High-throughput Analysis and Characterization (HTSAC) Method: A Promising Strategy for Drug Discovery

Target Name: HDAC10

NCBI ID: G83933

HDAC10

High-throughput Analysis and Characterization (HTSAC) Method: A Promising Strategy for Drug Discovery

High-throughput screening (HTS) has become an essential tool in drug discovery, as it allows researchers to quickly identify potential lead compounds that can be further developed into drugs. One of the most promising strategies in drug discovery is the use of pharmacophore-based virtual screening, which involves the use of computer-aided drug design to identify potential drug candidates based on their structural features. One of the most well-known pharmacophore-based virtual screening strategies is the High-throughput Analysis and Characterization (HTSAC) method, which has been used to identify potential drug targets in a variety of organisms, including humans.

In this article, we will focus on one of the most promising HDACs, HDAC10 (HDAC10 variant 1), and its potential as a drug target. We will begin by providing an overview of HDACs and their role in drug discovery, followed by an introduction to the structure and characteristics of the HDAC10 molecule. We will then discuss the HDAC10's potential as a drug target, including its unique features and the various diseases it is associated with. Finally, we will conclude by discussing the future of HDAC10 as a drug target and its potential for the development of new treatments.

Overview of HDACs

Hydroxyureas (HUs) are a class of drugs that are commonly used in the treatment of various diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. HUs work by inhibiting the activity of a protein called P-gp, which is involved in the transport of a variety of drugs, including statins, anticancer agents, and anti-inflammatory drugs. P-gp is also involved in the detoxification of drugs, which can lead to reduced drug efficacy or increased drug toxicity.

HDACs are a subclass of HUs that are specifically designed to inhibit P-gp activity. They are derived from the amino acid Asp295 and have been shown to be effective in a variety of models of drug discovery, including in the identification of potential drug targets and in the development of new anti-cancer agents.

HDAC10 is a promising HDAC that has been shown to be effective in a variety of models of drug discovery. It is derived from the Asp295 protein and has been shown to inhibit P-gp activity in a variety of cell lines and animal models.

Structure and Characterization of HDAC10

HDAC10 is a 29 amino acid protein that is expressed in a variety of tissues and organs, including the brain, heart, liver, and pancreas. It has a molecular weight of 30 kDa and a calculated pI of 1.5. HDAC10 has a single transmembrane domain and a nuclear localization region.

The HDAC10 transmembrane domain consists of a catalytic center and a region that is involved in the interaction with P-gp. The catalytic center is composed of two conserved Asp residues, Asp25 and Asp28, which are involved in the inhibition of P-gp activity. The region involved in the interaction with P-gp includes a short amino acid sequence that is critical for the protein's stability and functions as a binding site for P-gp.

HDAC10 has been shown to be effective in a variety of models of drug discovery, including the identification of potential drug targets and the development of new anti-cancer agents. For example, HDAC10 has been shown to be effective in the inhibition of P-gp activity in a variety of cell lines, including breast cancer, ovarian cancer, and prostate cancer. It has also been shown to be effective in the inhibition of P-gp activity in animal models of cancer, including the inhibition of the growth

Protein Name: Histone Deacetylase 10

Functions: Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine (PubMed:28516954). Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine (PubMed:28516954). Histone deacetylase activity has been observed in vitro (PubMed:11861901, PubMed:11726666, PubMed:11677242, PubMed:11739383). Has also been shown to be involved in MSH2 deacetylation (PubMed:26221039). The physiological relevance of protein/histone deacetylase activity is unclear and could be very weak (PubMed:28516954). May play a role in the promotion of late stages of autophagy, possibly autophagosome-lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells (PubMed:23801752, PubMed:29968769). May play a role in homologous recombination (PubMed:21247901). May promote DNA mismatch repair (PubMed:26221039)

The "HDAC10 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 HDAC10 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
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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