Results 1 to 10 of about 114,204 (164)
LPS-Challenged Macrophages Release Microvesicles Coated With Histones
Frontiers in Immunology, 2018 Histones are the protein component of nucleosomes, which are the basic packing unit of chromatin. However, histones are also found in the blood, both as components of nucleosomes leaked out from dead cells, or expelled from neutrophils in the active ...
Alessandra Agresti +2 more
exaly +3 more sources
Structure and function of archaeal histones [PDF]
PLoS Genetics, 2018 The genomes of all organisms throughout the tree of life are compacted and organized in chromatin by association of chromatin proteins. Eukaryotic genomes encode histones, which are assembled on the genome into octamers, yielding nucleosomes.
Remus T Damé +2 more
exaly +2 more sources
A feedback loop sustaining neutrophil extracellular trap formation involves S100 proteins, histones, TLR2 and RAGE, and is restrained by albumin [PDF]
Frontiers in ImmunologyNeutrophil extracellular trap (NET) generation must be tightly controlled as this essential antimicrobial response can also cause tissue damage and contribute to various pathologies.
Vanessa de Carvalho Oliveira +4 more
doaj +2 more sources
Histones and histone variant families in prokaryotes
Nature CommunicationsHistones are important chromatin-organizing proteins in eukaryotes and archaea. They form superhelical structures around which DNA is wrapped. Recent studies have shown that some archaea and bacteria contain alternative histones that exhibit different ...
Samuel Schwab +8 more
doaj +5 more sources
Structural analysis of OCT4 binding to human LIN28B nucleosomes [PDF]
Scientific ReportsStructural studies of nucleosomes most commonly involve histones from Xenopus species or humans. Yet, the effect of subtle differences in the amino acid sequences of these histones on key aspects of structure, such as nucleosome assembly, DNA positioning,
Kalyan K. Sinha, Mario Halic
doaj +2 more sources
Histones and histone modifications [PDF]
Current Biology, 2004 Histone variants, distinct patterns of posttranslational modifications of histones, and histone tail binding proteins all contribute to establishment of various ‘open’ or ‘closed’ chromatin domains that have specialized folding properties and biological functions. Some of these domains can be propagated through DNA replication and mitosis, guaranteeing
Peterson, Craig L, Laniel, Marc-André
openaire +2 more sources
Rapid purification of recombinant histones. [PDF]
PLoS ONE, 2014 The development of methods to assemble nucleosomes from recombinant histones decades ago has transformed chromatin research. Nevertheless, nucleosome reconstitution remains time consuming to this day, not least because the four individual histones must ...
Henrike Klinker +4 more
doaj +1 more source
In vitro interactions of extracellular histones with LDL suggest a potential pro-atherogenic role. [PDF]
PLoS ONE, 2010 Nuclear histones have previously been shown to aggregate LDL in vitro, suggestive of a possible pro-atherogenic role. Recent studies indicate that histones are released during acute inflammation, and therefore might interact with circulating lipoproteins
Alan D Pemberton, Jeremy K Brown
doaj +1 more source
Redox Biochemistry and Chemistry, 2023 In the nucleus, histones are essential in the packaging of DNA and the regulation of gene expression. These histones can also be released to the extracellular space by mechanisms such as necrosis and neutrophil extracellular trap (NET) formation ...
Els A. Hartsema +3 more
doaj +1 more source
Histone clipping: the punctuation in the histone code [PDF]
The EMBO Reports, 2021 Histone clipping was first discovered in the 1960s and still is a lingering mystery. Considering the essential roles of histones in regulating eukaryotic transcription through the histone code, clipping is a post-translational modification that appeals to the imagination.
openaire +2 more sources