RPS23: A Potential Drug Target Or Biomarker for Various Diseases

Target Name: RPS23

NCBI ID: G6228

RPS23

RPS23: A Potential Drug Target Or Biomarker for Various Diseases

Ribosomal subunit protein uS12 (RPS23) is a protein that plays a critical role in the regulation of gene expression in eukaryotic cells. It is a small protein that contains only 12 amino acids and is localized to the endoplasmic reticulum (ER) in eukaryotic cells. Despite its small size, RPS23 is highly conserved across different species and has been shown to play a role in various cellular processes, including DNA replication, gene expression, and cell signaling.

One of the unique features of RPS23 is its ability to interact with other proteins, including histone modifications and non-histone modifications. This interaction with other proteins makes RPS23 a potential drug target or biomarker for various diseases.

During DNA replication, RPS23 is involved in the initiation of DNA replication by binding to the complex protein TFII4, which is required for the initiation of DNA replication. This interaction between RPS23 and TFII4 suggests that RPS23 may be a drug target or biomarker for diseases that are characterized by abnormal DNA replication, such as cancer.

In addition to its role in DNA replication, RPS23 is also involved in the regulation of gene expression. It has been shown to interact with various transcription factors, including activator protein 1 (AP-1), which is a key transcription factor that regulates cell proliferation and survival. This interaction between RPS23 and AP-1 suggests that RPS23 may be a drug target or biomarker for diseases that are characterized by abnormal gene expression, such as cancer.

Another potential function of RPS23 is its role in cell signaling. It has been shown to interact with various protein kinases, including mitogen-activated kinase (MAK) 1 and MAK 2, which are involved in cell signaling. This interaction between RPS23 and MAKs suggests that RPS23 may be a drug target or biomarker for diseases that are characterized by abnormal cell signaling, such as neurodegenerative diseases.

RPS23 is also involved in the regulation of cell adhesion. It has been shown to interact with the protein cadherin, which is involved in cell adhesion. This interaction between RPS23 and cadherin suggests that RPS23 may be a drug target or biomarker for diseases that are characterized by abnormal cell adhesion, such as cancer.

In addition to its role in cell signaling, RPS23 is also involved in the regulation of cell cycle progression. It has been shown to interact with the protein p21, which is involved in the regulation of cell cycle progression. This interaction between RPS23 and p21 suggests that RPS23 may be a drug target or biomarker for diseases that are characterized by abnormal cell cycle progression, such as cancer.

Despite its small size, RPS23 has been shown to play a critical role in various cellular processes that are important for human health and disease. Its interaction with other proteins makes it a potential drug target or biomarker for various diseases, including cancer, neurodegenerative diseases, and diseases characterized by abnormal cell signaling. Therefore, further research is needed to fully understand the role of RPS23 in disease progression and the potential of RPS23 as a drug target or biomarker.

Protein Name: Ribosomal Protein S23

Functions: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:28257692, PubMed:23636399, PubMed:25957688, PubMed:25901680). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (PubMed:23636399, PubMed:25957688, PubMed:25901680). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (PubMed:23636399, PubMed:25957688, PubMed:25901680). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:23636399, PubMed:25957688, PubMed:25901680). Plays an important role in translational accuracy (PubMed:28257692). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)

The "RPS23 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 RPS23 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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