메뉴 건너뛰기




Volumn 190, Issue , 2009, Pages 327-358

Ammonia and urea permeability of mammalian aquaporins

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; AQUAPORIN; AQUAPORIN 1; AQUAPORIN 10; AQUAPORIN 2; AQUAPORIN 3; AQUAPORIN 4; AQUAPORIN 5; AQUAPORIN 6; AQUAPORIN 7; AQUAPORIN 8; AQUAPORIN 9; ARGININE; GLYCEROL; GLYCOPROTEIN; NITROGEN; PROTON; RH ASSOCIATED GLYCOPROTEIN; RH B GLYCOPROTEIN; RH C GLYCOPROTEIN; RHESUS ANTIGEN; UNCLASSIFIED DRUG; UREA; CARRIER PROTEIN; UREA TRANSPORTER;

EID: 61449361443     PISSN: 01712004     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-540-79885-9_17     Document Type: Review
Times cited : (100)

References (91)
  • 1
    • 0030897747 scopus 로고    scopus 로고
    • Permeation of ammonia across bilayer lipid membranes studied by ammonium ion selective microelectrodes
    • Antonenko YN, Pohl P, Denisov GA (1997) Permeation of ammonia across bilayer lipid membranes studied by ammonium ion selective microelectrodes. Biophys J 72:2187-2195
    • (1997) Biophys J , vol.72 , pp. 2187-2195
    • Antonenko, Y.N.1    Pohl, P.2    Denisov, G.A.3
  • 2
    • 9344238209 scopus 로고    scopus 로고
    • Distribution and possible roles of aquaporin 9 in the brain
    • Badaut J, Regli L (2004) Distribution and possible roles of aquaporin 9 in the brain. Neuroscience 129:971-981
    • (2004) Neuroscience , vol.129 , pp. 971-981
    • Badaut, J.1    Regli, L.2
  • 3
    • 33847168237 scopus 로고    scopus 로고
    • The erythrocyte urea transporter UT-B
    • Bagnasco SM (2006) The erythrocyte urea transporter UT-B. J Membr Biol 212:133-138
    • (2006) J Membr Biol , vol.212 , pp. 133-138
    • Bagnasco, S.M.1
  • 5
    • 33746280869 scopus 로고    scopus 로고
    • Aquaporin water and solute channels from malaria parasites and other pathogenic protozoa
    • Beitz E (2006) Aquaporin water and solute channels from malaria parasites and other pathogenic protozoa. Chem Med Chem 1:587-592
    • (2006) Chem Med Chem , vol.1 , pp. 587-592
    • Beitz, E.1
  • 6
    • 0842342619 scopus 로고    scopus 로고
    • Molecular dissection of water and glycerol permeability of the aquaporin from Plasmodium falciparum by mutational analysis
    • Beitz E, Pavlovic-Djuranovic S, Yasui M, Agre P, Schultz JE (2003) Molecular dissection of water and glycerol permeability of the aquaporin from Plasmodium falciparum by mutational analysis. Proc Natl Acad Sci U S A 101:1153-1158
    • (2003) Proc Natl Acad Sci U S A , vol.101 , pp. 1153-1158
    • Beitz, E.1    Pavlovic-Djuranovic, S.2    Yasui, M.3    Agre, P.4    Schultz, J.E.5
  • 7
    • 31044449089 scopus 로고    scopus 로고
    • Beitz E, Wu B, Holm LM, Schultz JE, Zeuthen T (2006) Point mutations in the aromatic/argine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons. Proc Natl Acad Sci U S A 103:269-274
    • Beitz E, Wu B, Holm LM, Schultz JE, Zeuthen T (2006) Point mutations in the aromatic/argine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons. Proc Natl Acad Sci U S A 103:269-274
  • 8
    • 36048973290 scopus 로고    scopus 로고
    • Function of a separate NH3-pore in aquaporin TIP2;2 from wheat
    • Bertl B, Kaldenhoff R (2007) Function of a separate NH3-pore in aquaporin TIP2;2 from wheat. FEBS Lett 581:5413-5417
    • (2007) FEBS Lett , vol.581 , pp. 5413-5417
    • Bertl, B.1    Kaldenhoff, R.2
  • 11
