Small molecule restoration of wildtype structure and function of mutant p53 using a novel zinc-metallochaperone based mechanism
Oncotarget2014Vol. 5(19), pp. 8879–8892
Citations Over TimeTop 10% of 2014 papers
Xin Yu, Adam R. Blanden, Sumana Narayanan, Lalithapriya Jayakumar, David Lubin, David J. Augeri, S. David Kimball, Stewart N. Loh, Darren R. Carpizo
Abstract
We have elucidated a novel mechanism to restore wild-type structure/function to mutant p53 using small molecules functioning as zinc-metallochaperones. The pharmacologic delivery of a metal ion to restore proper folding of a mutant protein is unique to medicinal chemistry and represents a new pathway to drug mutant p53.
Related Papers
- → Cotranslation of activated mutant p53 with wild type drives the wild-type p53 protein into the mutant conformation(1991)618 cited
- → Crystallographic structure determination of B10 mutants ofVitreoscillahemoglobin: role of Tyr29 (B10) in the structure of the ligand-binding site(2013)7 cited
- → Acid alpha-glucosidase deficiency: Identification and expression of a missense mutation (S529V) in a Japanese adult phenotype(1996)14 cited
- → Acid alpha-glucosidase deficiency: identification and expression of a missense mutation (S529V) in a Japanese adult phenotype(1996)2 cited
- Photosynthetic and Chlorophyll Fluorescence Characteristics of Xantha Type Rice Mutant(2007)