(Q27736290)

English

Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.3 A structure of an aspartate to lysine mutant at position 13 of CheY

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scholarly article

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Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.3 A structure of an aspartate to lysine mutant at position 13 of CheY (English)

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phosphorylation

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based on heuristic

inferred from title

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based on heuristic

inferred from title

author name string

M Jiang

1

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R B Bourret

2

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M I Simon

3

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K Volz

4

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language of work or name

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publication date

2 May 1997

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Journal of Biological Chemistry

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272

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18

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11850-5

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Communication modules in bacterial signaling proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Signal transduction schemes of bacteria

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Histidine and aspartate phosphorylation: two-component systems and the limits of homology

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors

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https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Sensory transduction in bacterial chemotaxis involves phosphotransfer between Che proteins.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Chemotaxis in Escherichia coli analysed by Three-dimensional Tracking

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https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

The Gradient-Sensing Mechanism in Bacterial Chemotaxis

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https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis

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https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Structural conservation in the CheY superfamily

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Divalent metal ion binding to the CheY protein and its significance to phosphotransfer in bacterial chemotaxis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.1-A structure of a threonine to isoleucine mutant at position 87 of CheY

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Phosphorylation assays for proteins of the two-component regulatory system controlling chemotaxis in Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

A pulsed diffusion technique for the growth of protein crystals for x-ray diffraction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Protein phosphorylation and bacterial chemotaxis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Effects of phosphorylation, Mg2+, and conformation of the chemotaxis protein CheY on its binding to the flagellar switch protein FliM.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Bioassay for carcinogenicity of rotenone in female Wistar rats.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Regulation of an enzyme by phosphorylation at the active site

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Bivalent-metal binding to CheY protein. Effect on protein conformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Bacterial chemotaxis signaling complexes: formation of a CheA/CheW complex enhances autophosphorylation and affinity for CheY.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonance

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Expression of CheA fragments which define domains encoding kinase, phosphotransfer, and CheY binding activities

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Phosphorylation-dependent binding of the chemotaxis signal molecule CheY to its phosphatase, CheZ.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Oligomerization of the phosphatase CheZ upon interaction with the phosphorylated form of CheY. The signal protein of bacterial chemotaxis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Mutants with defective phosphatase activity show no phosphorylation-dependent oligomerization of CheZ. The phosphatase of bacterial chemotaxis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Mutations leading to altered CheA binding cluster on a face of CheY.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

The role of a signaling protein in bacterial sensing: behavioral effects of increased gene expression

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

Change in direction of flagellar rotation is the basis of the chemotactic response in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.18.11850

21 January 2018

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10.1074/JBC.272.18.11850

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