Refolding and structural characterization of the human p53 tumor suppressor protein (Q74189456)

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9 November 2019

title

Refolding and structural characterization of the human p53 tumor suppressor protein (English)

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9 November 2019

author name string

Stefan Bell

series ordinal

1

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9 November 2019

Silke Hansen

series ordinal

2

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9 November 2019

Johannes Buchner

series ordinal

3

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9 November 2019

publication date

1 May 2002

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9 November 2019

published in

Biophysical Chemistry

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9 November 2019

volume

96

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9 November 2019

issue

2-3

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9 November 2019

page(s)

243-257

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p53, the cellular gatekeeper for growth and division

9 November 2019

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Hot-spot mutants of p53 core domain evince characteristic local structural changes.

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Definition of a consensus binding site for p53

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Conformational shifts propagate from the oligomerization domain of p53 to its tetrameric DNA binding domain and restore DNA binding to select p53 mutants.

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Refined solution structure of the oligomerization domain of the tumour suppressor p53

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Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms

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Thermodynamic analysis of the structural stability of the tetrameric oligomerization domain of p53 tumor suppressor

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Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain

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7 January 2021

Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

Transactivation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATA-binding protein

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7 January 2021

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Cell biology. The importance of being unfolded.

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Identifiers

DOI

1 reference

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9 November 2019

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