Target Name: RPS27
NCBI ID: G6232
Review Report on RPS27 Target / Biomarker Content of Review Report on RPS27 Target / Biomarker
RPS27
Other Name(s): 40S ribosomal protein S27 | MPS1 | metallopanstimulin 1 | Metallopanstimulin 1 | DBA17 | MPS-1 | S27 | Small ribosomal subunit protein eS27 | 40S ribosomal protein S27 (isoform 1) | RPS27 variant 1 | metallopan-stimulin 1 | Ribosomal protein S27 | small ribosomal subunit protein eS27 | Metallopan-stimulin 1 | Ribosomal protein S27, transcript variant 1 | RS27_HUMAN | ribosomal protein S27

Understanding The Role of Ribosomal Protein S27 in Cellular Processes

Ribosomal protein S27 (RPS27) is a protein that is expressed in all eukaryotic cells and plays a critical role in protein synthesis. It is a 40S subunit of the large ribosome and is composed of two structural domains: a catalytic domain and a regulatory domain. The catalytic domain is responsible for the chemical reaction that leads to protein synthesis, while the regulatory domain is involved in regulating the activity of the enzyme.

RPS27 has been identified as a potential drug target and has been shown to have a variety of therapeutic effects. One of the main reasons for its potential as a drug is its involvement in the regulation of cell growth and division. RPS27 has been shown to play a role in the regulation of cell cycle progression, and it has been shown to inhibit the growth of cancer cells.

Another potential drug target for RPS27 is its role in the regulation of cell signaling pathways. RPS27 has been shown to play a role in the regulation of several signaling pathways, including the TGF-β pathway and the PI3K/Akt pathway. These pathways are involved in the regulation of cell growth, survival, and angiogenesis, and RPS27 has been shown to play a negative role in their regulation.

In addition to its role in cell signaling pathways, RPS27 has also been shown to be involved in the regulation of protein synthesis itself. It has been shown to play a negative role in the regulation of protein synthesis, which can lead to the accumulation of mutated or misfolded proteins in the cell. This accumulation of mutated or misfolded proteins can lead to a variety of cellular problems, including the development of cancer.

The catalytic domain of RPS27 is responsible for the chemical reaction that leads to protein synthesis. This domain is composed of a single protein alpha-helix and a single beta-sheet. The alpha-helix is 鈥嬧?媡he primary structural feature of the catalytic domain, and it is responsible for the stability and active site of the enzyme. The beta-sheet is the secondary structural feature of the domain and is responsible for the stability of the overall structure of the enzyme.

The regulatory domain of RPS27 is involved in regulating the activity of the enzyme. This domain is composed of a series of short RNA molecules, known as small nucleotide regulatory proteins (SNRs). These SNRs are involved in the recognition and binding of specific DNA sequences , and they are responsible for regulating the opening and closing of the RNA molecule.

One of the main functions of the regulatory domain is to regulate the translation of the mRNA into the protein. This is done by the SNRs interacting with specific regions of the mRNA and by the regulation of the activity of the ribosome. SNRs have been shown to play a negative role in the regulation of protein synthesis, and it is thought that this may be one of the reasons for the negative impact that RPS27 has on protein synthesis.

Another function of the regulatory domain is to regulate the stability of the RNA molecule. This is done by the SNRs interacting with specific regions of the RNA molecule and by the regulation of the activity of the RNA polymerase. SNRs have been shown to play a negative role in the regulation of protein synthesis, and it is thought that this may be another reason for the negative impact that RPS27 has on protein synthesis.

In conclusion, RPS27 is a protein that is involved in the regulation of protein synthesis and has been shown to have a variety of therapeutic effects. Its potential as a drug target is due to its involvement in the regulation of cell growth and division, cell signaling pathways, and protein synthesis. The catalytic domain of RPS27 is responsible for the chemical reaction that leads to protein synthesis, while the regulatory domain is involved in regulating the activity of the enzyme. Further research is needed to fully understand the role of RPS27 in

Protein Name: Ribosomal Protein S27

Functions: Component of the small ribosomal subunit (PubMed:8706699, PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Required for proper rRNA processing and maturation of 18S rRNAs (PubMed:25424902). 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 "RPS27 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 RPS27 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

RPS27A | RPS27AP11 | RPS27AP12 | RPS27AP16 | RPS27AP17 | RPS27AP20 | RPS27AP5 | RPS27AP7 | RPS27L | RPS27P21 | RPS27P22 | RPS27P23 | RPS27P29 | RPS27P7 | RPS27P8 | RPS27P9 | RPS28 | RPS28P3 | RPS28P7 | RPS29 | RPS29P16 | RPS29P22 | RPS29P23 | RPS29P8 | RPS29P9 | RPS2P1 | RPS2P11 | RPS2P12 | RPS2P17 | RPS2P2 | RPS2P20 | RPS2P21 | RPS2P28 | RPS2P32 | RPS2P40 | RPS2P44 | RPS2P46 | RPS2P50 | RPS2P51 | RPS2P55 | RPS3 | RPS3A | RPS3AP10 | RPS3AP15 | RPS3AP18 | RPS3AP20 | RPS3AP24 | RPS3AP25 | RPS3AP26 | RPS3AP34 | RPS3AP36 | RPS3AP44 | RPS3AP46 | RPS3AP47 | RPS3AP5 | RPS3P2 | RPS3P5 | RPS3P6 | RPS3P7 | RPS4X | RPS4XP11 | RPS4XP13 | RPS4XP18 | RPS4XP21 | RPS4XP3 | RPS4XP5 | RPS4XP6 | RPS4XP9 | RPS4Y1 | RPS4Y2 | RPS5 | RPS5P6 | RPS6 | RPS6KA1 | RPS6KA2 | RPS6KA3 | RPS6KA4 | RPS6KA5 | RPS6KA6 | RPS6KB1 | RPS6KB2 | RPS6KC1 | RPS6KL1 | RPS6P1 | RPS6P13 | RPS6P15 | RPS6P17 | RPS6P25 | RPS6P26 | RPS6P6 | RPS7 | RPS7P1 | RPS7P10 | RPS7P11 | RPS7P2 | RPS7P3 | RPS7P4 | RPS7P5 | RPS7P8 | RPS8