Journal of Cancer Prevention

eISSN 2288-3657
pISSN 2288-3649

Cited by CrossRef (19)

  1. Ayon Chakraborty, Rajesh Ghosh, Ashis Biswas. Interaction of constituents of MDT regimen for leprosy with Mycobacterium leprae HSP18: impact on its structure and function. The FEBS Journal 2022;289:832
    https://doi.org/10.1111/febs.16212
  2. Wei Hou, Bo Liu, Hongtao Xu. Celastrol: Progresses in structure-modifications, structure-activity relationships, pharmacology and toxicology. European Journal of Medicinal Chemistry 2020;189:112081
    https://doi.org/10.1016/j.ejmech.2020.112081
  3. Ramona Schulz-Heddergott, Ute Moll. Gain-of-Function (GOF) Mutant p53 as Actionable Therapeutic Target. Cancers 2018;10:188
    https://doi.org/10.3390/cancers10060188
  4. Rosa Pennisi, Paolo Ascenzi, Alessandra Di Masi. Hsp90: A New Player in DNA Repair?. Biomolecules 2015;5:2589
    https://doi.org/10.3390/biom5042589
  5. Sayan Dutta Gupta, Manish Kumar Bommaka, Anindita Banerjee. Inhibiting protein-protein interactions of Hsp90 as a novel approach for targeting cancer. European Journal of Medicinal Chemistry 2019;178:48
    https://doi.org/10.1016/j.ejmech.2019.05.073
  6. Qiuyue Zhang, Ling Yan, Yuxuan Zhang, Lixiao Zhang, Jia Yu, Qidong You, Lei Wang. Rational Design of Peptide Inhibitors Targeting HSP90–CDC37 Protein–Protein Interaction. Future Med. Chem. 2024;16:125
    https://doi.org/10.4155/fmc-2023-0320
  7. Kiyun Park, Ihn-Sil Kwak. Disrupting effects of antibiotic sulfathiazole on developmental process during sensitive life-cycle stage of Chironomus riparius. Chemosphere 2018;190:25
    https://doi.org/10.1016/j.chemosphere.2017.09.118
  8. Lei Wang, Li Li, Wei-Tao Fu, Zheng-Yu Jiang, Qi-Dong You, Xiao-Li Xu. Optimization and bioevaluation of Cdc37-derived peptides: An insight into Hsp90-Cdc37 protein-protein interaction modulators. Bioorganic & Medicinal Chemistry 2017;25:233
    https://doi.org/10.1016/j.bmc.2016.10.028
  9. Sayan Dutta Gupta, Manish Kumar Bommaka, Gisela I. Mazaira, Mario D. Galigniana, Chavali Venkata Satya Subrahmanyam, Naryanasamy Lachmana Gowrishankar, Nulgumnalli Manjunathaiah Raghavendra. Molecular docking study, synthesis and biological evaluation of Mannich bases as Hsp90 inhibitors. International Journal of Biological Macromolecules 2015;80:253
    https://doi.org/10.1016/j.ijbiomac.2015.06.039
  10. Xianglin Shi, William F. Kiesman, Donald G. Walker. Comprehensive Accounts of Pharmaceutical Research and Development: From Discovery to Late-Stage Process Development Volume 1. 2015.
    https://doi.org/10.1021/bk-2016-1239.ch003
  11. Chia-Lung Tsai, Angel Chao, Shih-Ming Jung, Chi-Neu Tsai, Chiao-Yun Lin, Shun-Hua Chen, Shih-Che Sue, Tzu-Hao Wang, Hsin-Shih Wang, Chyong-Huey Lai. Stress-induced phosphoprotein-1 maintains the stability of JAK2 in cancer cells. Oncotarget 2016;7:50548
    https://doi.org/10.18632/oncotarget.10500
  12. Golnaz Bahramali, Bahram Goliaei, Zarrin Minuchehr, Sayed-Amir Marashi. A network biology approach to understanding the importance of chameleon proteins in human physiology and pathology. Amino Acids 2017;49:303
    https://doi.org/10.1007/s00726-016-2361-6
  13. Nausheen Joondan, Sabina J. Laulloo, Prakashanand Caumul, Prashant S. Kharkar. Antioxidant, Antidiabetic and Anticancer Activities of L-Phenylalanine and L-Tyrosine Ester Surfactants: In Vitro and In Silico Studies of their Interactions with Macromolecules as Plausible Mode of Action for their Biological Properties. CBC 2020;15:610
    https://doi.org/10.2174/1573407214666180829125309
  14. Megan Egbert, Adrian Whitty, György M. Keserű, Sandor Vajda. Why Some Targets Benefit from beyond Rule of Five Drugs. J. Med. Chem. 2019;62:10005
    https://doi.org/10.1021/acs.jmedchem.8b01732
  15. Chao YANG, Zhang-Feng ZHONG, Sheng-Peng WANG, Chi-Teng VONG, Bin YU, Yi-Tao WANG. HIF-1: structure, biology and natural modulators. Chinese Journal of Natural Medicines 2021;19:521
    https://doi.org/10.1016/S1875-5364(21)60051-1
  16. Fen Jiang, Hui-Jie Wang, Qi-Chao Bao, Lei Wang, Yu-Hui Jin, Qiong Zhang, Di Jiang, Qi-Dong You, Xiao-Li Xu. Optimization and biological evaluation of celastrol derivatives as Hsp90–Cdc37 interaction disruptors with improved druglike properties. Bioorganic & Medicinal Chemistry 2016;24:5431
    https://doi.org/10.1016/j.bmc.2016.08.070
  17. Wenqian Wang, Yang Liu, Zhixin Zhao, Chengying Xie, Yongping Xu, Youhong Hu, Haitian Quan, Liguang Lou. Y‐632 inhibits heat shock protein 90 (Hsp90) function by disrupting the interaction between Hsp90 and Hsp70/Hsp90 organizing protein, and exerts antitumor activity in vitro and in vivo. Cancer Science 2016;107:782
    https://doi.org/10.1111/cas.12934
  18. Xin Xie, Nan Zhang, Xiang Li, He Huang, Cheng Peng, Wei Huang, Leonard J. Foster, Gu He, Bo Han. Small-molecule dual inhibitors targeting heat shock protein 90 for cancer targeted therapy. Bioorganic Chemistry 2023;139:106721
    https://doi.org/10.1016/j.bioorg.2023.106721
  19. Young Ho Seo. Organelle-specific Hsp90 inhibitors. Arch. Pharm. Res. 2015;38:1582
    https://doi.org/10.1007/s12272-015-0636-1
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