Target Name: Ribonuclease MRP
NCBI ID: P19102
Review Report on Ribonuclease MRP Target / Biomarker Content of Review Report on Ribonuclease MRP Target / Biomarker
Ribonuclease MRP
Other Name(s): Rnase/Mrp complex

Ribonuclease MRP: A Potential Drug Target and Biomarker

Ribonuclease MRP (Rnase/Mrp complex), also known as Nuclease MRP, is a highly specific endonuclease that cleaves double-stranded RNA with high efficiency. This enzyme plays a crucial role in the regulation of gene expression and is involved in various cellular processes, including DNA replication, transcription, and RNA processing. Its unique catalytic mechanism and broad substrate specificity make it an attractive drug target for researchers.

The Ribonuclease MRP enzyme is a member of the nucleases family 1 (Nu family 1) and is classified as an endonuclease, which means it removes a nucleotide from a double-stranded RNA. This class of enzymes includes other well-known enzymes such as restriction enzymes and DNA polymerase. Endonucleases are widely used in molecular biology research as they allow researchers to study the dynamics of RNA molecules and their role in various cellular processes.

The Ribonuclease MRP enzyme has a specificity for double-stranded RNA and is capable of cleaving a wide range of RNA types, including microRNA (miRNA), double-stranded RNA (dsRNA), and small interfering RNA (siRNA). Its high specificity is due to the unique three-dimensional structure of the enzyme and its catalytic active site, which is composed of a hyperactive center loop and a base-pair binding site.

The catalytic mechanism of Ribonuclease MRP involves a series of steps that ultimately result in the cleavage of double-stranded RNA. The first step is the formation of a RNA-DNA complex, where the RNA molecule is bound to the DNA template. The second step is the cleavage of the RNA-DNA complex by the enzyme, which occurs through a series of intermediate states. The final step is the formation of a double-stranded RNA break, which results in the cleavage of the RNA molecule.

The Ribonuclease MRP enzyme has a unique feature that allows it to cleave double-stranded RNA with high efficiency, even in the presence of DNA templates. This property makes it an attractive drug target, as researchers can use small interfering RNA (siRNA) to deliver targeted mutations to specific genes. SiRNA is a naturally occurring RNA molecule that can be designed to specifically target mRNAs for degradation. By using siRNA, researchers can knock down the expression of a gene of interest and study its function.

Another promising approach to target Ribonuclease MRP is to use small molecules as inhibitors. Researchers have synthesized a variety of small molecules that can inhibit the activity of Ribonuclease MRP and prevent its catalytic activity. These small molecules can be used to treat various diseases, including cancer , neurodegenerative diseases, and genetic disorders.

In addition to its potential as a drug target, Ribonuclease MRP also has potential as a biomarker. The Ribonuclease MRP enzyme can be used to study the effects of drugs on gene expression and can be used as a tool to study the underlying mechanisms of various diseases . For example, researchers have used Ribonuclease MRP to study the effects of cancer treatments on gene expression and to identify potential biomarkers for cancer.

In conclusion, Ribonuclease MRP is an attractive drug target and biomarker due to its unique catalytic mechanism and broad substrate specificity. Its ability to cleave double-stranded RNA with high efficiency makes it an attractive target for small interfering RNA (siRNA) treatments, and its use as a tool to study the underlying mechanisms of various diseases makes it a valuable addition to the arsenal of molecular biologists.

Protein Name: Ribonuclease MRP

The "Ribonuclease MRP 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 Ribonuclease MRP 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

Ribonuclease P Complex | Ribosomal protein S6 kinase (RSK) | Ribosomal Protein S6 Kinase, 70kDa (p70S6K) | Ribosomal Protein S6 Kinase, 90kDa | Ribosomal subunit 40S | Ribosome-associated complex | RIC1 | RIC3 | RIC8A | RIC8B | RICH1-AMOT complex | RICTOR | RIDA | RIF1 | RIGI | RIIAD1 | RILP | RILPL1 | RILPL2 | RIMBP2 | RIMBP3 | RIMBP3B | RIMBP3C | RIMKLA | RIMKLB | RIMKLBP2 | RIMOC1 | RIMS1 | RIMS2 | RIMS3 | RIMS4 | RIN1 | RIN2 | RIN3 | RING1 | RINL | RINT1 | RIOK1 | RIOK2 | RIOK3 | RIOK3P1 | RIOX1 | RIOX2 | RIPK1 | RIPK2 | RIPK3 | RIPK4 | RIPOR1 | RIPOR2 | RIPOR3 | RIPPLY1 | RIPPLY2 | RIPPLY3 | RIT1 | RIT2 | RITA1 | RLBP1 | RLF | RLIM | RLIMP1 | RLN1 | RLN2 | RLN3 | RMC1 | RMDN1 | RMDN2 | RMDN3 | RMI1 | RMI2 | RMND1 | RMND5A | RMND5B | RMRP | RMST | RN7SK | RN7SKP119 | RN7SKP145 | RN7SKP16 | RN7SKP168 | RN7SKP18 | RN7SKP2 | RN7SKP203 | RN7SKP246 | RN7SKP252 | RN7SKP255 | RN7SKP257 | RN7SKP26 | RN7SKP275 | RN7SKP287 | RN7SKP292 | RN7SKP3 | RN7SKP35 | RN7SKP48 | RN7SKP51 | RN7SKP55 | RN7SKP64 | RN7SKP67 | RN7SKP80 | RN7SL1 | RN7SL128P