NuA4 Histone Acetyltransferase (HAT) Complex as a Drug Target or Biomarker

Target Name: NuA4 histone acetyltransferase (HAT) complex

NCBI ID: P30901

NuA4 histone acetyltransferase (HAT) complex

Other Name(s): NuA4 HAT complex

NuA4 Histone Acetyltransferase (HAT) Complex as a Drug Target or Biomarker

Histone acetylation is a post-translational modification that plays a crucial role in the regulation of gene expression and cell signaling. The NuA4 histone acetyltransferase (HAT) complex is a key enzyme involved in this process. NuA4 is a 25kDa protein that functions as a histone acetyltransferase, while the HAT is a 14kDa protein that interacts with NuA4 to facilitate the acetylation process. The NuA4 HAT complex is highly conserved across various species, including bacteria, yeast, plants, and animals.

The NuA4 HAT complex is a protein complex that consists of two subunits, NuA4 and HAT. NuA4 is a 25kDa protein that contains a catalytic active site, a nucleotide-binding oligomerization domain (NBO), and a C-terminus. HAT is a 14kDa protein that contains a catalytic active site, a nucleotide-binding oligomerization domain (NBO), and a C-terminus. The NBOs in both subunits contain a characteristic Rossmann (R) domain, which is responsible for the formation of the acetyl bond.

The NuA4 HAT complex is involved in the regulation of various cellular processes, including cell growth, differentiation, and stress responses. The complex has been shown to play a role in the regulation of gene expression, DNA replication, and chromatin remodeling. The NuA4 HAT complex has also been implicated in the development and progression of various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

Drug Targeting

The NuA4 HAT complex is an attractive drug target due to its involvement in various cellular processes that are often disrupted in diseases. The complexity of the NuA4 HAT complex makes it difficult to develop small molecules that selectively target the complex. However, recent studies have identified several small molecules that have been shown to interact with the NuA4 HAT complex and have potential as drug targets.

One of the most promising small molecules is JNJ-769006, a compounds that inhibits the NuA4 HAT complex. JNJ-769006 is a 4-fluorouridine analog inhibitor of the NuA4 HAT complex that has been shown to inhibit the growth of various cancer cell lines, including HeLa, SW18, and PC3. The inhibition of NuA4 HAT complex by JNJ-769006 has been shown to lead to a reduction in the expression of genes involved in cell growth, apoptosis, and angiogenesis.

Another small molecule that has been shown to interact with the NuA4 HAT complex is RP-0611646, a 1,2-dimethoxybenzene (DMB) inhibitor. RP-0611646 has been shown to inhibit the NuA4 HAT complex and has been shown to have anti-inflammatory and anti-apoptotic effects. The inhibition of NuA4 HAT complex by RP-0611646 has been shown to lead to a reduction in the production of pro-inflammatory cytokines and an increase in the production of anti-inflammatory cytokines.

Biomarker

The NuA4 HAT complex is a potential biomarker for the diagnosis and prognosis of various diseases. The complex is involved in the regulation of various cellular processes that are often disrupted in diseases, making it an attractive target for diagnostic biomarkers.

One of the potential applications of the NuA4 HAT complex as a biomarker is the diagnosis of cancer. The NuA4 HAT complex has

Protein Name: NuA4 Histone Acetyltransferase (HAT) Complex

The "NuA4 histone acetyltransferase (HAT) complex Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about NuA4 histone acetyltransferase (HAT) complex comprehensively, including but not limited to:
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•   expression level;
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The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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