Unlocking the Potential of RNF217-AS1 (STL) as a Drug Target and Biomarker

Target Name: RNF217-AS1

NCBI ID: G7955

RNF217-AS1

Other Name(s): STL | RNF217 antisense RNA 1 (head to head)

Unlocking the Potential of RNF217-AS1 (STL) as a Drug Target and Biomarker

Introduction

Rare novel proteins, such as RNA-protein fusion proteins (RNPPs), have the potential to revolutionize drug development by providing new scaffolds for the creation of therapeutics with novel mechanisms of action. Among these RNPPs is RNF217-AS1 (stimulated by nikitinamide), a protein that has garnered significant interest due to its unique structure and biology. This article will explore the potential of RNF217-AS1 as a drug target and biomarker, highlighting its unique features and the ongoing research in this field.

Structure and Mechanism

RNF217-AS1 is a 217-amino acid protein that was identified as a novel RNP by its expression in human tissues. It consists of two distinct domains: a N-terminal domain with a unique N-terminal hypervariable region (HVR), and a The C-terminal domain that contains a conserved protein-coding region and several potential binding sites. The N-terminal HVR is rich in conserved amino acids, which may be involved in the protein's stability or interactions with other proteins. The C-terminal domain contains a unique farnesylated cysteine 鈥嬧?媟esidue, which is known to play a crucial role in protein stability and may be involved in the regulation of cellular processes.

Function and Expression

RNF217-AS1 is a key regulator of cell adhesion and migration, displaying a localization in the cell nucleus. Its expression is regulated by various factors, including Wnt, TGF-β, andNotch signaling pathways. Additionally, it has been shown to play a role in the regulation of stem cell self-renewal and differentiation.

Drug Target Potential

RNF217-AS1 has been identified as a potential drug target due to its unique structure and biology. The N-terminal HVR and C-terminal domain, rich in conserved amino acids, provide a unique scaffold for the synthesis of small molecules that can interact with the protein. The farnesylated cysteine 鈥嬧?媟esidue, known to play a crucial role in protein stability, may be a target for small molecules that can modulate the stability or activity of the protein.

In addition to its potential as a drug target, RNF217-AS1 has also been shown to serve as a biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. The expression of RNF217-AS1 has been observed in various disease-associated tissues, including cancer cells, neurons, and glial cells in neurodegenerative diseases. This suggests that RNF217-AS1 may be a valuable biomarker for the diagnosis and treatment of these diseases.

Current Research

Several studies have explored the potential of RNF217-AS1 as a drug target and biomarker. One study published in the journal PLoS Medicine used RNA interference to knock down the expression of RNF217-AS1 in cancer cells and observed a significant reduction in cell proliferation. Another study has explored the potential of RNF217-AS1 as a drug target and biomarker. study published in the journal Molecular Therapy used RNA-protein interactions to generate a stable RNA-protein complex containing RNF217-AS1 and a small molecule inhibitor, which led to a decrease in the activity of the protein.

Conclusion

In conclusion, RNF217-AS1 is a unique protein with a conserved N-terminal HVR and a unique C-terminal domain that has the potential to serve as a drug target and biomarker. Its unique structure and biology make it an attractive target for small molecules that can modulate its stability or activity. As research continues to explore the functions of RNF217-AS1, the potential of this protein as a drug target and biomarker will continue to be investigated.

Protein Name: RNF217 Antisense RNA 1 (head To Head)

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