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The X-ray crystal structure of HDAC8 complexed with inhibitor confirms the formation of a unique subpocket in HDAC8.
These data provide support for the hypothesis that HDAC8 may undergo metal switching in vivo that, in turn, may regulate its activity. However, future studies are needed to explore the identity of the metal ion bound to HDAC8 in cells under varied conditions
The study reports the crystal structure of the HDAC8-trapoxin A complex at 1.24 A resolution, revealing that the ketone moiety of l-Aoe undergoes nucleophilic attack to form a zinc-bound tetrahedral gem (show GEM Proteins)-diolate that mimics the tetrahedral intermediate and its flanking transition states in catalysis.
The findings suggest that miR (show MLXIP Proteins)-455-3p plays a critical role during chondrogenesis by directly targeting HDAC2 (show HDAC2 Proteins)/8 and promoting histone H3 (show HIST3H3 Proteins) acetylation.
7-amino-4-methylcoumarin did not affect acetyllysine preference in a multiply acetylated substrate. In contrast, AMC significantly enhanced KDAC6 substrate affinity, greatly reduced Sirt1 (show SIRT1 Proteins) activity, eliminated the substrate sequence specificity of KDAC4, and had no consistent effect with KDAC8 substrates.
Enzymological, biophysical, and structural studies of Cornelia de Lange Syndrome HDAC8 protein mutants have yielded critical insight on compromised catalysis in vitro. Most CdLS (show NIPBL Proteins) HDAC8 mutations trigger structural changes that directly or indirectly impact substrate binding and catalysis.
class I HDACs (HDAC1 (show HDAC1 Proteins), 2, 3 and 8) play a major role in regulating extracellular matrix and Epithelial-mesenchymal transition, whereas class IIa HDACs (HDAC4 (show HDAC4 Proteins) and 5) are less effective.
Losses of catalytic efficiency in histone deacetylase 8 (HDAC8) are observed for G304A and G305A mutations.
Data suggest sequencing of histone deacetylase 8 protein (HDAC8) as an indispensable part of the routine molecular diagnostic for patients with Cornelia de Lange syndrome (CdLS (show NIPBL Proteins)) or CdLS (show NIPBL Proteins)-overlapping features.
HDAC8 were overexpressed in oral squamous cell carcinoma tissues, mainly localized in the cytoplasm.
Results indicate that HDAC8 functions to modulate p53 (show TP53 Proteins) activity to ensure long-term hematopoietic stem cells (LT-HSCs) maintenance and cell survival under stress.
this study demonstrates a novel role of HDAC8 in LeTx immunotoxicity and regulation of pro-IL-1beta (show IL1B Proteins) production likely through eRNAs.
findings show how HDAC8 drives nonalcoholic fatty liver disease-associated hepatocarcinogenesis
Data reveal a role for miR-21-3p in regulating HDAC8 expression and Akt/Gsk3beta pathway in cardiac hypertrophy.
histone deacetylase 8 inhibition reduces gene expression and production of proinflammatory cytokines in vitro and in vivo
HDAC8 and Sirt1 (show SIRT1 Proteins) were also demonstrated to interact directly with ERRalpha (show ESRRA Proteins) in vivo and to deacetylate and increase the DNA binding affinity of ERRalpha (show ESRRA Proteins) in vitro.
Global deletion of Hdac8 in mice leads to perinatal lethality due to skull instability, and deletion of Hdac8 in cranial neural crest cells and Hdac8 specifically represses the aberrant expression of homeobox (show PRRX1 Proteins) transcription factors such as Otx2 (show OTX2 Proteins) and Lhx1 (show LHX1 Proteins)
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 I of the histone deacetylase family. It catalyzes the deacetylation of lysine residues in the histone N-terminal tails and represses transcription in large multiprotein complexes with transcriptional co-repressors. Multiple transcript variants encoding different isoforms have been found for this gene.
histone deacetylase 8
, histone deacetylase-like 1