histone


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Related to histone: nonhistone

his·tone

 (hĭs′tōn′)
n.
Any of several basic proteins found in association with the DNA in the chromatin of eukaryotes.

histone

(ˈhɪstəʊn)
n
(Biochemistry) any of a group of basic proteins present in cell nuclei and implicated in the spatial organization of DNA

his•tone

(ˈhɪs toʊn)

n.
any of a group of five small basic proteins, occurring in the nucleus of eukaryotic cells, that organize DNA strands into nucleosomes by forming molecular complexes around which the DNA winds.
[< German Histon (1884) = hist- of uncertain orig. + -on, perhaps after Pepton peptone]

his·tone

(hĭs′tōn′)
Any of several proteins that, together with DNA, make up most of the chromatin in a cell nucleus.
ThesaurusAntonymsRelated WordsSynonymsLegend:
Noun1.histone - a simple protein containing mainly basic amino acids; present in cell nuclei in association with nucleic acids
simple protein - a protein that yields only amino acids when hydrolyzed
Translations
histone
References in periodicals archive ?
- US-based histone deacetylase inhibitors developer OnKure, Inc has entered into an exclusive license and option agreement with Massachusetts-based KDAc Therapeutics, Inc.
In the nucleus of cells, DNA wraps itself around histone proteins forming a 'beads-on-a-string' structure called chromatin.
According to the company, CS3003 is a small molecule inhibitor that selectively targets histone deacetylase 6 (HDAC6).
A number of potential approaches have been proposed for the treatment of cancer, but histone deacetylase inhibitors (HDACIs) are the emerging ones.
For the first time, through this research study "Histone Deacetylase Inhibition Restores Expression of Hypoxia-Inducible Protein NDRG1 in Pancreatic Cancer," Celine Tiffon confirms that the restoration of cellular differentiation is coupled to cell growth inhibition in-vitro by histone or non-histone protein acetylation, which increased NDRG1 expression, and restored responsiveness to hypoxia.
Evidence shows that DNA methylation, histone post-translational modifications, and micro-RNA (miRNA)-associated gene silencing are found in both human and animal models of PAH (8).
The new study looked at an epigenetic therapy that inhibits the enzyme G9a, a type of histone methyltransferase.
Onconova Therapeutics, a Phase 3 clinical-stage biopharmaceutical company focused on discovering and developing novel products to treat cancer, with a primary focus on Myelodysplastic Syndromes, announced the presentation of new data highlighting the mechanism of action of rigosertib in combination with azacitidine at the American Association for Cancer Research Special Conference on "Targeting DNA Methylation and Chromatin for Cancer Therapy." The epigenetic events modulated by rigosertib in combination with either agent resulted in global histone post-translational modifications, differential Pol II association with active histone marks, epigenetic reprogramming of pluripotency genes, and expansion of primitive hematopoietic pluripotent stem cells.
Some histone modifications compact the DNA to hide a gene from the cell's protein-making machinery and consequently turn gene "off." They can also loosen up DNA for gene exposure to turn gene "on."
We were interested in the role histone acetylation/deacetylation plays as a potential treatment strategy for sarcomas that are typically insensitive to traditional chemotherapeutic agents.
Acetylation and deacetylation on different positions of the N-terminal tail of core histones by histone acetylases (HATs) and histone deacetylases (HDACs) change the nucleosomal conformation of cells [1].
To date, the most commonly epigenetic changes include DNA methylation and histone modifications, such as methylation and acetylation at lysine residues.