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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Histone deacetylase 6

HDAC6, histone deacetylase 6
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to class II of the histone deacetylase/acuc/apha family. It contains an internal duplication of two catalytic domains which appear to function independently of each other. This protein possesses histone deacetylase activity and represses transcription. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Histone, HDAC, CAN, V1a, CYP3A4
Papers using HDAC6 antibodies
Protein Aggregates Are Recruited to Aggresome by Histone Deacetylase 6 via Unanchored Ubiquitin C Termini*
Supplier
Zhai R. Grace et al., In The Journal of Biological Chemistry, 2007
... Purchased protein reagents used in various experiments included: HDAC6 (Biomol), ubiquitin (Boston Biochem), tetraubiquitin ...
Histone modifications affect timing of oligodendrocyte progenitor differentiation in the developing rat brain
Supplier
Casaccia-Bonnefil Patrizia et al., In The Journal of Cell Biology, 2002
... for WB; Upstate Biotechnology); HDAC5 (1:100 for IHC, 1:500 for WB; Santa Cruz Biotechnology, Inc.); HDAC6 (1:100 for IHC, 1:500 for WB; Santa Cruz Biotechnology, Inc.); HDAC7 (1:100 for ...
Papers on HDAC6
Histone deacetylase inhibitors restore IL-10 expression in lipopolysaccharide-induced cell inflammation and reduce IL-1β and IL-6 production in breast silicone implant in C57BL/6J wild-type murine model.
New
Artico et al., Padova, Italy. In Autoimmunity, Feb 2016
In particular, selective HDAC3, HDAC6, and HDAC8 inhibitors have been described to downregulate the expression of pro-inflammatory cytokines (TNF-α, TGF-β, IL-1β, and IL-6).
Class I and IIa HDACs Mediate HIF-1α Stability through PHD2-Dependent Mechanism while HDAC6, a Class IIb Member, Promotes HIF-1α Transcriptional Activity in Nucleus Pulposus Cells of the Intervertebral Disc.
New
Risbud et al., Philadelphia, United States. In J Bone Miner Res, Feb 2016
Noteworthy, selective inhibition of HDAC6 and not of class I and IIa HDACs decreased HIF-1-mediated transcription under hypoxia, to a similar extent as lower-dose TSA, contrasting the reported role of HDAC6 as a transcriptional repressor in other cell types.
Loss of alpha-Tubulin Acetylation is Associated with TGF-beta-induced Epithelial-Mesenchymal Transition.
New
Feng et al., China. In J Biol Chem, Feb 2016
We found that TGF-β increased the activity of HDAC6, a major deacetylase of α-tubulin, without affecting its expression levels.
Essential role of HDAC6 in the regulation of PD-L1 in melanoma.
New
Villagra et al., Fort Lee, United States. In Mol Oncol, Feb 2016
In this context, our present work demonstrates that the pharmacological or genetic abrogation of HDAC6 in primary melanoma samples and cell lines, down-regulates the expression of PD-L1, an important co-stimulatory molecule expressed in cancer cells, which activates the inhibitory regulatory pathway PD-1 in T-cells.
Ciliopathies: Does HDAC6 Represent a New Therapeutic Target?
Review
New
Zhou et al., Tianjin, China. In Trends Pharmacol Sci, Jan 2016
Histone deacetylase 6 (HDAC6) is a unique cytoplasmic enzyme that regulates many biological processes through its deacetylase and ubiquitin-binding activities.
The Shp2-induced epithelial disorganization defect is reversed by HDAC6 inhibition independent of Cdc42.
New
Chang et al., Taipei, Taiwan. In Nat Commun, Dec 2015
HDAC6 suppression reverses oncogenic Shp2-induced multiple apical domains and spindle mis-orientation during division in cysts to acquire normal lumenogenesis.
Tubulin acetylation: responsible enzymes, biological functions and human diseases.
Review
New
Yang et al., Montréal, Canada. In Cell Mol Life Sci, Nov 2015
In mammals, its level is mainly governed by opposing actions of α-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6).
Preclinical and clinical studies of the NEDD9 scaffold protein in cancer and other diseases.
