The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding (Q27640458)

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James Head

object named as

James F Head

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author name string

V M Haridasan Namboodiri

1

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Ildikó V Akey

ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster

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language of work or name

English

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publication date

February 2003

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published in

Structure

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volume

11

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issue

2

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page(s)

175-86

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cites work

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Chromatin assembly in vitro and in vivo

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Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence

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Silver staining, immunofluorescence, and immunoelectron microscopic localization of nucleolar phosphoproteins B23 and C23

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A constitutive nucleolar protein identified as a member of the nucleoplasmin family.

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Identification of a small, very acidic constitutive nucleolar protein (NO29) as a member of the nucleoplasmin family

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Major nucleolar proteins shuttle between nucleus and cytoplasm

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Identification of nucleophosmin/B23, an acidic nucleolar protein, as a stimulatory factor for in vitro replication of adenovirus DNA complexed with viral basic core proteins.

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Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA

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Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus egg extracts

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Nucleoplasmin remodels sperm chromatin in Xenopus egg extracts

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Template activating factor-I remodels the chromatin structure and stimulates transcription from the chromatin template

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DOI

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Consolidated OpenCitations Corpus – April 2017

release_4el7kmiswzdafbr2jzezeqzqae

3896326

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https://api.fatcat.wiki/v0/release/4el7kmiswzdafbr2jzezeqzqae

24 November 2022

mapped directly with Wikidata item

3896326

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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