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Example sentences for: nucleophosmin
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A nucleic acid binding domain in the C-terminus of nucleophosmin is also lacking in NPM3 and nucleoplasmin, but the known functions of nucleoplasmin in nucleosome assembly and sperm decondensation suggest that this protein, and possibly NPM3, can accomplish intermolecular reactions involving nucleic acids in other ways, perhaps by associating with other proteins that have this binding activity.
To enable an amino acid comparison between NPM3 with other members of the nucleophosmin/nucleoplasmin family, we searched the nonredundant GenBank database using human NPM3, Xenopus nucleoplasmin and human nucleophosmin as BLASTP queries, and 11 additional full-length proteins were retrieved (Table 2).
Multiple phosphorylation sites and nuclear localization signals, or the ability to bind proteins with such signals, are also characteristics of nucleophosmin and nucleoplasmin [ 16 27 28 29 ] . When the functions of NPM3 are elucidated, it will be of interest to determine the contribution of phosphorylation to these activities, since the functions of both nucleoplasmin and nucleophosmin are regulated by phosphorylation, which is extensive in both proteins [ 7 17 ] ).
Some of these activities include nucleic acid binding [ 11 ] , ribonuclease activity (for processing preribosomal RNA) [ 12 ] and association with maturing preribosomal ribonucleoprotein particles [ 13 14 ] . It may also be involved in the transport of ribosomal or other nucleosomal proteins across the nuclear membrane, as it is known to shuttle between the cytoplasm and nucleus and to stimulate the nuclear importation of proteins [ 15 16 ] . Nucleophosmin also appears to be intimately involved in centrosome duplication.
Two well studied proteins that participate in the processes of chromatin and ribosome assembly are nucleoplasmin and nucleophosmin, respectively, two related proteins whose characteristic acidic domains have been shown to bind the basic proteins involved in these processes and present them to the nucleic acid.