DAPK2: A Potential Drug Target and Biomarker for Death-Associated Protein Kinase 2

Target Name: DAPK2

NCBI ID: G23604

DAPK2

DAPK2: A Potential Drug Target and Biomarker for Death-Associated Protein Kinase 2

Death-associated protein kinase 2 (DAPK2) is a protein that plays a crucial role in the regulation of cell survival and proliferation. Its function is highly conserved across various species, and it has been implicated in various cellular processes, including cell death, apoptosis, and autophagy. DAPK2 has also been implicated in the development of various diseases, including neurodegenerative disorders, cancer, and autoimmune diseases. As a result, targeting DAPK2 has become an attractive research topic in recent years.

DAPK2: Structure and Function

DAPK2 is a protein that contains 11 known amino acid residues and 18 putative amino acid residues. It is a member of the serine/threonine protein kinase (STP) family and is characterized by a catalytic core and a variable catalytic region. The catalytic core of DAPK2 consists of a nucleotide-binding domain (NBD) and a kinase domain (KD). The NBD is responsible for binding nucleotides, while the KD is responsible for the catalytic activity of the protein.

The function of DAPK2 is highly conserved across various species. It has been shown to play a role in various cellular processes, including cell survival, apoptosis, and autophagy. DAPK2 has been shown to promote the formation of a mitochondrial stress response, which is associated with the development of neurodegenerative disorders. DAPK2 has also been shown to play a role in the regulation of cellular proliferation and the establishment of tissue repair following injury or inflammation.

DAPK2 as a Drug Target

DAPK2 has been identified as a potential drug target due to its involvement in various diseases. Its function in cell survival and proliferation makes it an attractive target for small molecules that can inhibit its activity. Several studies have shown that inhibitors of DAPK2 have been effective in treating neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease.

One of the compounds that has been shown to be an effective inhibitor of DAPK2 is benzodiazepine (BZP). BZP is a anxiolytic and anticonvulsant drug that has been used to treat various neurological disorders. Several studies have shown that BZP is a potent inhibitor of DAPK2 and has been shown to protect against neurodegenerative disorders in animal models.

Another compound that has been shown to be an effective inhibitor of DAPK2 is curcumin (CUR), a compound that is derived from the turmeric plant. CUR has been shown to have neuroprotective properties and to inhibit the activity of DAPK2. Several studies have shown that CUR is effective in treating various neurological disorders, including neurodegenerative disorders.

DAPK2 as a Biomarker

DAPK2 has also been shown to be a potential biomarker for various diseases. Its function in the regulation of cell survival and proliferation makes it an attractive target for biomarkers that can be used to diagnose and monitor diseases.

One of the biomarkers that has been shown to be sensitive to DAPK2 is the protein p53. P53 is a tumor suppressor protein that is involved in the regulation of cell growth and apoptosis. Several studies have shown that DAPK2 can interact with p53 and that changes in DAPK2 activity can affect p53 function. These interactions between DAPK2 and p53 make DAPK2 a potential biomarker for various diseases.

Another biomarker that has been shown to be sensitive to DAPK2 is the gene expression profile. DAPK2 has

Protein Name: Death Associated Protein Kinase 2

Functions: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell death signals, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Acts as a mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation (PubMed:17347302). Regulates granulocytic motility by controlling cell spreading and polarization (PubMed:24163421)

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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;
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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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