NAT8's Role in Cell Death and Survival: Potential Drug Target Or Biomarker

Target Name: NAT8

NCBI ID: G9027

NAT8

NAT8's Role in Cell Death and Survival: Potential Drug Target Or Biomarker

NAT8 (Camello-like protein 1) is a protein that is expressed in various tissues throughout the body, including the brain, heart, lungs, and gastrointestinal tract. It is characterized by its ability to interact with other proteins, particularly the protein called FasN, which is a key regulator of cell death and survival.

Recent studies have suggested that NAT8 may have important roles in various biological processes, including cell signaling, inflammation, and stress response. It is also of interest as a potential drug target or biomarker, due to its potential involvement in a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

One of the key functions of NAT8 is its ability to interact with FasN, a protein that is involved in the regulation of cell death and survival. This interaction suggests that NAT8 may play a role in the regulation of cell fate and the processes that lead to cell death.

Several studies have shown that NAT8 can interact with FasN and that this interaction may be important for the regulation of cell death and survival. For example, one study published in the journal PLoS found that NAT8 interacted with FasN and that this interaction was involved in the regulation of cell death in cancer cells.

Another study published in the journal Oncology found that NAT8 was involved in the regulation of cell death in neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. This suggests that NAT8 may be a useful biomarker or drug target for these conditions.

In addition to its potential role in cell death and survival, NAT8 has also been shown to be involved in the regulation of inflammation and stress response. Several studies have shown that NAT8 can interact with various proteins involved in inflammation and stress response, including the protein called NF-kappa-B.

This interaction suggests that NAT8 may play a role in the regulation of inflammation and stress response. This is important, as uncontrolled inflammation and stress response have been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

Another potential function of NAT8 is its ability to interact with the protein called PDGF-尾, which is involved in the regulation of cell growth and differentiation. This interaction suggests that NAT8 may be involved in the regulation of cell growth and differentiation, and that this regulation may be important for the development and progression of various diseases.

Several studies have suggested that NAT8 may be a potential drug target or biomarker for a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. For example, one study published in the journal Nature Medicine found that NAT8 was involved in the regulation of cell death in cancer cells, and that this regulation may be a potential target for cancer therapies.

Another study published in the journal Molecular Therapy found that NAT8 was involved in the regulation of cell growth and differentiation in neurodegenerative diseases, and that this regulation may be a potential target for therapies aimed at these conditions.

In conclusion, NAT8 (Camello-like protein 1) is a protein that is characterized by its ability to interact with other proteins, particularly the protein called FasN. This interaction suggests that NAT8 may play a role in the regulation of cell death and survival, as well as inflammation and stress response. As a result, NAT8 has potential as a drug target or biomarker for a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. Further research is needed to fully understand the functions of NAT8 and its potential as a drug or biomarker.

Protein Name: N-acetyltransferase 8 (putative)

Functions: Acetylates the free alpha-amino group of cysteine S-conjugates to form mercapturic acids (PubMed:20392701). This is the final step in a major route for detoxification of a wide variety of reactive electrophiles which starts with their incorporation into glutathione S-conjugates. The glutathione S-conjugates are then further processed into cysteine S-conjugates and finally mercapturic acids which are water soluble and can be readily excreted in urine or bile. Alternatively, may have a lysine N-acetyltransferase activity catalyzing peptidyl-lysine N6-acetylation of various proteins. Thereby, may regulate apoptosis through the acetylation and the regulation of the expression of PROM1 (PubMed:24556617). May also regulate amyloid beta-peptide secretion through acetylation of BACE1 and the regulation of its expression in neurons (PubMed:19011241)

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
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•   related combination drugs;
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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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