Now showing items 110-116 of 116

    • Targeted disruption of the Cl−/HCO3− exchanger Ae2 results in osteopetrosis in mice 

      Praetorius, J.; Nielsen, S; Agre, P; Frische, S.; Gawenis, L R; Kwon, T H; Fejerskov, O.; Josephsen, K. (National Academy of Sciences, 2009-02-03)
      Osteoclasts are multinucleated bone-resorbing cells responsible for constant remodeling of bone tissue and for maintaining calcium homeostasis. The osteoclast creates an enclosed space, a lacuna, between their ruffled ...
    • Targeted disruption of the Cl−/HCO3− exchanger Ae2 results in osteopetrosis in mice 

      Kwon, T; Gawenis, L; Frische, S.; Praetorius, J.; Josephsen, K.; Agre, P (National Academy of Sciences, 2009-02-03)
      Osteoclasts are multinucleated bone-resorbing cells responsible for constant remodeling of bone tissue and for maintaining calcium homeostasis. The osteoclast creates an enclosed space, a lacuna, between their ruffled ...
    • Temporary loss of perivascular aquaporin-4 in neocortex after transient middle cerebral artery occlusion in mice 

      Amiry-Moghaddam, M.; Ottersen, O. P.; Agre, P; Rash, J. E.; Haug, F. M.; Laake, P.; Skare, O.; Zeynalov, E.; Davidson, K. G.; Yasumura, T.; Mylonakou, M. N.; Otsuka, T.; Bhardwaj, A.; Frydenlund, D. S. (National Academy of Sciences, 2006-09-05)
      The aquaporin-4 (AQP4) pool in the perivascular astrocyte membranes has been shown to be critically involved in the formation and dissolution of brain edema. Cerebral edema is a major cause of morbidity and mortality in ...
    • 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 ...
    • Water and ion permeation of aquaporin-1 in planar lipid bilayers. Major differences in structural determinants and stoichiometry. 

      Pohl, Peter; Agre, Peter; Rothe, Ulrich; Kozono, David; Saparov, S. M. (American Society for Biochemistry and Molecular Biology, 2001-08-24)
      The aquaporin-1 (AQP1) water channel protein is known to facilitate the rapid movement of water across cell membranes, but a proposed secondary role as an ion channel is still unsettled. Here we describe a method to ...
    • Water channel properties of major intrinsic protein of lens 

      Agre, P; Van Os, C. H.; Guggino, W B; Deen, P. M.; Preston, G M; Mulders, S. M. (American Society for Biochemistry and Molecular Biology, 1995-04-14)
      The functions of major intrinsic protein (MIP) of lens are still unresolved; however the sequence homology with channel-forming integral membrane protein (CHIP) and other Aquaporins suggests that MIP is a water channel. ...
    • Water channel properties of major intrinsic protein of lens 

      Guggino, W B; Mulders, S. M.; Preston, G M; Deen, P. M.; Agre, P; Van Os, C. H. (American Society for Biochemistry and Molecular Biology, 1995-04-14)
      The functions of major intrinsic protein (MIP) of lens are still unresolved; however the sequence homology with channel-forming integral membrane protein (CHIP) and other Aquaporins suggests that MIP is a water channel. ...