    • 0033520342 scopus 로고    scopus 로고
    • Functional reconstitution and characterization of AqpZ, the E. coli water channel protein
    • Borgnia MJ, Kozono D, Calamita G, Maloney PC, Agre P (1999) Functional reconstitution and characterization of AqpZ, the E. coli water channel protein. J Mol Biol 291:1169-1179
    • (1999) J Mol Biol , vol.291 , pp. 1169-1179
    • Borgnia, M.J.1    Kozono, D.2    Calamita, G.3    Maloney, P.C.4    Agre, P.5
  • 12
    • 0033913601 scopus 로고    scopus 로고
    • The Escherichia coli aquaporin-Z water channel
    • Calamita G (2000) The Escherichia coli aquaporin-Z water channel. Mol Microbiol 37:254-262
    • (2000) Mol Microbiol , vol.37 , pp. 254-262
    • Calamita, G.1
  • 17
    • 33947302077 scopus 로고    scopus 로고
    • Defective hepatocyte aquaporin-8 expression and reduced canalicular membrane water permeability in estrogeninduced cholestasis
    • Carreras F, Lehmann GL, Ferri D, Tioni MF, Calamita G, Marinelli RA (2007) Defective hepatocyte aquaporin-8 expression and reduced canalicular membrane water permeability in estrogeninduced cholestasis. Am J Physiol 292:G905-G912
    • (2007) Am J Physiol , vol.292
    • Carreras, F.1    Lehmann, G.L.2    Ferri, D.3    Tioni, M.F.4    Calamita, G.5    Marinelli, R.A.6
  • 18
    • 33646170424 scopus 로고    scopus 로고
    • Origins of proton transport behavior from selectivity domain mutations of the aquaporin-1 channel
    • Chen H, Wu Y, Voth GA (2006) Origins of proton transport behavior from selectivity domain mutations of the aquaporin-1 channel. Biophys J: Biophys Lett 70:L73-L75
    • (2006) Biophys J: Biophys Lett , vol.70
    • Chen, H.1    Wu, Y.2    Voth, G.A.3
  • 19
    • 17044406611 scopus 로고    scopus 로고
    • The dynamics and energetics of water permeation and proton exclusion in aquaporins
    • de Groot BL, Grubmüller H (2005) The dynamics and energetics of water permeation and proton exclusion in aquaporins. Curr Opin Struct Biol 15:176-183
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 176-183
    • de Groot, B.L.1    Grubmüller, H.2
  • 20
    • 0141534474 scopus 로고    scopus 로고
    • The mechanism of proton exclusion in the aquaporin-1 water channel
    • de Groot BL, Frigato T, Helms V, Grubmüller H (2003) The mechanism of proton exclusion in the aquaporin-1 water channel. J Mol Biol 333:279-293
    • (2003) J Mol Biol , vol.333 , pp. 279-293
    • de Groot, B.L.1    Frigato, T.2    Helms, V.3    Grubmüller, H.4
  • 21
    • 0029834336 scopus 로고    scopus 로고
    • Selectivity of the renal collecting duct water channel aquaporin-3
    • Echevarŕia M,Windhager EE, Frindt G (1996) Selectivity of the renal collecting duct water channel aquaporin-3. J Biol Chem 271:25079-25082
    • (1996) J Biol Chem , vol.271 , pp. 25079-25082
    • Echevarŕia, M.1    Windhager, E.E.2    Frindt, G.3
  • 23
    • 0036209785 scopus 로고    scopus 로고
    • Aquaglyceroporins: Channel proteins with a conserved core, multiple functions, and variable surfaces
    • Engel A, Stahlberg H (2002) Aquaglyceroporins: channel proteins with a conserved core, multiple functions, and variable surfaces. Int Rev Cytol 215:75-104
    • (2002) Int Rev Cytol , vol.215 , pp. 75-104
    • Engel, A.1    Stahlberg, H.2
  • 24
    • 35648949891 scopus 로고    scopus 로고
    • Mouse models and the urinary concentrating mechanism in the new millenium
