scholarly article | Q13442814 |
P356 | DOI | 10.1016/S0005-2728(97)00101-1 |
P698 | PubMed publication ID | 9518621 |
P2093 | author name string | G B Cox | |
S M Howitt | |||
L P Hatch | |||
P2860 | cites work | The UNC operon nucleotide sequence, regulation and structure of ATP-synthase | Q40111464 |
Oxidative phosphorylation by mutant Escherichia coli membranes with impaired proton permeability | Q42037664 | ||
The function of ubiquinone in Escherichia coli | Q42172262 | ||
The transmembrane topology of the a [corrected] subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusions | Q44849296 | ||
The proton pore of the F0F1-ATPase of Escherichia coli: Ser-206 is not required for proton translocation. | Q54740051 | ||
Role of the carboxyl terminal region of H+-ATPase (F0F1a subunit from Escherichia coli | Q67897409 | ||
Mutational analysis of the function of the a-subunit of the F0F1-APPase of Escherichia coli | Q68409126 | ||
DNA sequencing with chain-terminating inhibitors | Q22066207 | ||
A rapid alkaline extraction procedure for screening recombinant plasmid DNA | Q24614998 | ||
2 New M13 vectors for cloning | Q27861042 | ||
Hybridization between Escherichia coli and Shigella. | Q33972142 | ||
An acidic or basic amino acid at position 26 of the b subunit of Escherichia coli F1F0-ATPase impairs membrane proton permeability: suppression of the uncF469 nonsense mutation | Q36287927 | ||
Second-site revertants of an arginine-210 to lysine mutation in the a subunit of the F0F1-ATPase from Escherichia coli: implications for structure | Q37254308 | ||
The proton-translocating ATPase of Escherichia coli | Q37855044 | ||
The coupling of the relative movement of the a and c subunits of the F0 to the conformational changes in the F1-ATPase | Q38465000 | ||
The essential arginine residue at position 210 in the alpha subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity | Q38466250 | ||
The role of arginine in the conserved polar loop of the c-subunit of the Escherichia coli H(+)-ATPase | Q38469790 | ||
The proton pore in the Escherichia coli F0F1-ATPase: a requirement for arginine at position 210 of the a-subunit | Q38475847 | ||
The mechanism of ATP synthase: a reassessment of the functions of the b and a subunits | Q38477714 | ||
Partial diploids of Escherichia coli carrying normal and mutant alleles affecting oxidative phosphorylation | Q39817358 | ||
A mutation affecting a second component of the F0 portion of the magnesium ion-stimulated adenosine triphosphatase of Escherichia coli K12. The uncC424 allele | Q39820637 | ||
P433 | issue | 3 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Escherichia coli | Q25419 |
P304 | page(s) | 217-223 | |
P577 | publication date | 1998-03-01 | |
P1433 | published in | Biochimica et Biophysica Acta | Q864239 |
P1476 | title | Glutamate residues at positions 219 and 252 in the a-subunit of the Escherichia coli ATP synthase are not functionally equivalent | |
P478 | volume | 1363 |
Q33933707 | A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation. |
Q37312462 | A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase. |
Q43959096 | A point mutation in the ATP synthase of Rhodobacter capsulatus results in differential contributions of Delta(pH) and Delta(phi) in driving the ATP synthesis reaction |
Q50467127 | Expanding the clinical phenotypes of MT-ATP6 mutations. |
Q34478495 | Mutagenic analysis of the F0 stator subunits |
Q44588220 | The role of transmembrane span 2 in the structure and function of subunit a of the ATP synthase from Escherichia coli. |
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