(Q46986568)

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Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase. Deletions disrupt function but not enzyme assembly

scientific article published on 10 March 2006

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scholarly article

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Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase. Deletions disrupt function but not enzyme assembly (English)

1 reference

Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

Escherichia coli

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Daniel J Cipriano

1

1 reference

Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

Kristi S Wood

2

1 reference

Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

Yumin Bi

3

1 reference

Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

Stanley D Dunn

4

1 reference

Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

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publication date

10 March 2006

1 reference

Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

281

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Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

18

1 reference

Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

12408-12413

1 reference

Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

The ATP synthase--a splendid molecular machine

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Rotational coupling in the F0F1 ATP synthase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Catalytic mechanism of F1-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Dimerization interactions of the b subunit of the Escherichia coli F1F0-ATPase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Folding and stability of the b subunit of the F(1)F(0) ATP synthase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Specific heterodimer formation by the cytoplasmic domains of the b and b' subunits of cyanobacterial ATP synthase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

The structure of alpha-helical coiled coils

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Historical review: another 50th anniversary--new periodicities in coiled coils

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Coiled coils: new structures and new functions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Manipulating the length of the b subunit F1 binding domain in F1F0 ATP synthase from Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphenylglycoluril

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Genetic fusions of globular proteins to the epsilon subunit of the Escherichia coli ATP synthase: Implications for in vivo rotational catalysis and epsilon subunit function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

DNA Restriction Enzyme from E. coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

The b and delta subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

The role of the epsilon subunit in the Escherichia coli ATP synthase. The C-terminal domain is required for efficient energy coupling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Transient accumulation of elastic energy in proton translocating ATP synthase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513368200

21 January 2018

Identifiers

10.1074/JBC.M513368200

1 reference

Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

27 December 2017

http://europepmc.org/abstract/MED/16531410

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