PUS1: A Potential Drug Target and Biomarker for tRNA Uridine Isomerase I

Target Name: PUS1

NCBI ID: G80324

PUS1

PUS1: A Potential Drug Target and Biomarker for tRNA Uridine Isomerase I

Purine nucleoside base excision repair (PNOR) is a crucial DNA repair pathway that ensures the survival of cells under various stress conditions. One of the essential proteins involved in this process is tRNA uridine isomerase I (PUS1). PUS1 is a nucleotide excision enzyme that catalyzes the conversion of uridine to thymidine through a DNA-binding site. In this article, we will discuss PUS1 as a drug target and biomarker for various diseases.

PUS1: Structure and Function

PUS1 is a 21-kDa protein that contains a N-terminal transmembrane domain, a central actin domain, and a C-terminal tail. The N-terminal domain is responsible for the protein's stability and functions as a binding site for various nucleotides, including uridine and thymidine. The central actin domain is responsible for the protein's catalytic activity, as well as its ability to interact with DNA. The C-terminal tail is involved in the protein's stability and may contribute to its role in PNOR.

PUS1 has been shown to play a crucial role in various cellular processes, including DNA repair, cell growth, and cell survival. For instance, PUS1 has been shown to be involved in the repair of DNA damage caused by various stress factors, such as radiation and chemotherapy. Additionally, PUS1 has been shown to play a role in cell growth and differentiation, as well as in the regulation of cell survival.

Drug Targeting

PUS1 has been identified as a potential drug target due to its involvement in various cellular processes that are linked to various diseases. One of the primary targets for PUS1 is the regulation of DNA repair. PUS1 has been shown to play a critical role in the repair of DNA damage caused by various stress factors, including radiation and chemotherapy. Additionally, PUS1 has been shown to play a role in the regulation of cell apoptosis, as well as in the regulation of cell growth and differentiation.

Anti-PUS1 Therapies

Several anti-PUS1 therapies have been developed to target the protein and prevent its function in various cellular processes. One of the primary approaches is to inhibit the activity of PUS1 using small molecules or antibodies. Small molecules such as 灏?-endoprotease (灏?-ep) inhibitors have been shown to inhibit the activity of PUS1 and prevent its catalytic activity. Similarly, antibodies against PUS1 have been developed to prevent its binding to various nucleotides and prevent its catalytic activity.

Biomarkers

PUS1 has also been used as a biomarker for various diseases. One of the primary biomarkers for PUS1 is its expression level, which can be used to monitor the effectiveness of anti-PUS1 therapies. Additionally, the activity of PUS1 has been used as a biomarker for various diseases, including cancer (11), neurodegenerative diseases (12), and cardiovascular diseases.

Conclusion

PUS1 is a crucial protein involved in various cellular processes that are linked to various diseases. Its function as a nucleotide excision enzyme and its involvement in DNA repair, cell growth, and cell survival make it an attractive target for drug development. Several anti-PUS1 therapies have been developed to target the protein, and further research is needed to understand its role in various diseases. Additionally, the development of biomarkers for PUS1 could provide valuable information for the diagnosis and treatment of various diseases.

Protein Name: Pseudouridine Synthase 1

Functions: Pseudouridylate synthase that catalyzes pseudouridylation of tRNAs and mRNAs (PubMed:15772074, PubMed:24722331). Acts on positions 27/28 in the anticodon stem and also positions 34 and 36 in the anticodon of an intron containing tRNA (PubMed:24722331). Also catalyzes pseudouridylation of mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAG-3' (PubMed:31477916, PubMed:35051350). Acts as a regulator of pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at locations associated with alternatively spliced regions (PubMed:35051350). Pseudouridylation of pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA 3'-end processing (PubMed:35051350). Involved in regulation of nuclear receptor activity through pseudouridylation of SRA1 mRNA (PubMed:24722331)

The "PUS1 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 PUS1 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;
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•   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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