A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex (Q27732614)

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English	A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex	scientific article

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scholarly article

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A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex (English)

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author name string

R Kodandapani

1

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F Pio

2

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C Z Ni

3

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G Piccialli

4

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M Klemsz

5

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S McKercher

6

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R A Maki

7

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K R Ely

8

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language of work or name

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publication date

4 April 1996

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380

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6573

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456-60

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The Ets family of transcription factors

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The ETS-domain: a new DNA-binding motif that recognizes a purine-rich core DNA sequence

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The macrophage and B cell-specific transcription factor PU.1 is related to the ets oncogene

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Co-crystallization of an ETS domain (PU.1) in complex with DNA. Engineering the length of both protein and oligonucleotide.

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Solution structure of the ets domain of Fli-1 when bound to DNA

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The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation

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Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees

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Crystal structure of globular domain of histone H5 and its implications for nucleosome binding

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Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5

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Crystal structure of the DNA binding domain of the heat shock transcription factor

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Refolding proteins by gel filtration chromatography.

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

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Resolution of phase ambiguity in macromolecular crystallography

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Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO

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Accurate bond and angle parameters for X-ray protein structure refinement

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Conformation of Polypeptides and Proteins

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The effect of mathematics and coordinate system on comparability and "dependencies" of nucleic acid structure parameters.

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Site-directed mutagenesis by overlap extension using the polymerase chain reaction

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Identifiers

10.1038/380456A0

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Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

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Springer Nature article ID

10.1038/380456a0

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