(Q44924760)

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Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures

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Europe PubMed Central

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7 December 2017

Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures (English)

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Europe PubMed Central

PubMed publication ID

7 December 2017

Escherichia coli

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Chi YI

1

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7 December 2017

Yokota H

2

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7 December 2017

Kim SH

3

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7 December 2017

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1 September 1997

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7 December 2017

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7 December 2017

414

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7 December 2017

2

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7 December 2017

327-332

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7 December 2017

Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand

1 reference

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Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium.

1 reference

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Human growth hormone and extracellular domain of its receptor: crystal structure of the complex

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Global flexibility in a sensory receptor: a site-directed cross-linking approach.

1 reference

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Intrasubunit signal transduction by the aspartate chemoreceptor

1 reference

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Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo

1 reference

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21 January 2018

Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer.

1 reference

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21 January 2018

Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain.

1 reference

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21 January 2018

The fifth Datta Lecture. Structural similarities between the aspartate receptor of bacterial chemotaxis and the trp repressor of E. coli. Implications for transmembrane signaling

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2901027-2

21 January 2018

"Frozen" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors

1 reference

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21 January 2018

Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium.

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2901027-2

21 January 2018

AMoRe: an automated package for molecular replacement

1 reference

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

1 reference

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21 January 2018

Improved methods for building protein models in electron density maps and the location of errors in these models

1 reference

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21 January 2018

Attractant- and disulfide-induced conformational changes in the ligand binding domain of the chemotaxis aspartate receptor: a 19F NMR study

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2901027-2

21 January 2018

A model for transmembrane signalling by the aspartate receptor based on random-cassette mutagenesis and site-directed disulfide cross-linking.

1 reference

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21 January 2018

Molecular mechanism of transmembrane signaling by the aspartate receptor: a model

1 reference

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The crystal structure of trp aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinity

1 reference

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21 January 2018

The three-dimensional structure of trp repressor.

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2901027-2

21 January 2018

Imitation of Escherichia coli aspartate receptor signaling in engineered dimers of the cytoplasmic domain

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2901027-2

21 January 2018

Role of alpha-helical coiled-coil interactions in receptor dimerization, signaling, and adaptation during bacterial chemotaxis

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2901027-2

21 January 2018

Transmembrane signalling and the aspartate receptor

1 reference

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21 January 2018

The CCP4 suite: programs for protein crystallography

1 reference

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7 January 2021

Identifiers

10.1016/S0014-5793(97)01027-2

1 reference

Europe PubMed Central

PubMed publication ID

7 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

7 December 2017

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