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The secondary structure of the ets domain of human Fli-1 resembles that of the helix-turn-helix DNA-binding motif of the Escherichia coli catabolite gene activator protein.

Data up to Jan 2025

Published1994
Citations49
References20

Total Citations Per Year

Abstract

References (20)

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1993 • 739 citations

Interaction of murine ets-1 with GGA-binding sites establishes the ETS domain as a new DNA-binding motif.

1992 • 381 citations

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1991 • 330 citations

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1994 • 269 citations

Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core.

1992 • 241 citations

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1964 • 189 citations

Evolutionarily conserved Ets family members display distinct DNA binding specificities.

1992 • 175 citations

Elk-1 protein domains required for direct and SRF-assisted DNA-binding

1992 • 137 citations

The FLI-1 and chimeric EWS-FLI-1 oncoproteins display similar DNA binding specificities.

1994 • 132 citations

NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors

1994 • 104 citations

A single amino-acid substitution in the Ets domain alters core DNA binding specificity of Ets1 to that of the related transcription factors Elf1 and E74

1993 • 55 citations

Structural inferences of the ETS1 DNA-binding domain determined by mutational analysis.

1994 • 21 citations

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The secondary structure of the ets domain of human Fli-1 resembles that of the… (1994) – Proceedings of the National Academy of Sciences | Metascience Observatory Explorer