Title : Identification of two reactive cysteine residues in the tumor suppressor protein p53 using top-down FTICR mass spectrometry.

Pub. Date : 2011 May

PMID : 21472523






5 Functional Relationships(s)
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1 Identification of two reactive cysteine residues in the tumor suppressor protein p53 using top-down FTICR mass spectrometry. Cysteine tumor protein p53 Homo sapiens
2 The discovery of cysteine-targeting compounds that cause re-activation of mutant p53 and the death of tumor cells in vivo has emphasized the functional importance of p53 thiols. Cysteine tumor protein p53 Homo sapiens
3 The discovery of cysteine-targeting compounds that cause re-activation of mutant p53 and the death of tumor cells in vivo has emphasized the functional importance of p53 thiols. Cysteine tumor protein p53 Homo sapiens
4 Using a combination of top-down and middle-down FTICR mass spectrometry, we show that of the 10 Cys residues in the core domain of wild-type p53, Cys182 and Cys277 exhibit a remarkable preference for modification by the alkylating reagent N-ethylmaleimide. Cysteine tumor protein p53 Homo sapiens
5 Further alkylation of p53 beyond Cys182 and Cys277 was found to trigger co-operative modification of the remaining seven Cys residues and protein unfolding. Cysteine tumor protein p53 Homo sapiens