The cavity in the hydrophobic core of Myb DNA-binding domain is reserved for DNA recognition and trans-activation (Q70907200)

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14 October 2019

title

The cavity in the hydrophobic core of Myb DNA-binding domain is reserved for DNA recognition and trans-activation (English)

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14 October 2019

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14 October 2019

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14 October 2019

Ogata K

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14 October 2019

Kanei-Ishii C

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14 October 2019

Sasaki M

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14 October 2019

Hatanaka H

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14 October 2019

Nagadoi A

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14 October 2019

Enari M

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14 October 2019

Nakamura H

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14 October 2019

Sarai A

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14 October 2019

publication date

1 February 1996

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Nature structural biology

14 October 2019

published in

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14 October 2019

volume

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issue

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page(s)

178-187

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Study of protein dynamics by X-ray diffraction

14 October 2019

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Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect

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Functional analysis of c-Myb protein in T-lymphocytic cell lines shows that it trans-activates the c-myc promoter

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Characterization of the backbone dynamics of an anti-digoxin antibody VL domain by inverse detected 1H-15N NMR: comparisons with X-ray data for the Fab.

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Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: applicati

31 March 2020

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Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional NMR spectroscopy

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Transactivation and transformation by Myb are negatively regulated by a leucine-zipper structure

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSB0296-178

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14 October 2019

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