scholarly article | Q13442814 |
P356 | DOI | 10.1042/BJ1800103 |
P953 | full work available at URL | https://europepmc.org/articles/PMC1161024 |
https://europepmc.org/articles/PMC1161024?pdf=render | ||
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/158357/?tool=EBI | ||
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/158357/pdf/?tool=EBI | ||
P932 | PMC publication ID | 1161024 |
P698 | PubMed publication ID | 158357 |
P5875 | ResearchGate publication ID | 22977997 |
P50 | author | Allan Downie | Q60018884 |
P2093 | author name string | F. Gibson | |
Cox GB | |||
Senior AE | |||
Downie JA | |||
Fayle DR | |||
Gibson F | |||
Langman L | |||
L. Langman | |||
A. E. Senior | |||
G. B. Cox | |||
D. R. Fayle | |||
P2860 | cites work | Protein measurement with the Folin phenol reagent | Q20900776 |
Bacterial respiration | Q24564163 | ||
Energy transduction in Escherichia coli: new mutation affecting the Fo portion of the ATP synthetase complex | Q30452017 | ||
Inhibition, by a protease inhibitor, of the solubilization of the F1-portion of the Mg2+-stimulated adenosine triphosphatase of Escherichia coli | Q36417613 | ||
Mu-induced polarity in the unc operon of Escherichia coli | Q36420751 | ||
Purification and properties of reconstitutively active and inactive adenosinetriphosphatase from Escherichia coli | Q37451914 | ||
ATPase of Escherichia coli: purification, dissociation, and reconstitution of the active complex from the isolated subunits | Q39075259 | ||
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 | ||
Assembly of the catalytic unit of the Escherichia coli membrane ATPase in vitro requires the γ chain | Q39827590 | ||
Characterization of the purified membrane attachment (δ) subunit of the proton translocating adenosine triphosphatase from Escherichia coli | Q39830909 | ||
Genetic complementation between two mutant unc alleles (unc A401 and unc D409) affecting the F1 portion of the magnesium ion-stimulated adenosine triphosphatase of Escherichia coli K12 | Q39852050 | ||
Identfication of the altered subunit in the inactive F1ATPase of an Escherichia coli uncA mutant | Q39858051 | ||
Characterization of the mutant-unc D-gene product in a strain of Escherichia coli K12. An altered β-subunit of the magnesium ion-stimulated adenosine triphosphatase | Q39859884 | ||
Coupling factor ATPase from Escherichia coli. An uncA mutant (uncA401) with defective alpha subunit | Q39874658 | ||
Properties of membranes from mutant strains of Escherichia coli in which the β-subunit of the adenosine triphosphatase is abnormal | Q39895337 | ||
Oxidative phosphorylation in Escherichia coli K12. Mutations affecting magnesium ion- or calcium ion-stimulated adenosine triphosphatase | Q42025286 | ||
Reconstitution of oxidative phosphorylation and the adenosine triphosphate-dependent transhydrogenase activity by a combination of membrane fractions from unCA- and uncB- mutant strains of Escherichia coli K12. | Q42924008 | ||
Studies on the mitochondrial oligomycin-insensitivt ATPase. I. An improved method of purification and the behavior of the enzyme in solutions of various depolymerizing agents | Q43634042 | ||
Purification of a factor for both aerobic-driven and ATP-driven energy-dependent transhydrogenases of Escherichia coli | Q77920807 | ||
P433 | issue | 1 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Escherichia coli | Q25419 |
P304 | page(s) | 103-109 | |
P577 | publication date | 1979-04-01 | |
1979-04-15 | |||
P1433 | published in | Biochemical Journal | Q864221 |
P1476 | title | The uncA gene codes for the alpha-subunit of the adenosine triphosphatase of Escherichia coli. Electrophoretic analysis of uncA mutant strains | |
The uncA gene codes for the α-subunit of the adenosine triphosphatase of Escherichia coli. Electrophoretic analysis of uncA mutant strains | |||
P478 | volume | 180 |