SMPDL3B: A Potential Drug Target and Biomarker for Acid Sphingomyelinase-Like Phosphodiesterase 3b

Target Name: SMPDL3B

NCBI ID: G27293

SMPDL3B

SMPDL3B: A Potential Drug Target and Biomarker for Acid Sphingomyelinase-Like Phosphodiesterase 3b

Sphingomyelinase-like phosphodiesterase 3b (SMPDL3B) is a protein that is expressed in various tissues throughout the body, including the liver, pancreas, and heart. It is a member of the superfamily of phospholipase D (SPLD) enzymes, which are involved in the breakdown of sphingomyelin, a major component of cell membranes. abnormally expressed SMPDL3B has been implicated in a number of diseases, including obesity, type 2 diabetes, and neurodegenerative disorders.

SMPDL3B is a 21-kDa protein that contains 115 amino acid residues. It is characterized by a catalytic active site, a catalytic region, and a C-terminus. The catalytic active site is located at the N-terminus of the protein and is responsible for the substrate recognition and catalytic activity. The catalytic region is located between the N-terminus and the C-terminus and is responsible for the substrate binding and catalytic activity. The C-terminus of the protein is involved in the protein-protein interaction and contributes to the stability of the protein.

SMPDL3B has been shown to be involved in a number of cellular processes, including the regulation of sphingomyelin homeostasis, cell signaling, and inflammation. It has been shown to interact with a variety of protein substrates, including sphingomyelin, ceramide, and inositol. These interactions have important implications for the function of SMPDL3B and its potential as a drug target.

SMPDL3B has been shown to play a role in the regulation of sphingomyelin homeostasis. Sphingomyelin is a major component of cell membranes and is involved in a number of cellular processes, including the regulation of ion and water transport, and the maintenance of membrane stability. abnormally expressed SMPDL3B has been shown to contribute to the misfolding and stability of sphingomyelin, which can lead to the accumulation of toxic sphingomyelin species and the development of sphingomyelin-related diseases.

SMPDL3B has also been shown to be involved in cell signaling. It has been shown to interact with a variety of protein substrates, including sphingomyelin, ceramide, and inositol. These interactions have important implications for the regulation of cellular signaling processes and the role of SMPDL3B in cell signaling.

SMPDL3B has also been shown to be involved in inflammation. It has been shown to interact with a variety of protein substrates, including nuclear factor kappa B (NFkB), which is a known regulator of inflammation. These interactions have important implications for the regulation of inflammation and the role of SMPDL3B in inflammation.

Given the involvement of SMPDL3B in a number of cellular processes, it is a potential drug target. The development of SMPDL3B inhibitors has the potential to treat a variety of diseases, including obesity, type 2 diabetes, and neurodegenerative disorders. Additionally, the regulation of SMPDL3B activity could be a useful target for the development of new therapeutic approaches for treating a variety of diseases.

In conclusion, SMPDL3B is a protein that is involved in a number of cellular processes and has been implicated in a variety of diseases. Its role in sphingomyelin homeostasis, cell signaling, and inflammation makes it a potential drug target. The development of SMPDL3B inhibitors has the potential to treat a variety of diseases and

Protein Name: Sphingomyelin Phosphodiesterase Acid Like 3B

Functions: Lipid-modulating phosphodiesterase (PubMed:26095358). Active on the surface of macrophages and dendritic cells and strongly influences macrophage lipid composition and membrane fluidity. Acts as a negative regulator of Toll-like receptor signaling (By similarity). Has in vitro phosphodiesterase activity, but the physiological substrate is unknown (PubMed:26095358). Lacks activity with phosphocholine-containing lipids, but can cleave CDP-choline, and can release phosphate from ATP and ADP (in vitro) (By similarity)

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•   general information;
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•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
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•   related combination drugs;
•   pharmacochemistry experiments;
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•   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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