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1 d with storage chaperone proteins, including nucleoplasmin.
2 0) are removed from erythrocyte chromatin by nucleoplasmin.
3 osome remains intact even in the presence of nucleoplasmin.
4 e T antigen or the standard bipartite NLS of nucleoplasmin.
5 chromatin, a process that can be mediated by nucleoplasmin.
6 C causes it to dissociate from nucleophosmin/nucleoplasmin.
7 oocyte extracts or hypophosphorylated oocyte nucleoplasmin.
8 hts into the mechanism of histone binding by nucleoplasmins.
9 not form a decamer, unlike certain classical nucleoplasmins.
12 mplementary DNA for a highly acidic protein, nucleoplasmin 3 (NPM3), was found in multiple positive c
13 nced homology to the histone binding site of nucleoplasmin, a chromatin remodeling protein found in X
15 for this reaction, and have shown that it is nucleoplasmin, a previously known chromatin remodelling
16 On the basis of the similarity of Npm3 to nucleoplasmin and nucleophosmin in amino acid sequence,
18 the nuclear localization sequences (NLSs) of nucleoplasmin and the tumor suppressor p53 in human cell
21 luster downstream of the bipartite signal of nucleoplasmin can be directed to the nucleus by flanking
24 extracts or purified hyperphosphorylated egg nucleoplasmin decondense sperm chromatin and remove sper
27 additional A2 acidic tract C-terminal to the nucleoplasmin domain for interaction with histone H3/H4
28 her characterization revealed the N-terminal nucleoplasmin domain to interact with H2A/H2B and H3/H4
34 s of loop mutations support the premise that nucleoplasmins form decamers when they bind H2A-H2B dime
39 We conclude that hyperphosphorylation of nucleoplasmin is used to modulate the rapid changes in c
40 ructure confirmed that Pf indeed possesses a nucleoplasmin isoform (PfNPM), and the N-terminal core d
41 ly discovered that consists of an N-terminal nucleoplasmin-like (NPL) domain and a C-terminal FKBP pe
42 Here, we report the first structure of a nucleoplasmin-like domain (NPL) from the unrelated Droso
43 family of proteins that share the pentameric nucleoplasmin-like NPL domain and are found in protists,
44 tin assembly system comprises the Drosophila nucleoplasmin-like protein (dNLP) histone chaperone, the
45 l transcription regulator, which resembles a nucleoplasmin-like protein (NLP) with an AT-hook motif.
48 The experimental confirmation that HDTs are nucleoplasmins may spark new interest in this enigmatic
49 Addition of the histone binding protein, nucleoplasmin, mediated the displacement of the core his
52 ure, and sequence analysis revealed that the nucleoplasmin NLS coding sequence was deleted from the g
61 e also resolved the 3D cryo-EM structures of nucleoplasmin NPM2 co-isolated with the linker histone H
62 structures to enhance protamine dismissal by nucleoplasmin (NPM2) and enable the recruitment of HIRA
63 onation, we identified the histone chaperone nucleoplasmin (Npm2) as a putative nuclear size effector
64 of, and may share basic functions with, the nucleoplasmin/ nucleophosmin family of molecular chapero
66 udies showed that the nuclear phosphoprotein nucleoplasmin performs the first stage of chromatin deco
67 r localization signal (NLS) derived from the nucleoplasmin protein was inserted into the Myr1E Gag se
68 sphorylated CPC interacts with nucleophosmin/nucleoplasmin proteins, which are known to oligomerize i
69 m nuclei can be licensed by a combination of nucleoplasmin, RLF-M and a partially purified fraction t
70 hether the nuclear targeting activity of the nucleoplasmin sequence was responsible for the infectivi
73 activity, SW1-SNF, or the histone chaperone, nucleoplasmin, suggesting that the binding of these fact
74 tional nucleolar protein and a member of the nucleoplasmin superfamily of acidic histone chaperones.
75 nds upon the massive hyperphosphorylation of nucleoplasmin that occurs when oocytes mature into eggs.
78 ls an increased association of the chaperone nucleoplasmin with ribonucleoprotein particles dependent