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

scholarly article

The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10. is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2001PNAS...98.4966J
P356DOI10.1073/PNAS.081424898
P932PMC publication ID33147
P698PubMed publication ID11320246
P5875ResearchGate publication ID12016336

P2093author name stringW Jiang
R H Fillingame
J Hermolin
P2860cites workGenetic fusions of subunit c in the F0 sector of H+-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysisQ77478046
The oligomeric subunit C rotor in the fo sector of ATP synthase: unresolved questions in our understanding of functionQ80341736
Molecular architecture of the rotary motor in ATP synthaseQ27620502
Construction and characterization of new cloning vehicle. II. A multipurpose cloning systemQ28298407
Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmidQ29614535
Direct observation of the rotation of F1-ATPaseQ29615360
The ATP synthase--a splendid molecular machineQ29617444
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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 enzymeQ36405477
Energy-transducing H+-ATPase of Escherichia coli. Purification, reconstitution, and subunit compositionQ39264367
44 DCCD-sensitive ATPase (TF0·F1) from a thermophilic bacterium: Purification, dissociation into functional subunits, and reconstitution into vesicles capable of energy transformationQ39888331
The UNC operon nucleotide sequence, regulation and structure of ATP-synthaseQ40111464
Stoichiometry of the proton-ATPase of growing and resting, aerobic Escherichia coliQ41554830
Mechanistic stoichiometry of mitochondrial oxidative phosphorylationQ45036631
Arrangement of the multicopy H+-translocating subunit c in the membrane sector of the Escherichia coli F1F0 ATP synthaseQ47921294
Stoichiometry of subunits in the H+-ATPase complex of Escherichia coli.Q50935516
Intersubunit rotation in active F-ATPaseQ59065016
Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observationQ73216171
Molecular rotary motorsQ73301215
F-ATPase: specific observation of the rotating c subunit oligomer of EF(o)EF(1)Q73713214
Insights into the rotary catalytic mechanism of F0F1 ATP synthase from the cross-linking of subunits b and c in the Escherichia coli enzymeQ73959913
P433issue9
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
stoichiometryQ213185
P304page(s)4966-4971
P577publication date2001-04-01
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleThe preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10.
P478volume98

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cites work (P2860)
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