Review
New
Golemis et al., Philadelphia, United States. In Gene, Sep 2015
Downstream, NEDD9 regulation of partners including CRKL, WAVE, PI3K/AKT, ERK, E-cadherin, Aurora-A (AURKA), HDAC6, and others allow NEDD9 to influence functions as pleiotropic as migration, invasion, survival, ciliary resorption, and mitosis.
Improving survival by exploiting tumour dependence on stabilized mutant p53 for treatment.
New
Impact
Moll et al., Stony Brook, United States. In Nature, Aug 2015
The HSP90/HDAC6 chaperone machinery, which is significantly upregulated in cancer compared with normal tissues, is a major determinant of mutp53 stabilization.
Acetylation site specificities of lysine deacetylase inhibitors in human cells.
New
Impact
Choudhary et al., Copenhagen, Denmark. In Nat Biotechnol, Apr 2015
Furthermore, we confirmed that the effects of tubacin and bufexamac on cytoplasmic proteins result from inhibition of HDAC6.
Lineage specificity of primary cilia in the mouse embryo.
New
Impact
Anderson et al., New York City, United States. In Nat Cell Biol, Feb 2015
Basal bodies in XEN cells are mature and can form cilia when the AURKA-HDAC6 cilium disassembly pathway is inhibited.
[Histone deacetylase 6: structure, functions and development of selective inhibitors].
Review
Fang et al., In Yao Xue Xue Bao, 2015
Histone deacetylase 6 (HDAC6) is an unique subtype of histone deacetylases with two tandem deacetylase domains and substrate specificity for non-histone proteins.
Current topics of functional links between primary cilia and cell cycle.
Review
Inagaki et al., Nagoya, Japan. In Cilia, 2014
At the ciliary resorption step upon cell cycle re-entry, cilia are found to be disassembled not only by Aurora A-HDAC6 pathway but also by Nek2-Kif24 and Plk1-Kif2A pathways through their microtubule-depolymerizing activity.
Influenza A virus uses the aggresome processing machinery for host cell entry.
Impact
Yamauchi et al., Zürich, Switzerland. In Science, 2014
The capsids mimicked misfolded protein aggregates by carrying unanchored ubiquitin chains that activated a histone deacetylase 6 (HDAC6)-dependent pathway.
Overexpression of histone deacetylase 6 contributes to accelerated migration and invasion activity of hepatocellular carcinoma cells.
GeneRIF
Maesawa et al., Morioka, Japan. In Oncol Rep, 2012
Overexpression of the HDAC6 protein is involved in the migration and invasion activities of hepatocellular carcinoma cells.
Modulation of histone deacetylase 6 (HDAC6) nuclear import and tubulin deacetylase activity through acetylation.
GeneRIF
Qiu et al., Gainesville, United States. In J Biol Chem, 2012
Thus, we conclude that acetylation is an important post-translational modification that regulates HDAC6 tubulin deacetylase activity and nuclear import.
Charcot-Marie-Tooth disease: emerging mechanisms and therapies.
Review
GeneRIF
Van Den Bosch et al., Leuven, Belgium. In Int J Biochem Cell Biol, 2012
Studies suggest histone deacetylase 6 as a potential therapeutic target for inherited peripheral neuropathies.
Histone deacetylases 6 and 9 and sirtuin-1 control Foxp3+ regulatory T cell function through shared and isoform-specific mechanisms.
GeneRIF
Hancock et al., Philadelphia, United States. In Sci Signal, 2012
Data indicate that although histone deacetylases HDAC6, HDAC9, and Sirt1 all deacetylated Foxp3, each protein had different effects on transcription factors that control expression of the gene encoding Foxp3.
Roles of GRK2 in cell signaling beyond GPCR desensitization: GRK2-HDAC6 interaction modulates cell spreading and motility.
GeneRIF
Mayor et al., Madrid, Spain. In Sci Signal, 2011
GRK2-HDAC6 functional interaction may have important implications in pathological contexts related to epithelial cell migration
HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1-induced Charcot-Marie-Tooth disease.
Impact
GeneRIF
Van Den Bosch et al., Leuven, Belgium. In Nat Med, 2011
HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1-induced Charcot-Marie-Tooth disease.
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