NSFL1C: A Potential Drug Target and Biomarker (G55968)

Target Name: NSFL1C

NCBI ID: G55968

NSFL1C

NSFL1C: A Potential Drug Target and Biomarker

The protein NSFL1C (NSFL1 cofactor p47) is a key regulator of the DNA damage response pathway in eukaryotic cells.NSFL1C functions as a cofactor for the protein DNA-protein binding protein p53, which plays a crucial role in detecting and repairing DNA damage.NSFL1C is also involved in the regulation of cell growth, apoptosis, and the response to environmental stressors.Given its involvement in multiple cellular processes, NSFL1C has potential as a drug target or biomarker.

NSFL1C: Structure and Function

The NSFL1C protein is approximately 40 kDa and consists of 250 amino acid residues.It has a characteristic Rossmann-fold structure that is unique among eukaryotic proteins.The protein is predominantly monomeric and can exist in two forms: a soluble form and a membrane-bound form.The soluble form of NSFL1C can interact with p53 and other DNA-protein binding proteins, while the membrane-bound form plays a role in regulating the DNA damage response pathway.

NSFL1C is regulated by several factors, including DNA double-strand breaks, UV radiation, and chemicals such as camptothecin and mitomycin.These regulations are essential for the survival of cells under stress.NSFL1C functions as a negative regulator of the DNA damage response pathway, which ensures that cells are able to repair DNA damage and recover from stressors.

NSFL1C and Cancer

The NSFL1C protein has been implicated in the development and progression of several types of cancer, including breast, ovarian, and colorectal cancers.Studies have shown that high levels of NSFL1C are associated with poor prognosis in cancer patients.NSFL1C has also been shown to promote the growth and survival of cancer cells, which may contribute to its role in cancer development.

NSFL1C as a Drug Target

The NSFL1C protein is a potential drug target due to its involvement in multiple cellular processes.NSFL1C functions as a cofactor for the DNA-protein binding protein p53, which plays a crucial role in detecting and repairing DNA damage.Given its involvement in the regulation of DNA damage, NSFL1C may be a good target for drugs that are designed to inhibit the activity of p53 or other DNA-protein binding proteins.

NSFL1C has also been shown to promote the growth and survival of cancer cells, which may make it an attractive target for drugs that are designed to inhibit its activity.Studies have shown that inhibitors of NSFL1C have the potential to inhibit the growth and survival of cancer cells.

NSFL1C as a Biomarker

The NSFL1C protein has been shown to be involved in the regulation of several cellular processes, including cell growth, apoptosis, and the response to environmental stressors.Given its involvement in these processes, NSFL1C may be a useful biomarker for the diagnosis and prognosis of several types of cancer.

NSFL1C has also been shown to be regulated by several factors, including DNA double-strand breaks, UV radiation, and chemicals such as camptothecin and mitomycin.These regulations are essential for the survival of cells under stress.Given its involvement in the regulation of cellular processes, NSFL1C may be a useful biomarker for the assessment of the effectiveness of cancer treatments.

Conclusion

In conclusion, the NSFL1C protein is a key regulator of the DNA damage response pathway in eukaryotic cells.NSFL1C has

Protein Name: NSFL1 Cofactor

Functions: Reduces the ATPase activity of VCP (By similarity). Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis (By similarity). May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro) (PubMed:15498563). Together with UBXN2B/p37, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase (PubMed:23649807). Also, regulates spindle orientation during mitosis (PubMed:23649807)

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