SMAD1: A Potential Drug Target and Biomarker for Transforming Growth Factor-尾 Signaling

Target Name: SMAD1

NCBI ID: G4086

SMAD1

SMAD1: A Potential Drug Target and Biomarker for Transforming Growth Factor-尾 Signaling

The transforming growth factor-尾 (TGF-β) signaling pathway is a crucial regulator of cell growth, differentiation, and survival. It plays a vital role in the development, maintenance, and repair of tissues, and is often dysregulated in many diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders. The SMAD1 protein, a key member of the TGF-β signaling pathway, has emerged as a promising drug target and biomarker for several reasons.

SMAD1: Structure and Function

SMAD1 is a 21-kDa protein that belongs to the SMAD family of proteins. It is expressed in various tissues and cells, including liver, muscle, heart, and breast cells. SMAD1 functions as a negative regulator of TGF-β signaling, which means that it inhibits the activity of TGF-β proteins, thereby preventing them from promoting cell growth and proliferation.

SMAD1 is composed of an N-terminal transmembrane domain, a single transmembrane domain, and a C-terminal protein domain. The transmembrane domain is responsible for the protein's stability and functions as an receptor for various signaling molecules, including TGF-β. The single transmembrane domain contains the protein's active site, which is involved in the formation of the protein's alpha-helices, which are important for protein-protein interactions. The C-terminal protein domain contains the protein's tryptophan residues, which are involved in the formation of the protein's alpha-helices and contribute to protein stability.

SMAD1's function in TGF-β signaling is dependent on its N-terminal transmembrane domain, which contains the protein's TGF-β receptor. TGF-β receptors are a family of transmembrane proteins that play a critical role in cell signaling. They are involved in the regulation of cell growth, differentiation, and survival, and are often dysregulated in many diseases. The TGF-β receptor is a key target for SMAD1, as it is the protein that SMAD1 binds to and inhibits the activity of.

SMAD1's Interaction with TGF-β

SMAD1's function in TGF-β signaling is dependent on its interaction with the TGF-β receptor. The TGF-β receptor is a transmembrane protein that is involved in the regulation of cell growth, differentiation, and survival. It is composed of two transmembrane subunits, which are connected by a intracellular loop. The TGF-β receptor is involved in the regulation of cell proliferation, differentiation, and survival by promoting the production of growth factors and inhibiting the production of growth inhibitors.

SMAD1 plays a critical role in the regulation of TGF-β signaling by binding to the TGF-β receptor and inhibiting its activity. This interaction between SMAD1 and the TGF-β receptor is dependent on the protein's N-terminal transmembrane domain. The N-terminal transmembrane domain of SMAD1 contains a protein-protein interaction (PPI) domain that is involved in the formation of the protein's alpha-helices. This interaction between SMAD1 and the TGF-β receptor is critical for the regulation of TGF-β signaling by SMAD1.

SMAD1's Role in Cancer

SMAD1's role in cancer is well established. It is involved in the regulation of cell growth, differentiation, and survival, and is often dysregulated in many types of cancer. Many studies have shown that SMAD1 is involved in the regulation of cancer cell growth, and that its dysregulation is associated with cancer progression.

SMAD1's role in cancer is related to its interaction with the TGF-β receptor. As mentioned earlier, the TGF-β receptor is involved in the regulation of cancer cell growth, and is often dysregulated in many types of cancer. The interaction between SMAD1 and the TGF-β receptor is

Protein Name: SMAD Family Member 1

Functions: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression

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•   general information;
•   protein structure and compound binding;
•   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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