ArticleThe EMBO journal1987
Purification of a novel, nucleoplasmin-like protein from somatic nuclei.
Article in The EMBO journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 35 citations in OpenAlex.
- Identification of a small, very acidic constitutive nucleolar protein (NO29) as a member of the nucleoplasmin family.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Molecular cloning and functional characterization of a cDNA encoding nucleosome assembly protein 1 (NAP-1) from soybean.Molecular & general genetics : MGG · 1995Article
- DF 31, a sperm decondensation factor from Drosophila melanogaster: purification and characterization.The EMBO journal · 1995Article
- A histone-binding protein, nucleoplasmin, stimulates transcription factor binding to nucleosomes and factor-induced nucleosome disassembly.The EMBO journal · 1994Article
- Nucleosome assembly in vitro: separate histone transfer and synergistic interaction of native histone complexes purified from nuclei of Xenopus laevis oocytes.The EMBO journal · 1990Article
- On the biological role of histone acetylation.The Biochemical journal · 1990Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
We have purified a nucleoplasmin-like protein from the nuclei of somatic Xenopus laevis cells. This protein possesses a number of the distinctive features of nucleoplasmin isolated from oocytes or unfertilized eggs. The protein is recognized by both monoclonal and polyclonal antisera raised against egg nucleoplasmin. The protein has an oligomeric structure, which must be heated in SDS to completely dissociate, is acidic, phosphorylated and efficiently promotes the in vitro formation of chromatin. We have partially characterized this novel protein and because of its resemblance to nucleoplasmin isolated from oocytes or unfertilized eggs we have named this protein nucleoplasmin S.
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