(Q27618787)

2

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Q He

3

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C O Pabo

4

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S J Lippard

Proteins that specifically recognize cisplatin-damaged DNA: a clue to anticancer activity of cisplatin

5

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language of work or name

English

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publication date

17 June 1999

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published in

Nature

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volume

399

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issue

6737

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page(s)

708-12

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cites work

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Cisplatin and DNA repair in cancer chemotherapy

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Cisplatin-DNA adducts inhibit ribosomal RNA synthesis by hijacking the transcription factor human upstream binding factor

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

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A single HMG domain in high-mobility group 1 protein binds to DNAs as small as 20 base pairs containing the major cisplatin adduct

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Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex

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Structural basis for DNA bending by the architectural transcription factor LEF-1

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The definition of generalized helicoidal parameters and of axis curvature for irregular nucleic acids

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NMR solution structure of a DNA dodecamer duplex containing a cis-diammineplatinum(II) d(GpG) intrastrand cross-link, the major adduct of the anticancer drug cisplatin

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Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy

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Backbone dynamics of the A-domain of HMG1 as studied by 15N NMR spectroscopy.

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DNA bending: the prevalence of kinkiness and the virtues of normality

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Structure and isomerization of an intrastrand cisplatin-cross-linked octamer DNA duplex by NMR analysis

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Differences in the DNA-Binding Properties of the Hmg-Box Domains of HMG1 and the Sex-Determining Factor SRY

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The SRY cantilever motif discriminates between sequence- and structure-specific DNA recognition: alanine mutagenesis of an HMG box.

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Structural transitions of a GG-platinated DNA duplex induced by pH, temperature and box A of high-mobility-group protein 1

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Structure prediction of a complex between the chromosomal protein HMG-D and DNA.

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Differences in DNA recognition and conformational change activity between boxes A and B in HMG2 protein

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Mutational analysis of the DNA binding domain A of chromosomal protein HMG1.

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Processing of X-ray diffraction data collected in oscillation mode

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[26] Screening for heavy-atom derivatives and obtaining accurate isomorphous differences.

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The CCP4 suite: programs for protein crystallography

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The HMG-1 box protein family: classification and functional relationships.

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