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  1. No Access

    Article

    Molecular alterations in proteasomes of rat liver during aging result in altered proteolytic activities

    Aging induces alterations of tissue protein homoeostasis. To investigate one of the major systems catalysing intracellular protein degradation we have purified 20S proteasomes from rat liver of young (2 months...

    Sabrina Gohlke, Michele Mishto, Kathrin Textoris-Taube, Christin Keller… in AGE (2014)

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    Article

    Circulating Extracellular Proteasome in the Cerebrospinal Fluid: A Study on Concentration and Proteolytic Activity

    Alterations of the intracellular ubiquitin–proteasome pathway are found in neurodegenerative and inflammatory disorders of the central nervous system, as well as in its malignancies. Inhibitory substrates of t...

    Oliver Mueller, Timur Anlasik, Jonas Wiedemann… in Journal of Molecular Neuroscience (2012)

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    Article

    Reciprocal Effects of α-Synuclein Overexpression and Proteasome Inhibition in Neuronal Cells and Tissue

    Defects in the 20S/26S proteasome and conformational changes in α-synuclein (α-syn) are implicated in the development of sporadic and familial cases of PD. The objective of this study was to evaluate whether α...

    Melanie Dyllick-Brenzinger, Cheryl A. D’Souza, Burkhardt Dahlmann… in Neurotoxicity Research (2010)

  4. No Access

    Article

    The base of the proteasome regulatory particle exhibits chaperone-like activity

    Protein substrates of the proteasome must apparently be unfolded and translocated through a narrow channel to gain access to the proteolytic active sites of the enzyme. Protein folding in vivo is mediated by mole...

    Beate C. Braun, Michael Glickman, Regine Kraft, Burkhardt Dahlmann… in Nature Cell Biology (1999)