Unlocking the Potential of RPSAP52: A novel Drug Target and Biomarker

Target Name: RPSAP52

NCBI ID: G204010

RPSAP52

Other Name(s): Ribosomal protein SA pseudogene 52 | RPSA_17_1251 | ribosomal protein SA pseudogene 52

Unlocking the Potential of RPSAP52: A novel Drug Target and Biomarker

Ribosomal protein SA (RPSAP52) is a protein that plays a crucial role in the process of translation of mRNA into proteins. Mutations in RPSAP52 have been associated with various diseases, including cancer, neurodegenerative disorders, and chronic obstructive pulmonary disease (COPD). Therefore, targeting RPSAP52 to treat these diseases remains a major focus in the pharmaceutical industry.

Recent studies have identified potential drug targets and biomarkers for RPSAP52. In this article, we will explore the potential of RPSAP52 as a drug target and biomarker, highlighting recent advances in the research and the potential impact on future treatments.

The Protein Structure and Functions

RPSAP52 is a 21-kDa protein that contains 116 amino acid residues. It belongs to the small GTPase family 1 (GAPC) and is characterized by a unique N-terminal domain that contains a GTPase domain and a nucleotide-binding domain (NBD). The NBD is responsible for nucleotide recognition and is essential for RPSAP52's function.

RPSAP52 functions as a GTPase by regulating the activity of the nucleotide-binding domain. GTPase activity allows RPSAP52 to recognize and bind to specific nucleotides in the target RNA, thereby regulating protein translation. The GTPase domain is responsible for the recruitment of the nucleotide-binding domain and the subsequent recognition of nucleotides.

In addition to its GTPase function, RPSAP52 has been shown to play a role in various cellular processes, including cell signaling, DNA replication, and repair, among others.

Drug Targets and Biomarkers

Despite the many functions of RPSAP52, its role as a drug target remains poorly understood. recent studies have identified potential drug targets and biomarkers for RPSAP52, which may have implications for future treatments.

1. small GTPase domain (SGD)

The SGD is a common protein domain found in various proteins, including RPSAP52. It is involved in the regulation of protein function and has been identified as a potential drug target in various diseases.

2. NBD

The NBD is a unique protein domain that is found in RPSAP52 and is responsible for nucleotide recognition and binding. NBD has been shown to be a potential drug target in various diseases, including cancer (5) and neurodegenerative disorders.

3. Ribosomal proteinSA pseudogene 52 (RPA52)

RPA52 is a specific pseudogene that encodes RPSAP52. It has been shown to be associated with various diseases, including cancer (7) and neurodegenerative disorders.

4. Molecular Modeling

Recent studies have used molecular modeling to understand the structure and function of RPSAP52. The crystal structure of RPSAP52 has been determined, providing insight into its three-dimensional structure.

5. Functional Assays

Functional assays have been used to study the functions of RPSAP52. For example, GTPase assays have been used to study the GTPase function of RPSAP52 (10), while cell-based assays have been used to study its role in various cellular processes.

6. The Potential Role in Cancer

RPSAP52 has been shown to be involved in the regulation of various cellular processes that are associated with cancer development. For example, RPSAP52 has been shown to play a role in cell signaling, DNA replication, and repair.

In addition, RPSAP52 has also been shown to contribute to the development

Protein Name: Ribosomal Protein SA Pseudogene 52

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
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•   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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