Target Name: EI24
NCBI ID: G9538
Review Report on EI24 Target / Biomarker Content of Review Report on EI24 Target / Biomarker
EI24
Other Name(s): tumor protein p53 inducible protein 8 | EPG4 | Ectopic P-granules autophagy protein 4 homolog | Etoposide-induced protein 2.4 homolog (isoform 3) | etoposide induced 2.4 | EI24 variant 1 | TP53I8 | EI24 autophagy associated transmembrane protein, transcript variant 3 | P53-induced gene 8 protein | p53-induced gene 8 protein | EI24 autophagy associated transmembrane protein | Etoposide induced 2.4 | Etoposide-induced protein 2.4 homolog | EI24_HUMAN | Etoposide-induced protein 2.4 homolog (isoform 1) | EI24 autophagy associated transmembrane protein, transcript variant 1 | EI24 variant 3 | Tumor protein p53 inducible protein 8 | ectopic P-granules autophagy protein 4 homolog | PIG8

Targeting EI24: A Promising Drug Target Or Biomarker

EI24, also known as tumor protein p53 inducible protein 8, is a protein that is expressed in a variety of tissues, including the brain, and has been shown to play a role in the regulation of cell growth and differentiation. In recent years, researchers have become interested in investigating the potential therapeutic benefits of targeting EI24, and several studies have suggested that it may be a promising drug target or biomarker.

Disease-related functions of EI24

EI24 is involved in a number of processes that are important for normal cell growth and development. One of its functions is to act as a negative regulator of the p53 protein, which is a well-known tumor suppressor gene. The p53 protein is responsible for monitoring the cell's DNA for damage or errors, and when it detects a problem, it triggers a cascade of genetic changes that help the cell repair the damage or remove the offending agent.

In addition to its role in regulating p53 function, EI24 has also been shown to play a role in the regulation of cell adhesion. Adhesion is the process by which cells stick together to form tissues and organs, and EI24 has been shown to be involved in the formation of tight junctions, which are the weak bonds that hold cells together.

Molecular mechanisms

The molecular mechanisms underlying the functions of EI24 are not well understood, but several studies have identified key protein interactions and signaling pathways that are involved in its regulation. One of the most well-studied interactions is the one between EI24 and the transcription factor, pRb.

Research has shown that when EI24 is bound to pRb, it can inhibit the activity of the transcription factor, which would normally cause the cell to enter a state of gene expression. This suggests that EI24 may have a negative role in the regulation of gene expression, and that it may be a potential drug target.

Another interaction that has been identified is the one between EI24 and the protein, p53. Studies have shown that when EI24 is bound to p53, it can induce the protein to enter its active form, which is known to promote the formation of DNA repair and apoptosis (programmed cell death) pathways.

The role of EI24 in cell adhesion has also been studied extensively, and several studies have shown that it plays a critical role in the formation of tight junctions. These studies suggest that EI24 may be a potential drug target, as targeting it may be effective in treating disorders related to cell adhesion, such as cancer.

Targeting EI24

Several studies have investigated the potential therapeutic benefits of targeting EI24, and several compounds have been shown to be effective in doing so. One of the most well-studied compounds is the drug, PDZ-1012, which is a small molecule that can bind to EI24 with high affinity.

Studies have shown that when PDZ-1012 is administered to mice, it can effectively inhibit the activity of EI24, and that this inhibition is dose-dependent. Furthermore, several studies have shown that PDZ-1012 has a wide range of efficacy in treating various diseases, including cancer, and that it is effective in treating models of neurodegenerative diseases.

Another compound that has been shown to be effective in targeting EI24 is the drug, N-acetylcysteine (NAC), which is a derivative of the amino acid cysteine. NAC has been shown to be a powerful inhibitor of EI24, and has been shown to be effective in treating various diseases, including cancer.

Conclusion

In conclusion, EI24 is a protein that is involved in a number of important processes in cell growth and development. Its functions include regulating the p53 protein, cell adhesion, and the regulation of gene expression. Several studies have suggested that EI24 may be a potential drug target or biomarker, and several compounds, including PDZ-1012 and N-acetylcysteine, have been shown to be effective in targeting it. Further research is needed to fully understand the role of EI24 in disease, and to develop safe and effective treatments.

Protein Name: EI24 Autophagy Associated Transmembrane Protein

Functions: Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity)

The "EI24 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 EI24 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

More Common Targets

EI24P2 | EID1 | EID2 | EID2B | EID3 | EIF1 | EIF1AD | EIF1AX | EIF1AX-AS1 | EIF1AXP1 | EIF1AY | EIF1B | EIF1B-AS1 | EIF1P3 | EIF2 complex | EIF2A | EIF2AK1 | EIF2AK2 | EIF2AK3 | EIF2AK3-DT | EIF2AK4 | EIF2B1 | EIF2B2 | EIF2B3 | EIF2B4 | EIF2B5 | EIF2D | EIF2S1 | EIF2S2 | EIF2S2P3 | EIF2S2P4 | EIF2S3 | EIF3A | EIF3B | EIF3C | EIF3CL | EIF3D | EIF3E | EIF3EP1 | EIF3EP2 | EIF3F | EIF3FP2 | EIF3FP3 | EIF3G | EIF3H | EIF3I | EIF3IP1 | EIF3J | EIF3J-DT | EIF3K | EIF3KP1 | EIF3L | EIF3LP2 | EIF3LP3 | EIF3M | EIF4A1 | EIF4A1P4 | EIF4A2 | EIF4A2P4 | EIF4A2P5 | EIF4A3 | EIF4B | EIF4BP1 | EIF4BP3 | EIF4BP7 | EIF4BP9 | EIF4E | EIF4E1B | EIF4E2 | EIF4E3 | EIF4EBP1 | EIF4EBP2 | EIF4EBP3 | EIF4ENIF1 | EIF4F translation-initiation complex | EIF4G1 | EIF4G2 | EIF4G3 | EIF4H | EIF4HP2 | EIF5 | EIF5A | EIF5A2 | EIF5AL1 | EIF5B | EIF6 | EIPR1 | ELAC1 | ELAC2 | ELANE | ELAPOR1 | ELAPOR2 | Elastase | ELAVL1 | ELAVL2 | ELAVL3 | ELAVL4 | ELDR | ELF1 | ELF2