    • Fenton RA, Knepper MA (2007) Mouse models and the urinary concentrating mechanism in the new millenium. Physiol Rev 87:1083-1112
    • (2007) Physiol Rev , vol.87 , pp. 1083-1112
    • Fenton, R.A.1    Knepper, M.A.2
  • 25
    • 0141643394 scopus 로고    scopus 로고
    • Ontogeny, distribution, and possible functional implications of an unusual aquaporin, AQP8, in mouse liver
    • Ferri D, Mazzone A, Liquori GE, Cassano G, Svelto M, Calamita G (2003) Ontogeny, distribution, and possible functional implications of an unusual aquaporin, AQP8, in mouse liver. Hepatology 38:947-957
    • (2003) Hepatology , vol.38 , pp. 947-957
    • Ferri, D.1    Mazzone, A.2    Liquori, G.E.3    Cassano, G.4    Svelto, M.5    Calamita, G.6
  • 26
    • 0035853805 scopus 로고    scopus 로고
    • The water channel aquaporin-8 is mainly intracellular in rat hepatocytes, and its plasma membrane insertion is stimulated by cyclic AMP
    • Garcia F, Kierbel A, Larocca MC, Gradilone SA, Splinter P, LaRusso NF,Marinelli RA (2001) The water channel aquaporin-8 is mainly intracellular in rat hepatocytes, and its plasma membrane insertion is stimulated by cyclic AMP. J Biol Chem 276:12147-12152
    • (2001) J Biol Chem , vol.276 , pp. 12147-12152
    • Garcia, F.1    Kierbel, A.2    Larocca, M.C.3    Gradilone, S.A.4    Splinter, P.5    LaRusso, N.F.6    Marinelli, R.A.7
  • 27
    • 33845669996 scopus 로고    scopus 로고
    • The structure of aquaporins
    • Gonen T, Walz T (2006) The structure of aquaporins. Q Rev Biophys 39:361-396
    • (2006) Q Rev Biophys , vol.39 , pp. 361-396
    • Gonen, T.1    Walz, T.2
  • 28
    • 33745292751 scopus 로고    scopus 로고
    • Physiological roles of glycerol-transporting aquaporins: The aquaglycerolporins
    • Hara-Chikuma M, Verkman AS (2006) Physiological roles of glycerol-transporting aquaporins: the aquaglycerolporins. Cell Mol Life Sci 63:1386-1392
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1386-1392
    • Hara-Chikuma, M.1    Verkman, A.S.2
  • 30
    • 0342385828 scopus 로고    scopus 로고
    • Physiological functions of the liver
    • Greger R, Windhorst U eds, Springer-Verlag, Berlin, Heidelberg, pp
    • Häussinger (1996a) Physiological functions of the liver. In: Greger R, Windhorst U (eds.) Comprehensive human physiology, vol. 2. Springer-Verlag, Berlin, Heidelberg, pp. 1369-1391
    • (1996) Comprehensive human physiology , vol.2 , pp. 1369-1391
    • Häussinger1
  • 31
    • 25644442889 scopus 로고    scopus 로고
    • Zonal metabolism in the liver
    • Greger R, Windhorst U eds, Springer-Verlag, Berlin, Heidelberg, pp
    • Häussinger (1996b) Zonal metabolism in the liver. In: Greger R, Windhorst U (eds.) Comprehensive human physiology, vol 2. Springer-Verlag, Berlin, Heidelberg, pp. 1393-1402
    • (1996) Comprehensive human physiology , vol.2 , pp. 1393-1402
    • Häussinger1
  • 34
    • 77953681701 scopus 로고    scopus 로고
    • Ammonia transport in aquaporins: Molecular mechanisms and clinical relevance
    • Häussinger D, Kircheis G, Schliess F eds, Springer, Düsseldorf, pp
    • Holm, Zeuthen T (2007) Ammonia transport in aquaporins: molecular mechanisms and clinical relevance. In: Häussinger D, Kircheis G, Schliess F (eds.) Hepatic encephalopathy and nitrogen metabolism. Springer, Düsseldorf, pp. 387-393
