Target Name: FST
NCBI ID: G10468
Review Report on FST Target / Biomarker Content of Review Report on FST Target / Biomarker
FST
Other Name(s): FST variant FST317 | FST344 | follistatin isoform FST317 | Follistatin, transcript variant FST317 | Follistatin, transcript variant FST344 | Follistatin (isoform FST344) | activin-binding protein | FST variant FST344 | Follistatin (isoform FST317) | FST_HUMAN | Follistatin | follistatin | FS | Activin-binding protein

FST: A Protein involved in Cellular Processes and Potential Drug Target

FST (FST variant FST317) is a protein that is expressed in various tissues of the body, including the brain, heart, and kidneys. It is a member of the FST gene family, which encodes for the protein FSTN (fostin) and related proteins. FSTN is a non-coding RNA molecule that has been shown to play a role in the regulation of stem cell proliferation and differentiation.

FST has been shown to be involved in many different processes in the body, including the development and maintenance of tissues, the regulation of ion channels and signaling pathways, and the control of cell growth and differentiation. It is also involved in the regulation of inflammation and immune responses.

One of the key features of FST is its ability to interact with other proteins and molecules. It has been shown to form complex with a wide range of proteins, including transcription factors, DNA-binding proteins, and protein-coding genes. These interactions play a crucial role in the regulation of gene expression and the development of various diseases.

FST has also been shown to be involved in many different signaling pathways. It has been shown to be involved in the regulation of cell proliferation, differentiation, and survival, as well as in the regulation of cell migration and the formation of tissues. It is also involved in the regulation of ion channels and signaling pathways that are critical for many different physiological processes, including cell signaling, muscle contractions, and blood pressure.

In addition to its role in the regulation of cellular processes, FST has also been shown to have potential as a drug target. Its interaction with other proteins and molecules makes it a potential target for small molecules and other therapeutic agents that can modulate its activity.

One of the key challenges in studying FST is its complex structure and the difficulty in predicting its function. While much research has been done to understand its structure and the relationships between its various subunits, the precise functions of its subunits are not yet fully understood. This is particularly challenging given the complexity of its interactions with other proteins and molecules.

Despite these challenges, research into FST is ongoing and is providing new insights into its role in the regulation of cellular processes and its potential as a drug target. Studies have shown that FST can be modulated by small molecules, including inhibitors of tyrosine kinase activity, which suggests that its activity may be dependent on the levels of these molecules in the cell.

In addition, some researchers have used RNA interference techniques to knockdown FST expression in order to study its function. This has led to insights into the regulation of its expression and the roles of its various subunits.

Overall, FST is a protein that is expressed in various tissues of the body and is involved in a wide range of cellular processes. Its complex structure and the difficulty in predicting its function make it a challenging target for study, but its potential as a drug target makes it a valuable tool for the development of new therapies. Further research is needed to fully understand its role in the regulation of cellular processes and its potential as a therapeutic agent.

Protein Name: Follistatin

Functions: Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH)

The "FST 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 FST 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

FSTL1 | FSTL3 | FSTL4 | FSTL5 | FTCD | FTCDNL1 | FTH1 | FTH1P1 | FTH1P10 | FTH1P11 | FTH1P12 | FTH1P2 | FTH1P20 | FTH1P22 | FTH1P24 | FTH1P3 | FTH1P4 | FTH1P5 | FTH1P7 | FTH1P8 | FTHL17 | FTL | FTLP16 | FTLP2 | FTLP3 | FTLP7 | FTMT | FTO | FTO-IT1 | FTOP1 | FTSJ1 | FTSJ3 | FTX | FUBP1 | FUBP3 | FUCA1 | FUCA2 | Fucosyl GM1 | Fucosyltransferase | FUNDC1 | FUNDC2 | FUNDC2P2 | FUNDC2P3 | FUOM | FURIN | FUS | FUT1 | FUT10 | FUT11 | FUT2 | FUT3 | FUT4 | FUT5 | FUT6 | FUT7 | FUT8 | FUT8-AS1 | FUT9 | FUZ | FXN | FXR1 | FXR2 | FXYD1 | FXYD2 | FXYD3 | FXYD4 | FXYD5 | FXYD6 | FXYD6-FXYD2 | FXYD7 | FYB1 | FYB2 | FYCO1 | FYN | FYTTD1 | FZD1 | FZD10 | FZD10-AS1 | FZD2 | FZD3 | FZD4 | FZD4-DT | FZD5 | FZD6 | FZD7 | FZD8 | FZD9 | FZR1 | G protein-Coupled Inwardly-Rectifying Potassium Channel (GIRK) | G Protein-Coupled Receptor Kinases (GRKs) | G0S2 | G2E3 | G2E3-AS1 | G3BP1 | G3BP2 | G6PC1 | G6PC2 | G6PC3 | G6PD | GA-binding protein