Results 71 to 80 of about 360,616 (327)

Effect of the HDAC Inhibitor on Histone Acetylation and Methyltransferases in A2780 Ovarian Cancer Cells

open access: yesMedicina, 2021
Background andObjective: Epigenetic modifications are believed to play a significant role in the development of cancer progression, growth, differentiation, and cell death. One of the most popular histone deacetylases inhibitors (HDACIs), suberoylanilide
Umamaheswari Natarajan   +2 more
doaj   +1 more source

Histone Deacetylases and Histone Deacetylase Inhibitors: Molecular Mechanisms of Action in Various Cancers

open access: yesAdvanced Biomedical Research, 2019
Epigenetic modifications such as histone modification play an important role in tumorigenesis. There are several evidence that histone deacetylases (HDACs) play a key role in cancer induction and progression by histone deacetylation.
M. Sanaei, F. Kavoosi
semanticscholar   +1 more source

H3 Lysine 4 Is Acetylated at Active Gene Promoters and Is Regulated by H3 Lysine 4 Methylation [PDF]

open access: yes, 2011
Methylation of histone H3 lysine 4 (H3K4me) is an evolutionarily conserved modification whose role in the regulation of gene expression has been extensively studied.
Richard J. Festenstein   +31 more
core   +1 more source

Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis

open access: yesMolecular Systems Biology, 2017
Histone deacetylases have central functions in regulating stress defenses and development in plants. However, the knowledge about the deacetylase functions is largely limited to histones, although these enzymes were found in diverse subcellular ...
Markus Hartl   +15 more
doaj   +1 more source

Comparative effects of histone deacetylases inhibitors and resveratrol on Trypanosoma cruzi replication, differentiation, infectivity and gene expression

open access: yesInternational Journal for Parasitology: Drugs and Drug Resistance, 2017
Histone post-translational modification, mediated by histone acetyltransferases and deacetylases, is one of the most studied factors affecting gene expression.
Vanina A. Campo
doaj   +1 more source

Histone deacetylases and cancer [PDF]

open access: yesMolecular Oncology, 2012
Reversible acetylation of histone and non‐histone proteins is one of the most abundant post‐translational modifications in eukaryotic cells. Protein acetylation and deacetylation are achieved by the antagonistic actions of two families of enzymes, histone acetyltransferases (HATs) and histone deacetylases (HDACs).
Bruna, Barneda-Zahonero, Maribel, Parra
openaire   +2 more sources

Beyond Histone and Deacetylase: An Overview of Cytoplasmic Histone Deacetylases and Their Nonhistone Substrates [PDF]

open access: yes, 2011
Acetylation of lysines is a prominent form of modification in mammalian proteins. Deacetylation of proteins is catalyzed by histone deacetylases, traditionally named after their role in histone deacetylation, transcriptional modulation, and epigenetic ...
Yang, Wen-Ming   +3 more
core   +1 more source

Histone Deacetylases (HDACs) Guided Novel Therapies for T-cell lymphomas

open access: yesInternational Journal of Medical Sciences, 2019
T-cell lymphomas are a heterogeneous group of cancers with different pathogenesis and poor prognosis. Histone deacetylases (HDACs) are epigenetic modifiers that modulate many key biological processes.
Qing Zhang   +3 more
semanticscholar   +1 more source

Gut microbiome and aging—A dynamic interplay of microbes, metabolites, and the immune system

open access: yesFEBS Letters, EarlyView.
Age‐dependent shifts in microbial communities engender shifts in microbial metabolite profiles. These in turn drive shifts in barrier surface permeability of the gut and brain and induce immune activation. When paired with preexisting age‐related chronic inflammation this increases the risk of neuroinflammation and neurodegenerative diseases.
Aaron Mehl, Eran Blacher
wiley   +1 more source

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

open access: yesFEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai   +4 more
wiley   +1 more source

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