ATP5F1A: A Potential Drug Target and Biomarker (G498)

Target Name: ATP5F1A

NCBI ID: G498

ATP5F1A

ATP5F1A: A Potential Drug Target and Biomarker

ATP (adenosine triphosphate) is a crucial molecule in the process of cell signaling. It plays a vital role in the transfer of energy from the cell's energy sources to its target, thereby regulating various cellular processes. In particular, ATP is involved in the transfer of energy from the cell's energy reserves to the cytosol, where it functions as an intracellular signaling molecule.

The molecule ATP5F1A, also known as ORM (Oxidative stress-Inducible Regulator), is a potential drug target and biomarker in various diseases. It is a key regulator of the cellular response to oxidative stress, which is caused by the accumulation of reactive oxygen species (ROS) in the cell. ROS can cause damage to cellular components, including DNA, RNA, and proteins, leading to the development of various diseases, including cancer, neurodegenerative diseases, and systemic inflammatory diseases.

ATP5F1A is a protein that is expressed in various tissues and cells, including the brain, heart, liver, and pancreas. It is involved in the regulation of cellular processes, including cell signaling, DNA replication, and protein synthesis. It is also involved in the regulation of cellular responses to oxidative stress, which is caused by the accumulation of ROS in the cell.

The identification of ATP5F1A as a potential drug target and biomarker comes from several studies that have demonstrated its involvement in various diseases. For example, several studies have shown that ATP5F1A is involved in the development and progression of cancer, including breast, ovarian, and prostate cancer. Additionally, the molecule has been shown to be involved in the development of neurodegenerative diseases, including Alzheimer's and Parkinson's diseases.

The potential drug target for ATP5F1A is based on its role in the regulation of cellular responses to oxidative stress. Drugs that can inhibit the activity of ATP5F1A have been shown to have therapeutic potential in various diseases. For example, several studies have shown that inhibitors of ATP5F1A, such as L-NAME (L-Nitrosyl-ATP), have therapeutic potential in the treatment of cancer, neurodegenerative diseases, and systemic inflammatory diseases.

In addition to its potential therapeutic applications, ATP5F1A is also a valuable biomarker for the diagnosis and assessment of various diseases. The molecule can be used as a target for diagnostic tests, such as mass spectrometry (MS), to monitor the expression and activity of ATP5F1A in various tissues and cells. This technique can be used to diagnose diseases that are characterized by the accumulation of ROS in the cell, such as cancer, neurodegenerative diseases, and systemic inflammatory diseases.

In conclusion, ATP5F1A is a protein that is involved in the regulation of various cellular processes, including cell signaling, DNA replication, and protein synthesis. It is also involved in the regulation of cellular responses to oxidative stress, which is caused by the accumulation of ROS in the cell. The identification of ATP5F1A as a potential drug target and biomarker for various diseases makes it an attractive target for therapeutic development. Further research is needed to fully understand the role of ATP5F1A in the development and progression of various diseases.

Protein Name: ATP Synthase F1 Subunit Alpha

Functions: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (PubMed:30146159)

The "ATP5F1A 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 ATP5F1A 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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