(Q43168049)

15 November 2017

title

AtFKBP53 is a histone chaperone required for repression of ribosomal RNA gene expression in Arabidopsis (English)

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15 November 2017

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Hong Li

1

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15 November 2017

Sheng Luan

series ordinal

2

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15 November 2017

publication date

9 February 2010

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15 November 2017

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15 November 2017

volume

20

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15 November 2017

issue

3

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15 November 2017

page(s)

357-366

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https://scigraph.springernature.com/pub.10.1038/cr.2010.22

15 November 2017

exact match

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cites work

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Drosophila NAP-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays

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Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone

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A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing

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The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus.

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Nucleolin is a histone chaperone with FACT-like activity and assists remodeling of nucleosomes

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Arabidopsis NRP1 and NRP2 encode histone chaperones and are required for maintaining postembryonic root growth.

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A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models

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The yeast histone chaperone chromatin assembly factor 1 protects against double-strand DNA-damaging agents

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A WD40 domain cyclophilin interacts with histone H3 and functions in gene repression and organogenesis in Arabidopsis.

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An oncoprotein from the plant pathogen agrobacterium has histone chaperone-like activity

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Dependence of heterochromatic histone H3 methylation patterns on the Arabidopsis gene DDM1.

21 January 2018

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Dissection of Arabidopsis ADP-RIBOSYLATION FACTOR 1 function in epidermal cell polarity

21 January 2018

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Structure and Function of the Conserved Core of Histone Deposition Protein Asf1

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inferred from DOI database lookup

7 January 2021

based on heuristic

Highly acidic C-terminal domain of pp32 is required for the interaction with histone chaperone, TAF-Ibeta

1 reference

https://api.crossref.org/works/10.1038%2FCR.2010.22

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/CR.2010.22

1 reference

Dimensions Publication ID

15 November 2017

1024045230

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1 reference