(Q34985080)

English

Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ

scientific article

In more languages

default for all languages

No label defined

No description defined

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

1 reference

Europe PubMed Central

Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

transmembrane transport

0 references

transmembrane protein

0 references

author name string

Robert H Fillingame

1

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Oleg Y Dmitriev

2

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

language of work or name

0 references

publication date

1 October 2002

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Biochimica et Biophysica Acta

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

1565

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

2

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

232-245

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

ATP synthesis by oxidative phosphorylation

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

The oligomeric subunit C rotor in the fo sector of ATP synthase: unresolved questions in our understanding of function

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Intersubunit rotation in active F-ATPase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Direct observation of the rotation of F1-ATPase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

F-ATPase: specific observation of the rotating c subunit oligomer of EF(o)EF(1)

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Rotation of a complex of the gamma subunit and c ring of Escherichia coli ATP synthase. The rotor and stator are interchangeable

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

ATP synthase: a tentative structural model

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Energy transduction in ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Molecular imaging of Escherichia coli F0F1-ATPase in reconstituted membranes using atomic force microscopy

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Topographical structure of membrane-bound Escherichia coli F1F0 ATP synthase in aqueous buffer

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Arrangement of the multicopy H+-translocating subunit c in the membrane sector of the Escherichia coli F1F0 ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Genetic fusions of subunit c in the F0 sector of H+-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

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

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

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

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

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

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Defining the domain of binding of F1 subunit epsilon with the polar loop of F0 subunit c in the Escherichia coli ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Structure of the gamma-epsilon complex of ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Molecular architecture of the rotary motor in ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Structural biology. Proton-powered turbine of a plant motor

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Bacterial Na(+)-ATP synthase has an undecameric rotor

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

The second stalk of Escherichia coli ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

ATP synthase's second stalk comes into focus

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Direct indication for the existence of a double stalk in CF 0 F 1 1 1Edited by J. Karn

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

ATP Synthesis by Rotary Catalysis (Nobel lecture)

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Characterization of a b2delta complex from Escherichia coli ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

The second stalk composed of the b- and delta-subunits connects F0 to F1 via an alpha-subunit in the Escherichia coli ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Disulfide linkage of the b and delta subunits does not affect the function of the Escherichia coli ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Insights into the rotary catalytic mechanism of F0F1 ATP synthase from the cross-linking of subunits b and c in the Escherichia coli enzyme

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Structural changes linked to proton translocation by subunit c of the ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

The essential carboxyl group in subunit c of the F1F0 ATP synthase can be moved and H(+)-translocating function retained

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

The F1F0-ATPase of Escherichia coli. Substitution of proline by leucine at position 64 in the c-subunit causes loss of oxidative phosphorylation.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Hairpin folding of subunit c of F1Fo ATP synthase: 1H distance measurements to nitroxide-derivatized aspartyl-61.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Proton-translocating carboxyl of subunit c of F1Fo H(+)-ATP synthase: the unique environment suggested by the pKa determined by 1H NMR.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Changing the ion binding specificity of the Escherichia coli H(+)-transporting ATP synthase by directed mutagenesis of subunit c.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Molecular basis for the coupling ion selectivity of F1F0 ATP synthases: probing the liganding groups for Na+ and Li+ in the c subunit of the ATP synthase from Propionigenium modestum.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Apoprotein structure in the LH2 complex from Rhodopseudomonas acidophila strain 10050: modular assembly and protein pigment interactions

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Electron-crystallographic refinement of the structure of bacteriorhodopsin

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Operation of the F(0) motor of the ATP synthase

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Model of the c-subunit oligomer in the membrane domain of F-ATPases.

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Molecular architecture of the c-subunit oligomer in the membrane domain of F-ATPases probed by tryptophan substitution mutagenesis

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Molecular contacts in the transmembrane c-subunit oligomer of F-ATPases identified by tryptophan substitution mutagenesis

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

The gammaepsilon-c subunit interface in the ATP synthase of Escherichia coli. cross-linking of the epsilon subunit to the c subunit ring does not impair enzyme function, that of gamma to c subunits leads to uncoupling

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Structure of Ala24/Asp61 --> Asp24/Asn61 substituted subunit c of Escherichia coli ATP synthase: implications for the mechanism of proton transport and rotary movement in the F0 complex

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Molecular rotary motors

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2802%2900572-2

7 January 2021

Identifiers

10.1016/S0005-2736(02)00572-2

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 August 2017

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q34985080&oldid=2050141119"