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1 localization of nucleolar granular component protein B23.
2                           Phosphorylation of protein B23.1 by casein kinase II produced an additional
3                              Mutant forms of protein B23.1 in which the nuclear localization signal w
4 suggesting that the carboxyl-terminal end of protein B23.1 is not essential for oligomerization.
5                                The effect of protein B23.1 oligomerization on its interaction with a
6 significant amounts of monomer were present, protein B23.1 was capable of binding DNA, whereas condit
7                  This effect was not seen if protein B23.1 was phosphorylated with a cdc2 type protei
8          Under low ionic strength conditions protein B23.1 was predominantly a 2.1S monomer with smal
9                                              Protein B23.1 was previously shown to bind nucleic acids
10 mentation characteristics similar to that of protein B23.1, suggesting that the carboxyl-terminal end
11 he oligomerization properties of recombinant proteins B23.1 and B23.2.
12                                              Protein B23.2, the carboxyl-terminal truncated isoform,
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
15                                     Two host proteins, B23 and I2PP2A, were found to interact prefere
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
18                                              Protein B23 can be phosphorylated by protein kinase CK2
19 f the processing machinery, suggest that the protein B23 endoribonuclease could play a role in pre-rR
20                   These studies suggest that protein B23 exists in an equilibrium between monomer and
21                 Previous studies showed that protein B23 has several characteristics typical of molec
22  in the granular component, as marked by the protein B23, indicating a possible interaction with ribo
23                                              Protein B23 is a major nonribosomal nucleolar protein an
24                                              Protein B23 is a multifunctional nucleolar protein whose
25                                              Protein B23 is a multifunctional nucleolar protein whose
26                                              Protein B23 is an abundant nucleolar protein and a putat
27 directly hydrolyze ATP, substrate release by protein B23 is dependent on its phosphorylation by CK2.
28  to interact functionally with the nucleolar protein B23/NPM (B23) and inhibit rRNA biogenesis.
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-
31                                              Protein B23/nucleophosmin is a multifunctional protein t
32                                              Protein B23/nucleophosmin/numatrin (B23) is a key nucleo
33 pproach, we then evaluated whether nucleolar proteins B23/nucleophosmin and nucleolin, previously sho
34                               The effects of protein B23 on nuclear import were determined by an in v
35                   These results suggest that protein B23 plays a role as an accessory factor in the n
36 m stimulation (2-3-fold) at a molar ratio of protein B23:Rev of approximately 1:1.
37                                The action of protein B23 ribonuclease on different regions of pre-rRN
38                                              Protein B23 ribonuclease preferentially cleaved the sing
39  import of either substrate was increased if protein B23 was added to the incubation medium.
40 mponent of the segregated nucleolus, whereas protein B23 was found predominantly in the nucleoplasm.
41                            Nucleolar shuttle protein B23 was found to bind to human immunodeficiency
42 dary structure on the cleavage preference by protein B23 were studied.

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