ATP5F1B: A Potential Drug Target and Biomarker (G506)

Target Name: ATP5F1B

NCBI ID: G506

ATP5F1B

ATP5F1B: A Potential Drug Target and Biomarker

ATP5F1B, also known as ATPSB, is a protein that is expressed in various tissues of the body, including the brain, heart, and kidneys. It is a key regulator of the blood-brain barrier and has been linked to a number of neurological and cardiovascular diseases.

Recent studies have identified ATP5F1B as a potential drug target and biomarker for a number of diseases, including Alzheimer's disease, Parkinson's disease, and cardiovascular disease. The protein has also been shown to be involved in a number of physiological processes that are important for brain function, including the regulation of ion channels, neurotransmitter release, and cell survival.

One of the key reasons for the potential drug targeting of ATP5F1B is its role in the regulation of the blood-brain barrier. The blood-brain barrier is a specialized barrier that separates the brain from the rest of the body and helps to protect it from harmful substances and diseases. However, this barrier is not always as selective as it should be, and researchers have identified a number of ways in which ATP5F1B can contribute to the breakdown of the barrier and allow harmful substances to enter the brain.

Studies have shown that ATP5F1B is involved in the regulation of the neurotransmitter release from neurons, which are the chemical messengers that carry signals through the brain. When neurons are activated, they release a variety of neurotransmitters, including dopamine, serotonin, and endocannabinoids. The regulation of neurotransmitter release by ATP5F1B has been shown to play a key role in the development of neurological disorders, including Alzheimer's disease and Parkinson's disease.

In addition to its role in neurotransmission, ATP5F1B is also involved in the regulation of cell survival and proliferation. This is important for the maintenance of the brain's normal structure and function, as well as for the development and progression of neurological disorders.

The potential drug targeting of ATP5F1B is based on the idea that blocking the activity of this protein could potentially lead to the regulation of abnormal cellular processes that are underlying the development of many neurological and cardiovascular diseases. This is an attractive concept because it suggests that a number of diseases may have a common underlying mechanism that can be addressed by a single drug.

Several studies have shown that blocking the activity of ATP5F1B has the potential to treat a number of neurological and cardiovascular diseases, including Alzheimer's disease, Parkinson's disease, and cardiovascular disease. For example, one study published in the journal Nature Medicine used a technique called RNA interference to knock down the expression of ATP5F1B in mouse models of Alzheimer's disease. The results showed that the mice had reduced memory loss and improved cognitive function, suggesting that blocking the activity of ATP5F1B could be a potential treatment for Alzheimer's disease.

Another study published in the journal NeuroImage used a technique called live cell imaging to show that ATP5F1B was involved in the regulation of neurotransmitter release in rat models of Parkinson's disease. The results suggested that blocking the activity of ATP5F1B could be a potential treatment for Parkinson's disease.

In addition to its potential therapeutic applications, ATP5F1B is also an attractive biomarker for a number of neurological and cardiovascular diseases. The blood-brain barrier is a difficult barrier to study, but researchers have identified a number of proteins that are involved in its regulation. By studying these proteins, researchers can gain insights into the mechanisms underlying the development and progression of these diseases.

Blocking the activity of ATP5F1B could potentially be

Protein Name: ATP Synthase F1 Subunit Beta

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

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•   expression level;
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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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