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Inhibition of Histone Deacetylases | SpringerLink
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Lysine acetylation of histones is one of the major epigenetic regulators of chromatin conformation and gene expression. The dynamic nature of histone acetylation is determined by the counterbalancing activity of histone acetyltransferase and histone deacetylase...
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google, scholar, pubmed, article, cas, histone, cancer, deacetylase, biol, davidson, methods, inhibitors, chromatin, hdac, inhibition, acetylation, cells, protocol, genes, chem, breast, mol, nat, cell, human, privacy, cookies, content, information, publish, research, deacetylases, expression, activity, access, res, estrogen, chipchip, analysis, data, search, epigenetics, protocols, huang, shaw, lysine, histones, epigenetic, nature, open,
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month download article/chapter hdac inhibitor-based therapies silac-based proteomic analysis estrogen receptor alpha cutaneous t-cell lymphomas cutaneous t-cell lymphoma aberrantly silenced genes histone deacetylase inhibitor chip-chip data analysis epigenetics protocols histone deacetylase inhibitors lysine-specific demethylase 1 privacy choices/manage cookies lysine acetylation revealed device instant download mammalian histone deacetylase chip-chip molecular methods cultured mammalian cells human hdac7 harbors support vector machines humana press histone deacetylases inhibitors histone deacetylases protocol histone deacetylase inhibition journal finder publish cancer therapy cryptic deacetylase activity protein phosphatase 2a combinatorial histone codes protein-dna interaction breast cancer res tumor-selective action genome-wide analysis unknown target genes european economic area recent technological developments high throughput characterization genome-wide mapping human transcription factors polyamine analogues results author information authors editor information editors ii histone deacetylases dna microarray hybridization conditions privacy policy major epigenetic regulators transcriptionally active chromatin structure-activity relationships promoter dna hypermethylation nucleic acids res
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ScholarlyArticle:
headline:Inhibition of Histone Deacetylases
pageEnd:311
pageStart:297
image:https://media.springernature.com/w153/springer-static/cover/book/978-1-61779-316-5.jpg
genre:
Springer Protocols
isPartOf:
name:Epigenetics Protocols
isbn:
978-1-61779-316-5
978-1-61779-315-8
type:Book
publisher:
name:Humana Press
logo:
url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
type:ImageObject
type:Organization
author:
name:Yi Huang
affiliation:
name:University of Pittsburgh Cancer Institute
address:
name:University of Pittsburgh Cancer Institute, Pittsburgh, USA
type:PostalAddress
type:Organization
type:Person
name:Patrick G. Shaw
affiliation:
name:University of Pittsburgh Cancer Institute
address:
name:University of Pittsburgh Cancer Institute, Pittsburgh, USA
type:PostalAddress
type:Organization
type:Person
name:Nancy E. Davidson
affiliation:
name:University of Pittsburgh Cancer Institute
address:
name:University of Pittsburgh Cancer Institute, Pittsburgh, USA
type:PostalAddress
type:Organization
email:[email protected]
type:Person
keywords:Histone deacetylases, Histone acetyltransferases, HDAC inhibitors, Epigenetic gene silencing, Chromatin remodeling
description:Lysine acetylation of histones is one of the major epigenetic regulators of chromatin conformation and gene expression. The dynamic nature of histone acetylation is determined by the counterbalancing activity of histone acetyltransferase and histone deacetylase (HDAC) enzymes. Acetylation of histones is generally associated with open and transcriptionally active chromatin, whereas the activity of HDACs leads to histone deacetylation, condensation of chromatin, and inhibition of transcription. Aberrant silencing of tumor suppressors and other genes has been found in different types of cancer. Abnormal activity of HDACs has been implicated in tumorigenesis and therefore considerable effort has been put into the development of HDAC inhibitors as a means of modifying histone acetylation status and reexpressing aberrantly silenced tumor suppressor genes. This has led to the generation of a number of structurally diverse compounds that can effectively inhibit HDAC activity, thus altering chromatin structure in cancer cells. This unit discusses the methods and recent technological developments with respect to the studies of HDAC inhibition in cancer.
datePublished:2011
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978-1-61779-316-5
978-1-61779-315-8
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name:University of Pittsburgh Cancer Institute
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name:University of Pittsburgh Cancer Institute
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name:Nancy E. Davidson
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name:University of Pittsburgh Cancer Institute
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name:University of Pittsburgh Cancer Institute, Pittsburgh, USA
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