CHORDC1: A Potential Drug Target for TGF-β and NF-kappa-B (G26973)

Target Name: CHORDC1

NCBI ID: G26973

CHORDC1

CHORDC1: A Potential Drug Target for TGF-β and NF-kappa-B

CHORDC1, also known as Morgana, is a protein that is expressed in various tissues of the human body, including the brain, heart, liver, and kidneys. It is a key regulator of cell growth and differentiation, and is involved in the development and maintenance of tissues. In recent years, researchers have become interested in CHORDC1 as a potential drug target or biomarker, due to its unique structure and biology.

The Structure of CHORDC1

CHORDC1 is a transmembrane protein that consists of four domains: an extracellular domain, a transmembrane domain, an intracellular domain, and a C-terminal domain. The extracellular domain is involved in the protein's ability to interact with other cells and tissues, while the transmembrane domain is responsible for the protein's ability to span the cell membrane and interact with intracellular signaling pathways. The intracellular domain is involved in the protein's ability to interact with various intracellular signaling pathways, and the C-terminal domain is involved in the protein's ability to interact with other proteins.

CHORDC1's unique structure allows it to play a unique role in the regulation of cell growth and differentiation. It is able to interact with various signaling pathways, including the TGF-β pathway, which is involved in the regulation of cell growth and differentiation. This interaction between CHORDC1 and TGF-β allows the protein to regulate the growth and differentiation of various tissues, including muscles, bones, and organs.

CHORDC1's ability to interact with TGF-β also makes it a potential drug target. TGF-β is a potent signaling pathway that is involved in the regulation of cell growth, differentiation, and survival. Activating TGF-β can lead to the formation of various diseases, including cancer, neurodegenerative diseases, and developmental disorders. By targeting CHORDC1, researchers may be able to inhibit the activity of TGF-β and its negative effects on various tissues.

CHORDC1's Interaction with NF-kappa-B

NF-kappa-B is a signaling pathway that is involved in the regulation of inflammation, pain, and other cellular processes. CHORDC1 has been shown to interact with NF-kappa-B, which allows it to participate in the regulation of various cellular processes. This interaction between CHORDC1 and NF-kappa-B also makes it a potential biomarker for various diseases, including cancer.

CHORDC1's interaction with NF-kappa-B allows it to contribute to the regulation of cellular processes that are involved in the development and progression of cancer. For example, CHORDC1 has been shown to play a role in the regulation of cell cycle progression, which is a critical step in the development of cancer. Additionally, CHORDC1 has been shown to contribute to the regulation of angiogenesis, which is the process by which new blood vessels are formed. This contribution to angiogenesis may contribute to the development of various diseases, including cancer.

CHORDC1's Interaction with PDGF

PDGF is a signaling pathway that is involved in the regulation of cell growth, differentiation, and survival. CHORDC1 has been shown to interact with PDGF, which allows it to contribute to the regulation of various cellular processes. This interaction between CHORDC1 and PDGF also makes it a potential biomarker for various diseases, including cancer.

CHORDC1's interaction with PDGF allows it to contribute to the regulation of cellular processes that are involved in the development and progression of cancer. For example, CHORDC1 has been shown to play a role in the regulation of cell survival and angiogenesis, which are critical steps in

Protein Name: Cysteine And Histidine Rich Domain Containing 1

Functions: Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2 (PubMed:20230755). Proposed to act as co-chaperone for HSP90 (PubMed:20230755). May play a role in the regulation of NOD1 via a HSP90 chaperone complex (PubMed:20230755). In vitro, has intrinsic chaperone activity (PubMed:20230755). This function may be achieved by inhibiting association of ROCK2 with NPM1 (PubMed:20230755). Plays a role in ensuring the localization of the tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures the subsequent regulation of EGFR activity and EGF-induced actin cytoskeleton remodeling (PubMed:32053105). Involved in stress response (PubMed:20230755). Prevents tumorigenesis (PubMed:20230755)

The "CHORDC1 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 CHORDC1 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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