Cisd3-KO 基因敲除小鼠

1. Li, Yanchun, Wang, Xin, Huang, Zhihui, Tong, Xiangmin, Wang, Ying. 2021. CISD3 inhibition drives cystine-deprivation induced ferroptosis. In Cell death & disease, 12, 839. doi:10.1038/s41419-021-04128-2. https://pubmed.ncbi.nlm.nih.gov/34497268/

2. Li, Jie, Yang, Han, Qi, Yixin, He, Tianzhen, Wang, Ke. 2024. CISD3 is a prognostic biomarker and therapeutic target in pan-cancer. In Scientific reports, 14, 23494. doi:10.1038/s41598-024-74247-1. https://pubmed.ncbi.nlm.nih.gov/39379442/

3. Munir, Abdur-Rehman, Baig, Saad Ilyas, Razzaq, Muhammad Asif, Ali, Yasir, Azam, Syed Muhammad Abdullah. 2024. A novel (-)-(2S)-7,4'-dihydroxyflavanone compound for treating age-related diabetes mellitus through immunoinformatics-guided activation of CISD3. In Biogerontology, 26, 5. doi:10.1007/s10522-024-10147-1. https://pubmed.ncbi.nlm.nih.gov/39470889/

4. King, Skylar D, Gray, Chipo F, Song, Luhua, Mittler, Ron, Padilla, Pamela A. 2018. The cisd gene family regulates physiological germline apoptosis through ced-13 and the canonical cell death pathway in Caenorhabditis elegans. In Cell death and differentiation, 26, 162-178. doi:10.1038/s41418-018-0108-5. https://pubmed.ncbi.nlm.nih.gov/29666474/

5. Pérez-Ramírez, Monserrat, Hernández-Jiménez, Alejo Justino, Guerrero-Guerrero, Armando, Salamanca-Gómez, Fabio Abdel, García-Hernández, Normand. 2016. Genomics and epigenetics: A study of ependymomas in pediatric patients. In Clinical neurology and neurosurgery, 144, 53-8. doi:10.1016/j.clineuro.2016.02.041. https://pubmed.ncbi.nlm.nih.gov/26971296/

6. She, Jiajie, Su, Danna, Diao, Ruiying, Wang, Liping. 2022. A Joint Model of Random Forest and Artificial Neural Network for the Diagnosis of Endometriosis. In Frontiers in genetics, 13, 848116. doi:10.3389/fgene.2022.848116. https://pubmed.ncbi.nlm.nih.gov/35350240/

7. Inupakutika, Madhuri A, Sengupta, Soham, Nechushtai, Rachel, Padilla, Pamela, Mittler, Ron. 2017. Phylogenetic analysis of eukaryotic NEET proteins uncovers a link between a key gene duplication event and the evolution of vertebrates. In Scientific reports, 7, 42571. doi:10.1038/srep42571. https://pubmed.ncbi.nlm.nih.gov/28205535/

8. Karmi, Ola, Marjault, Henri-Baptiste, Pesce, Luca, Mittler, Ron, Nechushtai, Rachel. 2018. The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease. In Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 23, 599-612. doi:10.1007/s00775-018-1538-8. https://pubmed.ncbi.nlm.nih.gov/29435647/

9. Lipper, Colin H, Karmi, Ola, Sohn, Yang Sung, Onuchic, José N, Jennings, Patricia A. 2017. Structure of the human monomeric NEET protein MiNT and its role in regulating iron and reactive oxygen species in cancer cells. In Proceedings of the National Academy of Sciences of the United States of America, 115, 272-277. doi:10.1073/pnas.1715842115. https://pubmed.ncbi.nlm.nih.gov/29259115/