Interaction with p53 enhances binding of cisplatin-modified DNA by high mobility group 1 protein (Q28139455)

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H Izumi

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G Nagatani

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T Ise

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M Nomoto

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Y Iwamoto

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K Kohno

Journal of Biological Chemistry

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language of work or name

English

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publication date

9 March 2001

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published in

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volume

276

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issue

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page(s)

7534-40

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cites work

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DNA sequence context and protein composition modulate HMG-domain protein recognition of cisplatin-modified DNA.

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Structure-specific binding of the two tandem HMG boxes of HMG1 to four-way junction DNA is mediated by the A domain.

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Regulation of the sequence-specific DNA binding function of p53 by protein kinase C and protein phosphatases

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Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain

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The DNA-bending protein HMG-1 enhances progesterone receptor binding to its target DNA sequences

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The single-stranded DNA end binding site of p53 coincides with the C-terminal regulatory region.

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Steroid hormones induce HMG1 overexpression and sensitize breast cancer cells to cisplatin and carboplatin

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Identifiers

DOI

10.1074/JBC.M008143200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11106654

1 reference

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