ATP5PB: A Drug Target and Potential Biomarker for Mitochondrial Function

Target Name: ATP5PB

NCBI ID: G515

ATP5PB: A Drug Target and Potential Biomarker for Mitochondrial Function

ATP (adenosine triphosphate) is the primary energy source for the cell and represents the powerhouse of the cell. It is generated from the substrate pool and converted to adenosine by the action of ATP synthase (ATP synthase I) through the release of a high-energy molecule, ADP. Adenosine is then converted to ATP by the action of ATP synthase II, which uses a different substrate pool. The ATP synthase is a complex protein that consists of several subunits, including subunit B1 (ATP synthase subunit B1), which is a key component in the production of ATP from the substrate pool.

ATP5PB, also known as ATP synthase subunit B1, is a protein that belongs to the ATP synthase family and is responsible for the production of ATP from the substrate pool. It is a key component of the mitochondrial F0 complex, which is the first step in the production of ATP from the substrate pool. ATP5PB is essential for the function of the mitochondria, as it plays a critical role in the production of ATP, which is the energy source for the cell.

Drug Targets and Biomarkers

ATP5PB is a drug target that can be targeted by small molecules to inhibit its function. This approach can be used to treat various diseases, including cancer, neurodegenerative diseases, and cardiovascular diseases. The development of small molecules that inhibit the function of ATP5PB is an active area of research, and there are several ongoing clinical trials using these molecules to treat various diseases.

One of the potential biomarkers for the disease caused by ATP5PB dysfunction is the decline in ATP production. This decline in ATP production can be measured using various assays, including the assay for Adenosine Monophosphate (AMP) and Adenosine Triphosphate (ATP). The AMP assay is a sensitive assay for the production of ATP and can be used to measure the level of ATP produced by the mitochondria. The ATP assay is used to measure the level of ATP available for the cell to use.

Another potential biomarker for the disease caused by ATP5PB dysfunction is the decline in cellular metabolism. This decline in cellular metabolism can be measured using various assays, including the assay for Cellular Metabolism, such as the Light-Dependent Xenon Biosensor (LDX) assay.

Molecular Mechanisms

The ATP synthase is a complex protein that consists of several subunits, including subunit B1. The subunit B1 plays a critical role in the production of ATP from the substrate pool. It is a key component of the mitochondrial F0 complex, which is the first step in the production of ATP from the substrate pool.

ATP5PB is involved in the production of ATP from the substrate pool by participating in the catalytic cycle of ATP synthase. It is part of the active site, where the substrate is binded and the ATP synthase activity is optimized. The active site is the region of the protein where the substrate is bound and the catalytic activity is optimized.

The ATP synthase is a proton pump that uses ATP as a proton source to pump protons out of the mitochondria and into the cytosol. This process is called H+ transporting and is a key aspect of the ATP synthase function. The H+ transporting is critical for the function of the

Protein Name: ATP Synthase Peripheral Stalk-membrane Subunit B

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 and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements

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