Renal Epithelial Protein (Apx) Is an Actin Cytoskeleton-regulated Na+ Channel

This publication has 32 references indexed in Scilit:

• Constitutive and regulated membrane expression of aquaporin 1 and aquaporin 2 water channels in stably transfected LLC-PK1 epithelial cells.
  Proceedings of the National Academy of Sciences, 1995
• Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits
  Nature, 1994
• The structural and functional diversity of dystrophin
  Nature Genetics, 1993
• Primary structure of an apical protein from Xenopus laevis that participates in amiloride-sensitive sodium channel activity.
  The Journal of cell biology, 1992
• Analysis of the actin-binding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain.
  The Journal of cell biology, 1992
• Actin-Binding Protein Requirement for Cortical Stability and Efficient Locomotion
  Science, 1992
• Modular organization of actin crosslinking proteins
  Trends in Biochemical Sciences, 1991
• Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity.
  The Journal of cell biology, 1988
• Conductance and gating of epithelial Na channels from rat cortical collecting tubule. Effects of luminal Na and Li.
  The Journal of general physiology, 1988
• Single-Channel Recordings from Two Types of Amiloride-Sensitive Epithelial Na⁺Channels
  Membrane Biochemistry, 1986