    • (2007) Hepatic encephalopathy and nitrogen metabolism , pp. 387-393
    • Holm, Z.T.1
  • 35
    • 2442438631 scopus 로고    scopus 로고
    • Aquaporin 6 is permeable to glycerol and urea
    • Holm LM, Klaerke DA, Zeuthen T (2004) Aquaporin 6 is permeable to glycerol and urea. Pflügers Arch 448:181-186
    • (2004) Pflügers Arch , vol.448 , pp. 181-186
    • Holm, L.M.1    Klaerke, D.A.2    Zeuthen, T.3
  • 37
    • 0035053248 scopus 로고    scopus 로고
    • New insights into the Rh superfamily of genes and proteins in erythroid cells and nonerythroid tissues
    • Huang C-H, Liu PZ (2001) New insights into the Rh superfamily of genes and proteins in erythroid cells and nonerythroid tissues. Blood Cells Mol Dis 27:90-101
    • (2001) Blood Cells Mol Dis , vol.27 , pp. 90-101
    • Huang, C.-H.1    Liu, P.Z.2
  • 39
    • 0030860531 scopus 로고    scopus 로고
    • Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea
    • Ishibashi K, Kuwahara M, Gu Y, Kageyama Y, Tohsaka A, Suzuki F, Marumo F, Sasaki S (1997) Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea. J Biol Chem 272:20782-20786
    • (1997) J Biol Chem , vol.272 , pp. 20782-20786
    • Ishibashi, K.1    Kuwahara, M.2    Gu, Y.3    Kageyama, Y.4    Tohsaka, A.5    Suzuki, F.6    Marumo, F.7    Sasaki, S.8
  • 40
    • 0028227129 scopus 로고
    • Molecular cloning and expression of a member of the aquaporin family with permeability to glycerol and urea in addition to water expressed at the basolateral membrane of kidney collecting duct cells
    • Ishibashi K, Sasaki S, Fushimi K, Uchida S, Kuwahara M, Saito H, Furukawa T, Nakajima K, Yamaguchi M, Gojobori T, Marumo F (1994) Molecular cloning and expression of a member of the aquaporin family with permeability to glycerol and urea in addition to water expressed at the basolateral membrane of kidney collecting duct cells. Proc Natl Acad Sci U S A 91:6369-6273
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 6369-6273
    • Ishibashi, K.1    Sasaki, S.2    Fushimi, K.3    Uchida, S.4    Kuwahara, M.5    Saito, H.6    Furukawa, T.7    Nakajima, K.8    Yamaguchi, M.9    Gojobori, T.10    Marumo, F.11
  • 41
    • 0037135227 scopus 로고    scopus 로고
    • Cloning and identification of a new member of water channel (AQP10) as an aquaglyceroporin
    • Ishibashi K, Morinaga T, Kuwahara M, Sasaki S, Imai M (2002) Cloning and identification of a new member of water channel (AQP10) as an aquaglyceroporin. Biochim Biophys Acta 1576:335-340
    • (2002) Biochim Biophys Acta , vol.1576 , pp. 335-340
    • Ishibashi, K.1    Morinaga, T.2    Kuwahara, M.3    Sasaki, S.4    Imai, M.5
  • 43
    • 0000597153 scopus 로고
    • A physical interpretation of the phenomenological coefficients of membrane permeability
    • Kedem O, Katchalsky A (1961) A physical interpretation of the phenomenological coefficients of membrane permeability. J Gen Physiol 45:143-179
    • (1961) J Gen Physiol , vol.45 , pp. 143-179
    • Kedem, O.1    Katchalsky, A.2
  • 44
    • 33845318547 scopus 로고    scopus 로고
    • The Amt/MEP/Rh family: Structure of AmtB and the mechanism of ammonia gas conduction
    • Khademi S, Stroud RM (2006) The Amt/MEP/Rh family: structure of AmtB and the mechanism of ammonia gas conduction. Physiology 21:419-429
    • (2006) Physiology , vol.21 , pp. 419-429
    • Khademi, S.1    Stroud, R.M.2
  • 45
    • 4444221676 scopus 로고    scopus 로고
