Fo portion of Escherichia coli ATP synthase. Further resolution of trypsin-generated fragments from subunit b.

This publication has 30 references indexed in Scilit:

• Modification of subunit b of the Fo complex from Escherichia coli ATP synthase by a hydrophobic maleimide and its effects on Fo functions
  European Journal of Biochemistry, 1985
• Structure of the membrane-embedded F0 part of F1F0 ATP synthase from Escherichia coli as inferred from labeling with 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine
  Biochemistry, 1984
• Chemical modification of the F₀ part of the ATP synthase (F₁F₀) from Escherichia coli
  European Journal of Biochemistry, 1984
• Secondary and tertiary structure of membrane proteins involved in proton translocation
  Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1983
• Conformational change of the α subunit of Escherichia coli F1 ATPase: ATP changes the trypsin sensitivity of the subunit
  Archives of Biochemistry and Biophysics, 1983
• ATP Synthetase (F₁F₀) of Escherichia coli K‐12
  European Journal of Biochemistry, 1982
• E. coli F1-ATPase interacts with a membrane protein component of a proton channel
  Nature, 1982
• ATP‐synthetase complex (F₁F₀) from Escherichia coli
  FEBS Letters, 1982
• The isolated of F₀ of escherichia coli ATP‐synthase is reconstitutively active in H⁺‐conduction and ATP‐dependent energy‐transduction
  FEBS Letters, 1981
• ATPase of Escherichia coli: purification, dissociation, and reconstitution of the active complex from the isolated subunits
  Biochemistry, 1976