Yu. Ya. Zaikova

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We have performed the iTRAQ mass spectrometry analysis of extracellular proteasomes and revealed posttranslational modifications (PTMs) of subunits of extracellular 26S proteasomes. There are novel sites of ubiquitination and acetylation found in the proteasome subunits α2 (K196), α4 (K189 and K234), α6 (K217), and Rpn6 (A2). We have revealed that the(More)
The 26S proteasome is a multisubunit protein complex responsible for selective protein degradation in the cell. A number of proteins with known and unknown functions were shown to be permanently or temporarily associated with 26S proteasomes. Identification of proteins that interact with proteasomes is an important step in the understanding of the(More)
In this manuscript we compared the biochemical properties of intracellular (cytoplasmic) and extracellular (secreted) proteasomes by their peptidase activities and the levels of phosphorylation of their subunits judged by relative mobility in two-dimensional gel electrophoresis and immunoblotting with phospho-specific antibodies. A comparative analysis of(More)
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