RSAD1: A Potential Drug Target and Biomarker (G55316)

Target Name: RSAD1

NCBI ID: G55316

RSAD1

Other Name(s): Putative heme chaperone | RSAD1 variant 1 | oxygen-independent coproporphyrinogen-III oxidase-like protein RSAD1 | HemW | putative heme chaperone | radical S-adenosyl methionine domain containing 1 | Radical S-adenosyl methionine domain containing 1, transcript variant 1 | Radical S-adenosyl methionine domain-containing protein 1, mitochondrial | RSAD1_HUMAN | Oxygen-independent coproporphyrinogen-III oxidase-like protein RSAD1

RSAD1: A Potential Drug Target and Biomarker

Ribosome sarcosome adaptase (RSA) domain containing 1 (RSAD1) is a protein that plays a critical role in protein synthesis and post-translational modification (PTM) in eukaryotic cells. It is a key regulator of the initiation of protein synthesis and the folding of proteins into their functional states. RSAD1 is composed of a nucleotide-binding oligomeric domain (NBD), a Rossmann-fold, and a carboxy-terminal domain (CTD). The RSA domain is responsible for the protein's unique structure and function, allowing it to interact with various protein and nucleic acid species.

The RSA domain is involved in several different PTMs, including PTMs that regulate protein stability, localization, and interactions with other cellular components. One of the most significant functions of RSAD1 is its role in the regulation of protein stability. RSAD1 has been shown to interact with multiple protein substrates, including histone-associated proteins and nucleic acid-protein interactions. These interactions play a crucial role in regulating the stability and localization of these proteins, and are implicated in a wide range of cellular processes, including cell growth, differentiation, and stress responses.

In addition to its role in protein stability, RSAD1 is also involved in the regulation of protein-protein interactions and protein-nucleic acid interactions. The RSA domain has been shown to interact with several nucleic acid-protein interfaces, including the binding sites of RNA binding proteins. These interactions allow RSAD1 to regulate the activity of these proteins and influence a wide range of cellular processes, including gene expression, DNA replication, and repair, as well as cell survival and reproduction.

The potential drug targets for RSAD1 are numerous and varied. One of the most promising targets is the inhibition of RSAD1 activity, which has been shown to have a wide range of therapeutic potential in various cellular processes, including cancer, neurodegenerative diseases, and autoimmune disorders. The inhibition of RSAD1 activity has been shown to reduce the activity of multiple protein substrates, including histone-associated proteins, and to improve the stability and localization of these proteins.

Another potential drug target for RSAD1 is the modulation of its stability. The stability of RSAD1 is regulated by multiple factors, including its phosphorylation state, its ubiquitination state, and its interactions with other cellular components. Modulation of these factors could provide a means of therapeutic intervention in diseases where RSAD1 dysfunction is implicated, such as cancer, neurodegenerative diseases, and autoimmune disorders.

The RSAD1 gene has also been implicated in a number of diseases and disorders, including cancer, neurodegenerative diseases, and autoimmune disorders. The majority of these diseases are characterized by the accumulation of misfolded or dysfunctional proteins, which can lead to a wide range of cellular dysfunction and dysfunctional processes. The RSAD1 gene is thought to play a critical role in the regulation of protein stability and localization, and its dysfunction may contribute to the development and progression of these diseases.

In conclusion, RSAD1 is a protein that is involved in a wide range of cellular processes and functions, including protein synthesis, post-translational modification, and protein-protein and protein-nucleic acid interactions. Its unique structure and function, as well as its involvement in multiple cellular processes, make it a promising target for therapeutic intervention in a wide range of diseases and disorders. Further research is needed to fully understand the role of RSAD1 in cellular processes and to develop effective therapies based on its properties.

Protein Name: Radical S-adenosyl Methionine Domain Containing 1

Functions: May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen-III oxidase activity (Probable). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity)

The "RSAD1 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 RSAD1 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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