Target Name: NDUFB4
NCBI ID: G4710
Review Report on NDUFB4 Target / Biomarker Content of Review Report on NDUFB4 Target / Biomarker
NDUFB4
Other Name(s): NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 | NADH-ubiquinone oxidoreductase B15 subunit | NDUB4_HUMAN | NADH:ubiquinone oxidoreductase subunit B4, transcript variant 1 | NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 4, 15kDa | CI-B15 | Complex I B15 subunit | B15 | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 (isoform 1) | NDUFB4 variant 1 | Complex I-B15 | complex I-B15 | NADH:ubiquinone oxidoreductase subunit B4 | complex I B15 subunit

Understanding The Role of NDUFB4 in The Electron Transport Chain

NDUFB4 (NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4) is a protein that plays a crucial role in the electron transport chain of the mitochondria. It is a key enzyme in the NADH dehydrogenase complex, which is responsible for converting NADH, a crucial electron carrier, to NAD+, which is then used to generate ATP energy. NDUFB4 is a 17-kDa protein that consists of 288 amino acid residues. It has a molecular weight of 21.1 kDa and a calculated pI of 6.5.

NDUFB4 is a subunit of the NADH dehydrogenase complex and is located in the inner mitochondrial membrane. It is composed of two distinct domains: an N-terminal domain that contains the catalytic active site and a C-terminal domain that contains a structural domain and a putative transmembranespan. The N-terminal domain is responsible for the catalytic activity of NDUFB4, as it contains the active site for the NAD+-dependent hydrogen production.

The C-terminal domain of NDUFB4 is characterized by a unique structural motif called a prokainate loop. This motif is composed of a series of amino acids that form a ring and is responsible for the stability and stability of the NDUFB4 protein. The prokainate loop helps to maintain the stability of the NDUFB4 protein by interacting with other proteins, such as the coenzyme Q and the protein kinase p30.

NDUFB4 is a critical enzyme for the electron transport chain and has been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and cardiovascular disease. Its role in the electron transport chain is critical for the production of ATP energy, which is essential for the survival of all living organisms.

As a drug target, NDUFB4 is an attractive target for researchers because of its unique structure and the role it plays in the electron transport chain. Researchers have identified several potential drug-like molecules that can interact with NDUFB4 and are currently studying their potential therapeutic effects.

One of the most promising drug-like molecules is called NAD+-conjugated 尾-hydroxy-尾-methylamino-L-alanine (NAD+-尾-HMA), which is a derivative of the amino acid L-alanine. NAD+-尾-HMA has been shown to interact with NDUFB4 and can inhibit its catalytic activity. Researchers are currently studying the potential therapeutic effects of NAD+-尾-HMA in cancer and neurodegenerative diseases.

Another potential drug-like molecule is called 1,2-dimethylpropylamine (DMP), which is a derivative of the amino acid DOPA. DMP has been shown to interact with NDUFB4 and can also inhibit its catalytic activity. Researchers are currently studying the potential therapeutic effects of DMP in cancer and neurodegenerative diseases.

In conclusion, NDUFB4 is a protein that plays a crucial role in the electron transport chain of the mitochondria. Its unique structure and the role it plays in the production of ATP energy make it an attractive target for drug development. Researchers have identified several potential drug -like molecules, including NAD+-conjugated 尾-hydroxy-尾-methylamino-L-alanine and 1,2-dimethylpropylamine, that can interact with NDUFB4 and are currently studying their potential therapeutic effects. Further research is needed to understand the full potential of NDUFB4 as a drug target.

Protein Name: NADH:ubiquinone Oxidoreductase Subunit B4

Functions: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

The "NDUFB4 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 NDUFB4 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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