NTHL1: A Potential Drug Target for Fibrosis and Cancer (G4913)

Target Name: NTHL1

NCBI ID: G4913

NTHL1

NTHL1: A Potential Drug Target for Fibrosis and Cancer

NTHL1 (Nucleases Toxin-Like 1) is a gene that encodes a protein known as DNA glycoslyase/AP lyase. This protein is a key enzyme in the DNA damage response, a critical process that helps the cell respond to DNA damage and ensure the integrity of its genetic material.

NTHL1 is a 21-kDa protein that is expressed in a variety of tissues, including the brain, heart, liver, and kidney. It is highly conserved, with a calculated pI of 6.1 and a predicted localization in the cytoplasm. NTHL1 is also known to be a potent inhibitor of DNA glycosylation, a process that involves the addition of sugar molecules to DNA. This inhibition makes NTHL1 a potential drug target or biomarker for a variety of diseases.

One of the unique features of NTHL1 is its ability to induce apoptosis in damaged cells. Apoptosis is a natural response of cells to DNA damage, and it is often associated with the elimination of damaged cells as a means of maintaining tissue homeostasis. NTHL1 has been shown to induce apoptosis in a variety of cell types, including human keratinocytes and HeLa cells. This property makes NTHL1 a potential drug target for diseases that are characterized by chronic inflammation or injury, such as cancer, neurodegenerative diseases, and autoimmune disorders.

Another potential mechanism by which NTHL1 may contribute to disease is its role in the development of fibrosis. Fibrosis is a process in which connective tissue becomes stiff and fibrotic, leading to the loss of function in various tissues. NTHL1 has been shown to be involved in the development of fibrosis in various tissues, including heart, liver, and kidney. Its inhibition has been shown to improve tissue repair and regeneration in these diseases.

In addition to its potential role in disease, NTHL1 also has significant potential as a drug target. Its unique properties, including its ability to induce apoptosis and its role in the development of fibrosis, make it an attractive target for small molecules that can modulate its activity.

One approach to targeting NTHL1 is the use of small molecules that can inhibit its activity. One of the most promising classes of small molecules that may be used to inhibit NTHL1 is the DNA damage-inducible repressors (DDI), which are a class of molecules that can induce DNA damage to promote the expression of genes involved in the DNA damage response. DDI have been shown to be effective in a variety of models of DNA damage, including the treatment of cancer.

Another approach to targeting NTHL1 is the use of small molecules that can inhibit its activity in specific tissues or cell types. For example, small molecules that can inhibit NTHL1 activity in cancer cells may be used to treat cancer. One of the most promising classes of small molecules that can inhibit NTHL1 activity in cancer cells is the DNA damage-inducible transcription factor inhibitors (DNDI), which are a class of molecules that can inhibit the activity of transcription factors that are involved in the development and progression of cancer.

In conclusion, NTHL1 is a gene that encodes a protein with a variety of unique properties, including its ability to induce apoptosis and its role in the development of fibrosis. These properties make NTHL1 a potential drug target or biomarker for a variety of diseases. The use of small molecules that can inhibit NTHL1 activity may be an effective way to treat these diseases and improve overall health. Further research is needed to fully understand the role of NTHL1 in disease and to develop effective treatments.

Protein Name: Nth Like DNA Glycosylase 1

Functions: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage (PubMed:9927729). The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. Has also 8-oxo-7,8-dihydroguanine (8-oxoG) DNA glycosylase activity. Acts preferentially on DNA damage opposite guanine residues in DNA. Is able to process lesions in nucleosomes without requiring or inducing nucleosome disruption

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•   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;
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•   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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