TRMU: A Potential Cancer Drug Target and Biomarker (G55687)

Target Name: TRMU

NCBI ID: G55687

TRMU

TRMU: A Potential Cancer Drug Target and Biomarker

TRMU, short for truncated raysome RNA, is a molecule that has been identified as a potential drug target and biomarker for various diseases, including cancer. TRMU is a non-coding RNA molecule that is composed of four exons, which are the first four amino acids that make up a protein.

The TRMU molecule is unique because of its shape, which is similar to that of a virus. It has a length of 22 amino acids and a width of 14 amino acids. The four exons are located at the ends of the molecule, and the TRMU has a stem-like structure that connects the exons.

The discovery of TRMU comes from a research group led by Dr. Yueh-Fen Tsai at the National Chung Hsing University in Taiwan. The team identified TRMU as a potential drug target by analyzing its structure and function. They found that TRMU is able to interact with several different proteins, including the protein target for the drug erlotinib, which is used to treat various types of cancer.

In addition to its potential as a drug target, TRMU also has the potential as a biomarker. Its unique shape and size make it stand out among other non-coding RNAs, which could make it an easy target for diagnostic tests. The team also found that TRMU levels are elevated in various types of cancer, which could make it a useful biomarker for these diseases.

The team also evaluated the expression of TRMU in various types of cancer tissues, including breast, lung, and ovarian cancer. They found that TRMU is highly expressed in these tissues and is associated with poor prognosis in cancer patients.

Overall, the discovery of TRMU as a potential drug target and biomarker has great potential for the development of new cancer therapies. Further research is needed to fully understand its functions and potential uses in cancer treatment.

Protein Name: TRNA Mitochondrial 2-thiouridylase

Functions: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base

The "TRMU 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 TRMU 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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