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Histone chaperones and nucleosome assembly
scientific article
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scholarly article
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review article
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stated in
Europe PubMed Central
title
Histone chaperones and nucleosome assembly
(English)
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main subject
molecular chaperones
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Nucleophosmin/nucleoplasmin 2
1 reference
stated in
GOA release 2020-03-11
histone binding
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stated in
GOA release 2020-03-11
author
Karolin Luger
series ordinal
2
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Christopher W Akey
object named as
Christopher W Akey
series ordinal
1
1 reference
stated in
ORCID Public Data File 2021
language of work or name
English
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publication date
February 2003
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published in
Current Opinion in Structural Biology
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volume
13
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page(s)
6-14
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issue
1
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cites work
Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
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The core histone N termini function independently of linker histones during chromatin condensation.
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Molecular biology. Chromatin higher order folding--wrapping up transcription
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Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions
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Chromatin assembly during S phase: contributions from histone deposition, DNA replication and the cell division cycle.
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Chromatin assembly. Cooperation between histone chaperones and ATP-dependent nucleosome remodeling machines
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reference URL
https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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Crystal structure of the nucleosome core particle at 2.8 A resolution
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The atomic structure of the nucleosome core particle.
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Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
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Asymmetries in the nucleosome core particle at 2.5 A resolution
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Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
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Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution
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The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly
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The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding
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Special HATs for special occasions: linking histone acetylation to chromatin assembly and gene activation
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7 January 2021
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Multistep chromatin assembly on supercoiled plasmid DNA by nucleosome assembly protein-1 and ATP-utilizing chromatin assembly and remodeling factor
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Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin
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A CAF-1-PCNA-mediated chromatin assembly pathway triggered by sensing DNA damage
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7 January 2021
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Chromatin assembly factor I contributes to the maintenance, but not the re-establishment, of silencing at the yeast silent mating loci
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Hir proteins are required for position-dependent gene silencing in Saccharomyces cerevisiae in the absence of chromatin assembly factor I
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7 January 2021
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The RCAF complex mediates chromatin assembly during DNA replication and repair
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7 January 2021
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Interaction between the Drosophila CAF-1 and ASF1 chromatin assembly factors
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7 January 2021
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Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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Drosophila NAP-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays
1 reference
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7 January 2021
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Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B.
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The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly
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7 January 2021
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Histone H3 variants specify modes of chromatin assembly
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7 January 2021
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HIRA Is Critical for a Nucleosome Assembly Pathway Independent of DNA Synthesis
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7 January 2021
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Spt5 and spt6 are associated with active transcription and have characteristics of general elongation factors in D. melanogaster
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7 January 2021
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The many faces of chromatin remodeling: SWItching beyond transcription
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SWI2/SNF2 and related proteins: ATP-driven motors that disrupt protein-DNA interactions?
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7 January 2021
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Dynamics of ATP-dependent chromatin assembly by ACF.
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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inferred from DOI database lookup
Biochemical analysis of chromatin containing recombinant Drosophila core histones
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7 January 2021
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p300-mediated tax transactivation from recombinant chromatin: histone tail deletion mimics coactivator function
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7 January 2021
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Nuclear chaperones
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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inferred from DOI database lookup
Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus egg extracts
1 reference
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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Nucleoplasmin remodels sperm chromatin in Xenopus egg extracts
1 reference
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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Nucleosome assembly in vitro: separate histone transfer and synergistic interaction of native histone complexes purified from nuclei of Xenopus laevis oocytes.
1 reference
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Crossref
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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Sperm chromatin decondensation by template activating factor I through direct interaction with basic proteins
1 reference
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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Acidic polypeptides can assemble both histones and chromatin in vitro at physiological ionic strength
1 reference
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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DNA binding within the nucleosome core
1 reference
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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DNA-dependent divalent cation binding in the nucleosome core particle
1 reference
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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An acidic protein which assembles nucleosomes in vitro is the most abundant protein in Xenopus oocyte nuclei
1 reference
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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inferred from DOI database lookup
The synthesis and storage of histones during the oogenesis of Xenopus laevis
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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Purification of a novel, nucleoplasmin-like protein from somatic nuclei.
1 reference
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7 January 2021
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Coiled-coil structure-mediated dimerization of template activating factor-I is critical for its chromatin remodeling activity.
1 reference
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7 January 2021
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Molecular and cellular characterization of CRP1, a Drosophila chromatin decondensation protein.
1 reference
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster
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Crossref
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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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.
1 reference
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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A histone-binding protein, nucleoplasmin, stimulates transcription factor binding to nucleosomes and factor-induced nucleosome disassembly.
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https://api.crossref.org/works/10.1016%2FS0959-440X%2803%2900002-2
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7 January 2021
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Remodeling the chromatin structure of a nucleosome array by transcription factor-targeted trans-displacement of histones.
1 reference
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7 January 2021
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Deviant nucleosomes: the functional specialization of chromatin
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7 January 2021
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SETOR: hardware-lighted three-dimensional solid model representations of macromolecules
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7 January 2021
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Identifiers
DOI
10.1016/S0959-440X(03)00002-2
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1624246
OpenCitations bibliographic resource ID
1624246
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1624246
PubMed ID
12581654
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1624246
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