    • From structure to disease: The evolving tale of aquaporin biology
    • King LS, Kozono D, Agre P (2004) From structure to disease: the evolving tale of aquaporin biology. Nat Rev Mol Cell Biol 5:687-698
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 687-698
    • King, L.S.1    Kozono, D.2    Agre, P.3
  • 50
    • 0034682768 scopus 로고    scopus 로고
    • Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis
    • Liu Z, Chen Y, Mo R, Hui C, Cheng J-F, Mohandas N, Huang C-H (2000) Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis. J Biol Chem 275:25641-25651
    • (2000) J Biol Chem , vol.275 , pp. 25641-25651
    • Liu, Z.1    Chen, Y.2    Mo, R.3    Hui, C.4    Cheng, J.-F.5    Mohandas, N.6    Huang, C.-H.7
  • 51
    • 0035847047 scopus 로고    scopus 로고
    • Rh type B glycoprotein is a new member of the Rh superfamily and a putative ammonia transporter in mammals
    • Liu Z, Peng J, Mo R, Hui C-C, Huang C-H (2001) Rh type B glycoprotein is a new member of the Rh superfamily and a putative ammonia transporter in mammals. J Biol Chem 276:1424-1433
    • (2001) J Biol Chem , vol.276 , pp. 1424-1433
    • Liu, Z.1    Peng, J.2    Mo, R.3    Hui, C.-C.4    Huang, C.-H.5
  • 53
    • 33644758290 scopus 로고    scopus 로고
    • Purification and functional characterization of aquaporin-8
    • Liu K, Nagase H, Huang CG, Calamita G, Agre P (2006) Purification and functional characterization of aquaporin-8. Biol Cell 98:153-161
    • (2006) Biol Cell , vol.98 , pp. 153-161
    • Liu, K.1    Nagase, H.2    Huang, C.G.3    Calamita, G.4    Agre, P.5
  • 54
    • 19044393297 scopus 로고    scopus 로고
    • Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3 transport into the vacuole
    • Loque D, Ludewig U, Yuan L, von Wiren N (2005) Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3 transport into the vacuole. Plant Physiol 137:671-680
    • (2005) Plant Physiol , vol.137 , pp. 671-680
    • Loque, D.1    Ludewig, U.2    Yuan, L.3    von Wiren, N.4
  • 56
    • 33644867242 scopus 로고    scopus 로고
    • Characterization of ammonia transport by the kidney Rh glycoproteins RhBG and RhCG
    • Mak D-OM, Dang B, Weiner ID, Foskett JK, Westhoff CM (2006) Characterization of ammonia transport by the kidney Rh glycoproteins RhBG and RhCG. Am J Physiol 290:F297-F305
    • (2006) Am J Physiol , vol.290
    • Mak, D.-O.M.1    Dang, B.2    Weiner, I.D.3    Foskett, J.K.4    Westhoff, C.M.5
  • 57
    • 0033757434 scopus 로고    scopus 로고
    • The human rhesusassociated RhAG protein and a kidney homologue promote ammonium transport in yeast
    • Marini A-M, Matassi G, Raynal V, André B, Cartron J-P,Chérif-Zahar B (2000) The human rhesusassociated RhAG protein and a kidney homologue promote ammonium transport in yeast. Nat Genet 26:341-344
    • (2000) Nat Genet , vol.26 , pp. 341-344
    • Marini, A.-M.1    Matassi, G.2    Raynal, V.3    André, B.4    Cartron, J.-P.5    Chérif-Zahar, B.6
  • 58
    • 85177152899 scopus 로고    scopus 로고
    • Maurel C, Reizer J, Schroeder JI, Chrispeels MJ, Saier Jr MH (1994) Functional characterization of the Escherichia coli glycerol facilitator, GlpF, in Xenopus Oocytes. J Biol Chem 269:11869-11872
    • Maurel C, Reizer J, Schroeder JI, Chrispeels MJ, Saier Jr MH (1994) Functional characterization of the Escherichia coli glycerol facilitator, GlpF, in Xenopus Oocytes. J Biol Chem 269:11869-11872
