Discovery and Function of DNA Damage Inducible 2 (DDI2) (G84301)

Target Name: DDI2

NCBI ID: G84301

DDI2

Discovery and Function of DNA Damage Inducible 2 (DDI2)

DNA damage inducible 2 (DDI2) is a non-coding RNA molecule that has been identified as a potential drug target or biomarker. DDI2 is a key regulator of cellular processes that are essential for cell survival, and its dysfunction has been implicated in a number of diseases, including cancer.

The discovery of DDI2

DDI2 was first identified in the 1990s by researchers who were studying the regulation of gene expression in cancer cells. They found that DDI2 was a highly expressed gene in cancer cells, and that it was involved in the regulation of cellular processes that were critical for cancer cell survival.

Since then, researchers have continued to study DDI2 and its functions. They have found that DDI2 is involved in a number of cellular processes, including cell division, apoptosis (programmed cell death), and inflammation. They have also found that DDI2 is involved in the regulation of cellular signaling pathways that are critical for cancer cell growth and survival.

DDI2 as a drug target

DDI2 has emerged as a promising drug target because it is involved in a number of processes that are critical for cancer cell survival. Researchers have found that DDI2 is involved in the regulation of cell division, which is a critical process for cancer cell growth and survival. They have also found that DDI2 is involved in the regulation of apoptosis, which is the process by which cells die naturally.

DDI2 has been shown to play a key role in the regulation of apoptosis, and it is thought to do so by regulating the expression of genes that are involved in cell death. Researchers have found that DDI2 can inhibit the expression of genes that are involved in cell death, and that this inhibition can protect cancer cells from apoptosis.

In addition to its role in apoptosis, DDI2 is also thought to play a key role in the regulation of cell division. Researchers have found that DDI2 is involved in the regulation of the G1/S transition, which is the stage of cell division where cells prepare for cell division. They have also found that DDI2 can inhibit the G1/S transition, and that this inhibition can delay cell division.

DDI2 as a biomarker

DDI2 has also been identified as a potential biomarker for a number of diseases, including cancer. Researchers have found that DDI2 is often expressed in cancer cells, and that its expression can be used as a diagnostic marker for cancer. They have also found that DDI2 is involved in the regulation of cellular processes that are critical for cancer cell growth and survival, and that this involvement may make it an attractive target for cancer therapies.

In addition to its potential as a drug or biomarker, DDI2 is also of interest as a potential therapeutic target. Researchers have found that DDI2 can interact with a number of different proteins, including the protein p53. They have also found that DDI2 can modulate the activity of the protein p53, which is involved in the regulation of cell growth and apoptosis.

Conclusion

DDI2 is a non-coding RNA molecule that has been identified as a potential drug target or biomarker. DDI2 is involved in a number of cellular processes that are critical for cell survival, and its dysfunction has been implicated in a number of diseases, including cancer. Further research is needed to fully understand the functions of DDI2 and its potential as a drug or biomarker.

Protein Name: DNA Damage Inducible 1 Homolog 2

Functions: Aspartic protease that mediates the cleavage of NFE2L1/NRF1 at 'Leu-104', thereby promoting release of NFE2L1/NRF1 from the endoplasmic reticulum membrane (PubMed:27676298, PubMed:27528193). Ubiquitination of NFE2L1/NRF1 is a prerequisite for cleavage, suggesting that DDI2 specifically recognizes and binds ubiquitinated NFE2L1/NRF1 (PubMed:27528193). Seems to act as a proteasomal shuttle which links the proteasome and replication fork proteins like RTF2 (Probable). Required, with DDI1, for cellular survival following replication stress. Together or redudantly with DDI1, removes RTF2 from stalled forks to allow cell cycle progression after replication stress and maintains genome integrity (PubMed:29290612)

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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;
•   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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