Results 21 to 30 of about 196,399 (287)

Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork [PDF]

open access: yes, 2015
International audienceMCM2 is a subunit of the replicative helicase machinery shown to interact with histones H3 and H4 during the replication process through its N-terminal domain.
Almouzni, Geneviève   +13 more
core   +10 more sources

Investigation of in vitro histone H3 glycosylation using H3 tail peptides

open access: yesScientific Reports, 2022
Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
Jona Merx   +10 more
doaj   +1 more source

Probing the (H3-H4)(2) histone tetramer structure using pulsed EPR spectroscopy combined with site-directed spin labelling [PDF]

open access: yes, 2009
The (H3-H4)2 histone tetramer forms the central core of nucleosomes and, as such, plays a prominent role in assembly, disassembly and positioning of nucleosomes.
Bowman, A.   +4 more
core   +5 more sources

The Histone Deacetylase Complex (HDC) 1 protein of Arabidopsis thaliana has the capacity to interact with multiple proteins including histone 3-binding proteins and histone 1 variants [PDF]

open access: yes, 2016
Intrinsically disordered proteins can adopt multiple conformations thereby enabling interaction with a wide variety of partners. They often serve as hubs in protein interaction networks. We have previously shown that the Histone Deacetylase Complex (HDC)
Amtmann, Anna   +6 more
core   +1 more source

Extracellular histone H3 [PDF]

open access: yes, 2020
This research was aimed at studying histone proteins in tissue damage. An important finding was that the more histones were present in donor kidneys during machine preservation, the poorer the organ function after transplantation. The amount of histones seems to be related to the amount of kidney damage.
openaire   +1 more source

Histone Variant H3.3 Mutations in Defining the Chromatin Function in Mammals

open access: yesCells, 2020
The systematic mutation of histone 3 (H3) genes in model organisms has proven to be a valuable tool to distinguish the functional role of histone residues.
Matteo Trovato   +3 more
doaj   +1 more source

PRB1 is required for clipping of the histone H3 N terminal tail in Saccharomyces cerevisiae.

open access: yesPLoS ONE, 2014
Cathepsin L, a lysosomal protein in mouse embryonic stem cells has been shown to clip the histone H3 N- terminus, an activity associated with gene activity during mouse cell development.
Yong Xue   +4 more
doaj   +1 more source

Evidence for gene-specific rather than transcription rate-dependent histone H3 exchange in yeast coding regions. [PDF]

open access: yesPLoS Computational Biology, 2009
In eukaryotic organisms, histones are dynamically exchanged independently of DNA replication. Recent reports show that different coding regions differ in their amount of replication-independent histone H3 exchange.
Irit Gat-Viks, Martin Vingron
doaj   +1 more source

Characteristic H3 N-tail dynamics in the nucleosome core particle, nucleosome, and chromatosome

open access: yesiScience, 2022
Summary: The nucleosome core particle (NCP) comprises a histone octamer, wrapped around by ∼146-bp DNA, while the nucleosome additionally contains linker DNA.
Ayako Furukawa   +7 more
doaj   +1 more source

The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3–H4 tetramers and Asf1–H3–H4 complexes [PDF]

open access: yes, 2016
Wellcome Trust [094090, 097945, 099149]; Medical Research Council [G1100021]. Funding for open access charge: Wellcome Trust.Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography.
Angus Lamond   +11 more
core   +3 more sources

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