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Cited by 64

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Thiosemicarbazones Functioning as Zinc Metallochaperones to Reactivate Mutant p53

Yu, Xin, Blanden, Adam, Tsang, Ashley T., Zaman, Saif, Liu, Yue, Gilleran, John, Bencivenga, Anthony F., Kimball, S. David, Loh, Stewart N., Carpizo, Darren R.·2017·Molecular Pharmacology
DOI 10.1124/mol.116.107409
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Research works printed but not linked: 28

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  3. Blanden, 2015, Reactivating mutant p53 using small molecules as zinc metallochaperones: awakening a sleeping giant in cancer, Drug Discov Today, 20, 1391, 10.1016/j.drudis.2015.07.006 · DOI
  4. Blanden, 2015, Synthetic metallochaperone ZMC1 rescues mutant p53 conformation by transporting zinc into cells as an ionophore, Mol Pharmacol, 87, 825, 10.1124/mol.114.097550 · DOI · Paper page
  5. Bozym, 2006, Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor, ACS Chem Biol, 1, 103, 10.1021/cb500043a · DOI · Paper page
  6. Butler, 2003, Structure, function, and aggregation of the zinc-free form of the p53 DNA binding domain, Biochemistry, 42, 2396, 10.1021/bi026635n · DOI · Paper page
  7. Butler, 2007, Zn(2+)-dependent misfolding of the p53 DNA binding domain, Biochemistry, 46, 2630, 10.1021/bi062106y · DOI
  8. Finch, 2000, Triapine (3-aminopyridine-2-carboxaldehyde- thiosemicarbazone): A potent inhibitor of ribonucleotide reductase activity with broad spectrum antitumor activity, Biochem Pharmacol, 59, 983, 10.1016/S0006-2952(99)00419-0 · DOI · Paper page
  9. Finch, 1999, Triapine (3-aminopyridine-2-carboxaldehyde thiosemicarbazone; 3-AP): an inhibitor of ribonucleotide reductase with antineoplastic activity, Adv Enzyme Regul, 39, 3, 10.1016/S0065-2571(98)00017-X · DOI · Paper page
  10. Franken, 2006, Clonogenic assay of cells in vitro, Nat Protoc, 1, 2315, 10.1038/nprot.2006.339 · DOI · Paper page
  11. Freed-Pastor, 2012, Mutant p53: one name, many proteins, Genes Dev, 26, 1268, 10.1101/gad.190678.112 · DOI · Paper page
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  14. Kunos, 2013, Radiochemotherapy plus 3-aminopyridine-2-carboxaldehyde thiosemicarbazone (3-AP, NSC #663249) in advanced-stage cervical and vaginal cancers, Gynecol Oncol, 130, 75, 10.1016/j.ygyno.2013.04.019 · DOI
  15. Lokshin, 2007, p53 and p73 display common and distinct requirements for sequence specific binding to DNA, Nucleic Acids Res, 35, 340, 10.1093/nar/gkl1047 · DOI
  16. Ma, 2008, A multicenter phase II trial of 3-aminopyridine-2-carboxaldehyde thiosemicarbazone (3-AP, Triapine) and gemcitabine in advanced non-small-cell lung cancer with pharmacokinetic evaluation using peripheral blood mononuclear cells, Invest New Drugs, 26, 169, 10.1007/s10637-007-9085-0 · DOI · Paper page
  17. Méplan, 2000, Metalloregulation of the tumor suppressor protein p53: zinc mediates the renaturation of p53 after exposure to metal chelators in vitro and in intact cells, Oncogene, 19, 5227, 10.1038/sj.onc.1203907 · DOI · Paper page
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  19. Popović-Bijelić, 2011, Ribonucleotide reductase inhibition by metal complexes of Triapine (3-aminopyridine-2-carboxaldehyde thiosemicarbazone): a combined experimental and theoretical study, J Inorg Biochem, 105, 1422, 10.1016/j.jinorgbio.2011.07.003 · DOI
  20. Richardson, 2006, Dipyridyl thiosemicarbazone chelators with potent and selective antitumor activity form iron complexes with redox activity, J Med Chem, 49, 6510, 10.1021/jm0606342 · DOI · Paper page
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  22. Stefani, 2015, Identification of differential anti-neoplastic activity of copper bis(thiosemicarbazones) that is mediated by intracellular reactive oxygen species generation and lysosomal membrane permeabilization, J Inorg Biochem, 152, 20, 10.1016/j.jinorgbio.2015.08.010 · DOI
  23. Thelander, 1983, Mechanism of inhibition of mammalian ribonucleotide reductase by the iron chelate of 1-formylisoquinoline thiosemicarbazone. Destruction of the tyrosine free radical of the enzyme in an oxygen-requiring reaction, J Biol Chem, 258, 4063, 10.1016/S0021-9258(18)32582-1 · DOI
  24. Yu, 2014, Small molecule restoration of wildtype structure and function of mutant p53 using a novel zinc-metallochaperone based mechanism, Oncotarget, 5, 8879, 10.18632/oncotarget.2432 · DOI · Paper page
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Cited by

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Metadata

Authors
Yu, X., Blanden, A., Tsang, A. T., Zaman, S., Liu, Y., Gilleran, J., Bencivenga, A. F., Kimball, S. D., Loh, S. N., & Carpizo, D. R.
Venue
Molecular Pharmacology
Publisher
Elsevier BV
Published
2017-06
Volume
91
Issue
6
Pages
567-575
ISSN
0026-895X
DOI
10.1124/mol.116.107409
Cited by
64
References
3
Language
en
Licence
  • www.elsevier.com/tdm/userlicense/1.0/ (tdm)
  • www.elsevier.com/legal/tdmrep-license (tdm)

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CoChat. (2026). Citation check: Thiosemicarbazones Functioning as Zinc Metallochaperones to Reactivate Mutant p53. https://app.cochat.ai/papers/10.1124/mol.116.107409
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Yu, X., Blanden, A., Tsang, A. T., Zaman, S., Liu, Y., Gilleran, J., Bencivenga, A. F., Kimball, S. D., Loh, S. N., & Carpizo, D. R. (2017). Thiosemicarbazones Functioning as Zinc Metallochaperones to Reactivate Mutant p53. Molecular Pharmacology. https://doi.org/10.1124/mol.116.107409

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.