles/administration & dosage/pharmacology/therapeutic use
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Belelovsky, K. ; Elkobi, A. ; Kaphzan, H. ; Nairn, A. C. ; Rosenblum, K.

    Oxford, UK : Blackwell Science Ltd
    Published 2005
    Staff View
    ISSN:
    1460-9568
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Medicine
    Notes:
    In a variety of species memory consolidation following different learning paradigms has been shown to be dependent on protein synthesis. However, it is not known whether modulation of protein synthesis is a critical component of the consolidation process, nor is the identity of any protein(s) subject to translational regulation, known. We report here that phosphorylation of eukaryotic elongation factor-2 (eEF2), an indicator for translational elongation attenuation, is correlated with input that produces taste memory consolidation in the relevant cortex of rat. The temporal pattern of eEF2 phosphorylation is similar to extra-cellular regulated kinase 2 (ERK2) activation and S6K1 phosphorylation, which are known to stimulate translation initiation. In addition, increased eEF2 phosphorylation and increased αCaMKII expression is detected in a synaptoneurosomal fraction made from taste cortex following memory consolidation. These results suggest that increased initiation rate together with decreased elongation rate, during memory consolidation, shift the rate-limiting step of protein synthesis, to produce a local switch-like effect in the expression of neuronal proteins.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1111/j.1460-9568.2005.04428.x

    Articles: DFG German National Licenses