Mitochondrial F(0)F(1) ATP synthase. Subunit regions on the F1 motor shielded by F(0), Functional significance, and evidence for an involvement of the unique F(0) subunit F(6) (Q28570333)

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English	Mitochondrial F(0)F(1) ATP synthase. Subunit regions on the F1 motor shielded by F(0), Functional significance, and evidence for an involvement of the unique F(0) subunit F(6)	scientific journal article

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scholarly article

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PubMed publication ID

31 January 2017

Mitochondrial F(0)F(1) ATP synthase. Subunit regions on the F1 motor shielded by F(0), Functional significance, and evidence for an involvement of the unique F(0) subunit F(6) (English)

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PubMed publication ID

31 January 2017

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Y. H. Ko

1

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PubMed publication ID

31 January 2017

J. Hullihen

2

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31 January 2017

S. Hong

3

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31 January 2017

P. L. Pedersen

4

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31 January 2017

language of work or name

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publication date

20 October 2000

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PubMed publication ID

31 January 2017

Journal of Biological Chemistry

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PubMed publication ID

31 January 2017

275

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31 January 2017

42

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31 January 2017

32931–32939

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PubMed publication ID

31 January 2017

Catalytic mechanism of F1-ATPase

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The ATP synthase--a splendid molecular machine

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The stalk connecting the F1 and F0 domains of ATP synthase visualized by electron microscopy of unstained specimens

1 reference

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A cryoelectron microscopy study of the interaction of the Escherichia coli F1-ATPase with subunit b dimer.

1 reference

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Localization of the delta subunit in the Escherichia coli F(1)F(0)-ATPsynthase by immuno electron microscopy: the delta subunit binds on top of the F(1).

1 reference

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21 January 2018

Identification of the subunits of F1F0-ATPase from bovine heart mitochondria

1 reference

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Escherichia coli H(+)-ATPase: role of the delta subunit in binding Fl to the Fo sector

1 reference

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ATP synthase from bovine heart mitochondria: identification by proteolysis of sites in F0 exposed by removal of F1 and the oligomycin-sensitivity conferral protein

1 reference

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ATP synthase complex. Proximities of subunits in bovine submitochondrial particles

1 reference

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Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase. Cys-Cys cross-linking of F1 subunit epsilon to the polar loop of F0 subunit c.

1 reference

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Cross-linking of engineered subunit delta to (alphabeta)3 in chloroplast F-ATPase.

1 reference

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The stalk region of the Escherichia coli ATP synthase. Tyrosine 205 of the gamma subunit is in the interface between the F1 and F0 parts and can interact with both the epsilon and c oligomer.

1 reference

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21 January 2018

Delta subunit of rat liver mitochondrial ATP synthase: molecular description and novel insights into the nature of its association with the F1-moiety

1 reference

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

1 reference

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The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis

1 reference

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Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography

1 reference

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21 January 2018

Molecular architecture of the rotary motor in ATP synthase

1 reference

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Direct observation of the rotation of F1-ATPase

1 reference

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Direct observation of the rotation of epsilon subunit in F1-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M004453200

21 January 2018

Structure of the subunit c oligomer in the F1Fo ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme

1 reference

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21 January 2018

ATP synthase: two motors, two fuels

1 reference

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21 January 2018

The mechanism and regulation of ATP synthesis by F1-ATPases

1 reference

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21 January 2018

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

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

1 reference

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Method for Determination of the Amino Acid Sequence in Peptides

1 reference

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21 January 2018

Eukaryote membrane genetics: the Fo sector of mitochondrial ATP synthase

1 reference

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21 January 2018

The role of the stalk in the coupling mechanism of F1F0-ATPases

1 reference

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21 January 2018

ATP synthase: an electrochemical transducer with rotatory mechanics

1 reference

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21 January 2018

F1-ATPase: a rotary motor made of a single molecule

1 reference

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Energy transduction in ATP synthase

1 reference

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Structure/function of the beta-barrel domain of F1-ATPase in the yeast Saccharomyces cerevisiae

1 reference

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Novel Insights into the Chemical Mechanism of ATP Synthase

1 reference

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21 January 2018

The F1Fo-ATPase Complex from Bovine Heart Mitochondria: The Molar Ratio of the Subunits in the Stalk Region Linking the F1and FoDomains

1 reference

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21 January 2018

The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer

1 reference

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21 January 2018

ATP synthase's second stalk comes into focus

1 reference

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Novel features in the structure of bovine ATP synthase

1 reference

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Membrane topography and near-neighbor relationships of the mitochondrial ATP synthase subunits e, f, and g

1 reference

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Characterization of the interface between gamma and epsilon subunits of Escherichia coli F1-ATPase

1 reference

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Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation

1 reference

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Protein sequence analysis: automated microsequencing

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Pyrrolidonyl peptidase. An enzyme for selective removal of pyrrolidonecarboxylic acid residues from polypeptides

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Rat liver ATP synthase. Relationship of the unique substructure of the F1 moiety to its nucleotide binding properties, enzymatic states, and crystalline form

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Interaction between delta and epsilon subunits of F1-ATPase from pig heart mitochondria. Circular dichroism and intrinsic fluorescence of purified and reconstituted delta epsilon complex

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21 January 2018

Identifiers

10.1074/JBC.M004453200

1 reference

PubMed publication ID

31 January 2017

PubMed publication ID

1 reference

PubMed publication ID

31 January 2017

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