Interacting Helical Surfaces of the Transmembrane Segments of Subunits a and c′ of the Yeast V-ATPase Defined by Disulfide-mediated Cross-linking

This publication has 62 references indexed in Scilit:

• Coupling proton movements to c-ring rotation in F1Fo ATP synthase: aqueous access channels and helix rotations at the a–c interface
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2002
• Cysteine-directed Cross-linking to Subunit B Suggests That Subunit E Forms Part of the Peripheral Stalk of the Vacuolar H+-ATPase
  Published by Elsevier ,2002
• The vacuolar (H+)-ATPases — nature's most versatile proton pumps
  Nature Reviews Molecular Cell Biology, 2002
• Molecular Architecture of the Rotary Motor in ATP Synthase
  Science, 1999
• Helical Interactions and Membrane Disposition of the 16-kDa Proteolipid Subunit of the Vacuolar H+-ATPase Analyzed by Cysteine Replacement Mutagenesis
  Journal of Biological Chemistry, 1999
• Solution Structure of the Transmembrane H⁺-Transporting Subunit c of the F₁F_o ATP Synthase
  Biochemistry, 1998
• The b and δ Subunits of the Escherichia coli ATP Synthase Interact via Residues in their C-terminal Regions
  Journal of Biological Chemistry, 1998
• Improved method for high efficiency transformation of intact yeast cells
  Nucleic Acids Research, 1992
• Gene duplication as a means for altering H⁺/ATP ratios during the evolution of F_o F₁ ATPases and synthases
  FEBS Letters, 1990
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970