RPL39L: A Ribosomal Protein L39-like Molecule as a Potential Drug Target and Biomarker

Target Name: RPL39L

NCBI ID: G116832

RPL39L

RPL39L: A Ribosomal Protein L39-like Molecule as a Potential Drug Target and Biomarker

Ribosomal protein L39 (RPL39) is a protein that plays a crucial role in the process of translation of mRNAs into proteins. It is a large protein with a molecular weight of approximately 50 kDa and is found in most eukaryotic cells. RPL39 is composed of two structural domains: a 255 amino acid protein tail and a 61 amino acid protein N-terminus. The N-terminus of RPL39 contains a unique acetyl group, which is known to play a critical role in its stability and functions.

Despite its importance in cell signaling, RPL39 has not been extensively studied as a drug target or biomarker. The lack of research is mainly due to the small size of RPL39, which makes it difficult to manipulate and study in the lab. However, recent studies have identified potential targets for RPL39, providing new insights into its biology and suggesting that it may have a future as a drug or biomarker.

Targeting RPL39

Several studies have identified potential targets for RPL39. One of the most promising targets is the acetyl group on the N-terminus. The acetyl group is known to be a druggable site due to its stability and its ability to undergo conformational changes. Several studies have shown that inhibiting the activity of RPL39 by either blocking the acetyl group or removing it can lead to a decrease in the protein's stability and a reduction in cell signaling.

Another potential target for RPL39 is the N-terminus of the protein. The N-terminus of RPL39 contains a unique acetyl group that is known to play a critical role in its stability and functions. Several studies have shown that removing the N-terminus of RPL39 can lead to a decrease in the protein's stability and a reduction in cell signaling.

In addition to these potential targets, RPL39 has also been suggested as a potential biomarker for several diseases, including cancer. This is because RPL39 is highly expressed in many types of cancer cells and has been shown to be involved in cell signaling.

Conclusion

In conclusion, RPL39 is a protein that has not been extensively studied as a drug target or biomarker. However, recent studies have identified potential targets for RPL39, including the acetyl group on the N-terminus and the N-terminus itself. These studies suggest that RPL39 may have a future as a drug or biomarker, and further research is needed to fully understand its biology and its potential as a therapeutic target.

Protein Name: Ribosomal Protein L39 Like

Functions: Male germ cell-specific component of the ribosome, which is required for the formation of sperm and male fertility. Replaces the RPL39 paralog in the ribosome of male germ cells. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The male germ cell-specific ribosome displays a ribosomal polypeptide exit tunnel of distinct size and charge states compared with the classical ribosome. It is responsible for regulating the biosynthesis and folding of a subset of male germ-cell-specific proteins that are essential for the formation of sperm

The "RPL39L 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 RPL39L 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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