Target Name: DDB2
NCBI ID: G1643
Review Report on DDB2 Target / Biomarker Content of Review Report on DDB2 Target / Biomarker
DDB2
Other Name(s): Damage specific DNA binding protein 2, transcript variant WT | DDBb | damage specific DNA binding protein 2 | DNA damage-binding protein 2 (isoform WT) | DNA damage-binding protein 2 | UV-damaged DNA-binding protein 2 | DDB2_HUMAN | DDB2 variant WT | Damage-specific DNA-binding protein 2 | UV-DDB2 | UV-DDB 2 | xeroderma pigmentosum group E protein | DDBB | XPE | DDB p48 subunit | damage-specific DNA binding protein 2, 48kDa

The Importance of DDB2 as a Drug Target and Biomarker

In today's era of advanced medical research and precision medicine, drug targets and biomarkers hold immense significance. These molecules play a critical role in the development of novel therapeutic interventions and provide insights into the diagnosis, prognosis, and monitoring of various diseases. One such molecule of great interest is DDB2, also known as damaged DNA-binding protein 2.

The Role of DDB2 in DNA Repair Pathways

DDB2 is part of the damaged DNA-binding protein complex, which aids in the recognition and repair of DNA damage. DNA damage can occur due to numerous factors, including exposure to environmental toxins, ultraviolet radiation from the sun, or errors during DNA replication. If left unrepaired, DNA damage can lead to mutations, genomic instability, and the development of various diseases, including cancer.

DDB2 plays a crucial role in initiating the nucleotide excision repair (NER) pathway, which is responsible for correcting DNA damage caused by ultraviolet radiation. It recognizes and binds to DNA lesions and recruits other proteins necessary for the repair process. The NER pathway ensures the integrity of DNA and prevents the accumulation of mutations that could lead to malignant transformation.

DDB2 as a Potential Drug Target

Given its critical role in DNA repair, DDB2 has gained considerable attention as a potential drug target. Modulating DDB2 activity could have therapeutic implications, particularly in cancer treatment. In some cancer types, the expression of DDB2 is downregulated or inhibited, leading to impaired DNA repair mechanisms and increased genomic instability. Exploiting this vulnerability could help develop therapies that selectively target cancer cells while sparing healthy cells.

Scientists are actively investigating various approaches to target DDB2 in cancer therapy. One avenue of research involves developing small molecule inhibitors that can bind to DDB2 and disrupt its function. By inhibiting DDB2, these compounds aim to prevent efficient DNA repair in cancer cells, leading to their eventual demise. Although still in the early stages, these inhibitors show promising results in preclinical studies, warranting further investigation and development.

DDB2 as a Biomarker for Cancer Diagnosis and Prognosis

Beyond its potential as a drug target, DDB2 has also emerged as a valuable biomarker for cancer diagnosis and prognosis. Biomarkers are characteristics or molecules that can be measured and evaluated to provide information about the presence, severity, or progression of a disease. By assessing DDB2 levels, medical professionals can gain insight into the DNA repair capacity of cancer cells and predict the clinical outcomes for patients.

Numerous studies have reported alterations in DDB2 expression in various cancers. For example, decreased DDB2 expression correlates with poor prognosis in certain types of cancer, including melanoma, ovarian, and lung cancer. In contrast, high expression levels of DDB2 have been associated with favorable outcomes in breast and gastric cancers. This suggests that DDB2 could serve as a valuable predictive biomarker for patient stratification and treatment selection.

Additionally, DDB2 levels could potentially be used to monitor treatment response and disease progression. Serial measurements of DDB2 expression in cancer patients undergoing therapy could help assess the effectiveness of treatment and identify resistance development. Such information would allow for timely adjustments in treatment regimens, potentially improving patient outcomes and reducing unnecessary adverse effects.

The Future of DDB2 Research

As our understanding of DDB2 continues to expand, further research is needed to uncover its full therapeutic potential and validate its utility as a biomarker. Clinical trials evaluating DDB2-targeted therapies are essential to determine their safety, efficacy, and ideal patient populations. Furthermore, large-scale studies correlating DDB2 expression with clinical outcomes across diverse cancer types would solidify its role as a reliable biomarker.

In conclusion, DDB2 holds immense promise as both a drug target and biomarker. Its crucial role in DNA repair pathways makes it an attractive target for developing novel cancer therapies. Moreover, its association with prognosis and treatment response makes it a potentially valuable biomarker for patient management. Continued research in this field will undoubtedly contribute to advancing personalized medicine and bringing us closer to more effective and tailored treatments for cancer and other diseases.

Protein Name: Damage Specific DNA Binding Protein 2

Functions: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:10882109, PubMed:11278856, PubMed:11705987, PubMed:9892649, PubMed:12732143, PubMed:15882621, PubMed:16473935, PubMed:18593899, PubMed:32789493). Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:10882109, PubMed:11278856, PubMed:11705987, PubMed:16260596, PubMed:12944386, PubMed:14751237, PubMed:32789493). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:10882109, PubMed:11278856, PubMed:11705987, PubMed:16260596, PubMed:12944386). Also functions as the substrate recognition module for the DCX (DDB2-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB2-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1) (PubMed:12732143, PubMed:15882621, PubMed:16473935, PubMed:18593899, PubMed:26572825). The DDB2-CUL4-ROC1 complex may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage (PubMed:16678110, PubMed:16473935). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:16678110, PubMed:16473935). The DDB2-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed:15882621). The DDB2-CUL4-ROC1 complex also ubiquitinates KAT7/HBO1 in response to DNA damage, leading to its degradation: recognizes KAT7/HBO1 following phosphorylation by ATR (PubMed:26572825)

The "DDB2 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 DDB2 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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