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Chromatin assembly: biochemical identities and genetic redundancy
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scholarly article
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stated in
Europe PubMed Central
PubMed ID
10322140
retrieved
26 June 2017
review article
1 reference
stated in
Europe PubMed Central
title
Chromatin assembly: biochemical identities and genetic redundancy
(English)
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stated in
Europe PubMed Central
PubMed ID
10322140
retrieved
26 June 2017
main subject
genetic redundancy
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based on heuristic
inferred from title
author name string
Adams CR
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
10322140
retrieved
26 June 2017
Kamakaka RT
series ordinal
2
1 reference
stated in
Europe PubMed Central
PubMed ID
10322140
retrieved
26 June 2017
publication date
1 April 1999
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stated in
Europe PubMed Central
PubMed ID
10322140
retrieved
26 June 2017
published in
Current Opinion in Genetics & Development
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stated in
Europe PubMed Central
PubMed ID
10322140
retrieved
26 June 2017
volume
9
1 reference
stated in
Europe PubMed Central
PubMed ID
10322140
retrieved
26 June 2017
page(s)
185-190
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stated in
Europe PubMed Central
PubMed ID
10322140
retrieved
26 June 2017
issue
2
1 reference
stated in
Europe PubMed Central
PubMed ID
10322140
retrieved
26 June 2017
cites work
Structure, dynamics, and function of chromatin in vitro.
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https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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Chromatin replication
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The regulation of histone synthesis in the cell cycle
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Yeast histone H3 and H4 amino termini are important for nucleosome assembly in vivo and in vitro: redundant and position-independent functions in assembly but not in gene regulation
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reference URL
https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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7 January 2021
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Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase
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A search for proteins that interact genetically with histone H3 and H4 amino termini uncovers novel regulators of the Swe1 kinase in Saccharomyces cerevisiae
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Histone H4 and the maintenance of genome integrity
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https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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Checkpoints on the road to mitosis
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7 January 2021
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The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism
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7 January 2021
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Identification of a gene encoding a yeast histone H4 acetyltransferase
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Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4
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Chromatin assembly factors: a dual function in nucleosome formation and mobilization?
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https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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7 January 2021
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Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro
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https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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The p150 and p60 subunits of chromatin assembly factor I: a molecular link between newly synthesized histones and DNA replication
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Postreplicative chromatin assembly by Drosophila and human chromatin assembly factor 1
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Ultraviolet radiation sensitivity and reduction of telomeric silencing in Saccharomyces cerevisiae cells lacking chromatin assembly factor-I.
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https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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7 January 2021
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RLF2, a subunit of yeast chromatin assembly factor-I, is required for telomeric chromatin function in vivo
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7 January 2021
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The p55 subunit of Drosophila chromatin assembly factor 1 is homologous to a histone deacetylase-associated protein
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Chromatin assembly factor 1 (CAF-1) colocalizes with replication foci in HeLa cell nuclei
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7 January 2021
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Effects of histone H4 depletion on the cell cycle and transcription of Saccharomyces cerevisiae
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https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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7 January 2021
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Evidence that Spt6p controls chromatin structure by a direct interaction with histones
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https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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7 January 2021
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Soluble acidic complexes containing histones H3 and H4 in nuclei of Xenopus laevis oocytes
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https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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Chromatin assembly coupled to DNA repair: a new role for chromatin assembly factor I.
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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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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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https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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7 January 2021
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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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Histones in transit: cytosolic histone complexes and diacetylation of H4 during nucleosome assembly in human cells
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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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Members of the NAP/SET family of proteins interact specifically with B-type cyclins
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https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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Control of mitotic events by Nap1 and the Gin4 kinase
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Potentiation of RNA polymerase II transcription by Gal4-VP16 during but not after DNA replication and chromatin assembly
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ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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7 January 2021
based on heuristic
inferred from DOI database lookup
DNA-dependent phosphorylation of histone H2A.X during nucleosome assembly in Xenopus laevis oocytes: involvement of protein phosphorylation in nucleosome spacing.
1 reference
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https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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7 January 2021
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Cse4p is a component of the core centromere of Saccharomyces cerevisiae
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
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7 January 2021
based on heuristic
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Histone acetylation reduces H1-mediated nucleosome interactions during chromatin assembly
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0959-437X%2899%2980028-8
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1016/S0959-437X(99)80028-8
1 reference
stated in
Europe PubMed Central
PubMed ID
10322140
retrieved
26 June 2017
PubMed ID
10322140
1 reference
stated in
Europe PubMed Central
PubMed ID
10322140
retrieved
26 June 2017
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