Unlocking the Potential of ATP5MF: A Potential Drug Target and Biomarker

Target Name: ATP5MF

NCBI ID: G9551

ATP5MF

Unlocking the Potential of ATP5MF: A Potential Drug Target and Biomarker

ATP (adenylyl triphosphate) is one of the most critical energy molecules in the cell. It is a small molecule that plays a central role in cell signaling, protein synthesis, and DNA replication. ATP is synthesized fromADP(+) by the process of phosphorylation, which involves the transfer of a phosphate group from a phosphate donor to an ADP molecule. The ATP synthase enzyme is the primary enzyme responsible for generating ATP from ADP. The Fo membrane domain of the ATP synthase enzyme is the site of the ATP synthase reaction, and it is a well-established protein that has been extensively studied. The F1Fo-ATP synthase complex is a protein complex that consists of the ATP synthase enzyme, F1 subunit, and the Fo membrane domain. The F1Fo-ATP synthase complex is responsible for generating ATP and is a potential drug target and biomarker.

The ATP synthase reaction is a critical process for maintaining cellular energy homeostasis. It is the rate at which ATP is generated from ADP to provide energy for cellular processes. The process of ATP synthesis involves the transfer of a phosphate group from a phosphate donor to an ADP molecule. The ATP synthase enzyme is the primary enzyme responsible for generating ATP from ADP. The Fo membrane domain of the ATP synthase enzyme is the site of the ATP synthase reaction, and it is a well-established protein that has been extensively studied.

The F1Fo-ATP synthase complex is a protein complex that consists of the ATP synthase enzyme, F1 subunit, and the Fo membrane domain. The F1Fo-ATP synthase complex is responsible for generating ATP and is a potential drug target and biomarker. The F1 subunit of the F1Fo-ATP synthase complex is a protein that contains a unique catalytic active site. It has been shown to be involved in the regulation of ATP synthase activity and may play a role in the development of ATP synthase-related diseases.

The Fo membrane domain of the ATP synthase enzyme is a protein that is located on the surface of the ATP synthase enzyme. It is responsible for the regulation of ATP synthase activity and has been shown to play a role in the regulation of cellular processes. The Fo membrane domain is a well-established protein that has been extensively studied, and it is thought to be involved in the regulation of ATP synthase activity by affecting the structure and function of the ATP synthase enzyme.

The potential drug target for the F1Fo-ATP synthase complex is the regulation of ATP synthase activity. It is believed that the F1Fo-ATP synthase complex plays a role in the regulation of ATP synthase activity and may be a potential drug target for the treatment of diseases related to ATP synthase activity.

The F1Fo-ATP synthase complex is also a potential biomarker for the regulation of ATP synthase activity. The F1Fo-ATP synthase complex is expressed in many different cell types and is involved in the regulation of cellular processes. It is thought to be involved in the regulation of ATP synthase activity and may be a potential biomarker for the treatment of diseases related to ATP synthase activity.

Conclusion

In conclusion, the F1Fo-ATP synthase complex is a protein complex that is responsible for generating ATP and is a potential drug target and biomarker. The F1Fo-ATP synthase complex is thought to be involved in the regulation of ATP synthase activity and may be a potential

Protein Name: ATP Synthase Membrane Subunit F

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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane

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•   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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