Histone deacetylases (HDACs): characterization of the classical HDAC family.

By Annemieke J M de Ruijter, A. V. van Gennip, H. Caron, S. Kemp, A. V. van Kuilenburg. Biochemical Journal, 2003

3,135 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/955397d2bc26685238ca22e1b7ae72e42fbc01f7

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

Citations in the corpus

SIRT1 controls endothelial angiogenic functions during vascular growth. (2007, background): “HDACs are divided into three classes based on their homology with yeast proteins Rpd3 (class I), Hda1 (class II), and Sir2 (class III) (de Ruijter et al. 2003; North and Verdin 2004).”
Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. (2005, background): “Histone deacetylases are divided into three categories based on their homology to yeast proteins Rpd3p (class I), Hda1p (class II), and Sir2p (class III) ( de Ruijter et al., 2003; North and Verdin, 2004).”
Metabolic reprogramming and epigenetic modifications on the path to cancer (2021, background): “Zinc-dependent histone deacetylases (zinc-dependent HDACs) and NAD+-dependent sirtuins are two major families of lysine deacetylases (De Ruijter et al., 2003; Jing and Lin, 2015).”
Targeting epigenetic regulators for cancer therapy: mechanisms and advances in clinical trials (2019, background): “The class IV protein shares sequence similarity with both class I and class II proteins.(207,208) Classes I, II, and IV are included in the histone deacetylase family, whereas class III HDACs belong to the Sir2 regulator family.”
Suppressive effect of short-chain fatty acids on production of proinflammatory mediators by neutrophils. (2011, background): “A common view has emerged that histone acetylation, which reduces the affinity between histone proteins and DNA, facilitating the binding of transcription factors to DNA, enhances transcription, whereas histone deacetylation is associated with transcription repression [35].”
Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. (2004, background): “This restriction suggests that it does not play an important role in conserved processes, though it may have developmental or tissue-specific functions consistent with its apparently tissue-specific expression.(22) The deep divergence of the HDAC8 branch might be taken to suggest that HDAC8 is an an”
Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes (2009, background): “…into four classes: class I (HDAC1, 2, 3, and 8 with a homology to Rpd3), class II (HDAC4, 5, 6, 7, 9, and 10 with a homology to Hda1), class III (Sirt1, 2, 3, 4, 5, 6, and 7 with a homology to Sir2), and class IV (HDAC11) (de Ruijter et al., 2003; Yang and Gregoire, 2005; Yang and Seto, 2008).”
The world of protein acetylation. (2016, background): “Class IV has only one known representative, HDAC11, which differs phylogenetically from the Zn-dependent yeast proteins Rpd3 (class I) and HDA1 (class II), aswell as from theNAD-dependent Sir2 homolog, and therefore forms its own subclass [208].”
The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men (2008, background): “, which led to the designation of the zinc-dependent Rpd3/Hda1 family as the 'classical family”
HDAC family: What are the cancer relevant targets? (2009, background): “HDACs are grouped into class I, class II, class III and class IV based on their sequence homology to their yeast orthologues Rpd3, HdaI and Sir2, respectively [5,6].”