Helical Interactions and Membrane Disposition of the 16-kDa Proteolipid Subunit of the Vacuolar H+-ATPase Analyzed by Cysteine Replacement Mutagenesis

This publication has 36 references indexed in Scilit:

• Visualization of a peripheral stalk in V-type ATPase: Evidence for the stator structure essential to rotational catalysis
  Proceedings of the National Academy of Sciences, 1997
• STRUCTURE, FUNCTION AND REGULATION OF THE VACUOLAR (H⁺)-ATPase
  Annual Review of Cell and Developmental Biology, 1997
• Direct observation of the rotation of F1-ATPase
  Nature, 1997
• Identification of functionally important helical faces in transmembrane segments by scanning mutagenesis.
  Proceedings of the National Academy of Sciences, 1995
• Ductin – a proton pump component, a gap junction channel and a neurotransmitter release channel
  BioEssays, 1995
• Determination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptor.
  Proceedings of the National Academy of Sciences, 1992
• Locations of Arg-82, Asp-85, and Asp-96 in helix C of bacteriorhodopsin relative to the aqueous boundaries.
  Proceedings of the National Academy of Sciences, 1991
• Transmembrane Protein Structure: Spin Labeling of Bacteriorhodopsin Mutants
  Science, 1990
• The evolution of H+-ATPases
  Trends in Biochemical Sciences, 1989
• cDNA sequence encoding the 16-kDa proteolipid of chromaffin granules implies gene duplication in the evolution of H+-ATPases.
  Proceedings of the National Academy of Sciences, 1988