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1 localization of nucleolar granular component protein B23.
6 significant amounts of monomer were present, protein B23.1 was capable of binding DNA, whereas condit
10 mentation characteristics similar to that of protein B23.1, suggesting that the carboxyl-terminal end
13 cleolin, the previously identified nucleolar proteins B23 and fibrillarin, proteins with electrophore
14 leolar (sno)RNA, fibrillarin, nucleolin, and proteins B23 and p52, accumulate in perichromosomal regi
16 d the abundant and multifunctional nucleolar protein B23 as a potential target of FRGY2a and its rela
17 enhanced the rate of CK2 phosphorylation of protein B23 by 2-3-fold, and this enhancement was depend
19 f the processing machinery, suggest that the protein B23 endoribonuclease could play a role in pre-rR
22 in the granular component, as marked by the protein B23, indicating a possible interaction with ribo
27 directly hydrolyze ATP, substrate release by protein B23 is dependent on its phosphorylation by CK2.
29 two-hybrid system which identified nucleolar protein B23 (nucleophosmin) as being associated with C23
30 ts the interaction of ARF with the nucleolar protein B23(nucleophosmin) and promotes a transient p53-
33 pproach, we then evaluated whether nucleolar proteins B23/nucleophosmin and nucleolin, previously sho
40 mponent of the segregated nucleolus, whereas protein B23 was found predominantly in the nucleoplasm.
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