Now showing items 1-3 of 3

    • Biologically active two-dimensional crystals of aquaporin CHIP 

      Zeidel, Mark L.; Walz, Thomas; Smith, Barbara L.; Agre, Peter; Engel, Andreas (American Society for Biochemistry and Molecular Biology, 1994-01-21)
      Plasma membranes of several mammalian tissues are highly permeable to water due to the presence of CHIP, the 28-kDa channel-forming integral protein which is the archetypal member of the aquaporin family of water channel ...
    • Structural determinants of water permeation through aquaporin-1 

      Fujiyoshi, Yoshinori; Engel, Andreas; Heymann, J. Bernard; Agre, Peter; Walz, Thomas; Hirai, Teruhisa; Mitsuoka, Kaoru; Murata, Kazuyoshi (Nature Publishing Group, 2000-10-05)
      Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple ...
    • The three-dimensional structure of aquaporin-1 

      Engel, Andreas; Agre, Peter; Smith, Barbara L.; Fujiyoshi, Yoshinori; Mitsuoka, Kaoru; Heymann, J. Bernard; Murata, Kazuyoshi; Hirai, Teruhisa; Walz, Thomas (Nature Publishing Group, 1997-06-05)
      The entry and exit of water from cells is a fundamental process of life. Recognition of the high water permeability of red blood cells led to the proposal that specialized water pores exist in the plasma membrane. Expression ...