Title : Reversible amyloid formation by the p53 tetramerization domain and a cancer-associated mutant.

Pub. Date : 2003 Mar 28

PMID : 12634062






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Circular dichroism, Fourier transform infrared spectroscopy and staining with Congo red and thioflavin T showed that p53tet-wt and p53tet-R337H adopt an alternative beta-sheet conformation (p53tet-wt-beta and p53tet-R337H-beta, respectively), characteristic of amyloid-like fibrils, when incubated at pH 4.0 and elevated temperatures. thioflavin T tumor protein p53 Homo sapiens
2 Circular dichroism, Fourier transform infrared spectroscopy and staining with Congo red and thioflavin T showed that p53tet-wt and p53tet-R337H adopt an alternative beta-sheet conformation (p53tet-wt-beta and p53tet-R337H-beta, respectively), characteristic of amyloid-like fibrils, when incubated at pH 4.0 and elevated temperatures. thioflavin T tumor protein p53 Homo sapiens