  • 60
    • 0032484119 scopus 로고    scopus 로고
    • Bidirectional water fluxes and specificity for small hydrophilic molecules in aquaporins 0 to 5
    • Meinild A-K, Klaerke DA, Zeuthen T (1998) Bidirectional water fluxes and specificity for small hydrophilic molecules in aquaporins 0 to 5. J Biol Chem 273:32446-32451
    • (1998) J Biol Chem , vol.273 , pp. 32446-32451
    • Meinild, A.-K.1    Klaerke, D.A.2    Zeuthen, T.3
  • 64
  • 68
    • 33847768229 scopus 로고    scopus 로고
    • Aquaglyceroporin PbAQP during intraerythrocytic development of the malaria parasite Plasmodium berghei
    • Promeneur D, Lui Y, Maciel J, Agre P, King LS, Kumar N (2007) Aquaglyceroporin PbAQP during intraerythrocytic development of the malaria parasite Plasmodium berghei. Proc Natl Acad Sci U S A 104:2211-2216
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 2211-2216
    • Promeneur, D.1    Lui, Y.2    Maciel, J.3    Agre, P.4    King, L.S.5    Kumar, N.6
  • 73
    • 34247104106 scopus 로고    scopus 로고
    • Fast and selective ammonia transport by aquaporin-8
    • Saparov MS, Liu K, Agre P, Pohl P (2007) Fast and selective ammonia transport by aquaporin-8. J Biol Chem 282:5296-5301
    • (2007) J Biol Chem , vol.282 , pp. 5296-5301
    • Saparov, M.S.1    Liu, K.2    Agre, P.3    Pohl, P.4
  • 74
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignments aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL X windows interface: flexible strategies for multiple sequence alignments aided by quality analysis tools. Nucleic Acids Res 25:4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 75
    • 0032739871 scopus 로고    scopus 로고
    • Functional and molecular characterization of the human neutral solute channel aquaporin-9
    • Tsukaguchi H,Weremowicz S, Morton CC, Hediger MA (1999) Functional and molecular characterization of the human neutral solute channel aquaporin-9. Am J Physiol 277:F685-F696
    • (1999) Am J Physiol , vol.277
    • Tsukaguchi, H.1    Weremowicz, S.2    Morton, C.C.3    Hediger, M.A.4
  • 76
    • 24344497831 scopus 로고    scopus 로고
    • More than just water channels: Unexpected cellular roles of aquaporins
    • Verkman AS (2005) More than just water channels: unexpected cellular roles of aquaporins. J Cell Sci 118:3225-3232
    • (2005) J Cell Sci , vol.118 , pp. 3225-3232
    • Verkman, A.S.1
  • 77
    • 0028280013 scopus 로고
    • Unusual permeability properties of gastric gland cells
    • Waisbren SJ, Geibel JP, Modlin IM, Boron WF (1994) Unusual permeability properties of gastric gland cells. Nature 368:332-335
    • (1994) Nature , vol.368 , pp. 332-335
    • Waisbren, S.J.1    Geibel, J.P.2    Modlin, I.M.3    Boron, W.F.4
  • 78
    • 0348140626 scopus 로고    scopus 로고
    • Renal and hepatic expression of the ammonium transporter proteins, Rh B glycoprotein and Rh C glycoprotein
    • Weiner D, Verlander JW (2003) Renal and hepatic expression of the ammonium transporter proteins, Rh B glycoprotein and Rh C glycoprotein. Acta Physiol Scand 179:331-338
    • (2003) Acta Physiol Scand , vol.179 , pp. 331-338
    • Weiner, D.1    Verlander, J.W.2
  • 79
    • 0037066722 scopus 로고    scopus 로고
    • Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter
    • Westhoff CM, Ferreri-Jacobia M, Mak DD, Foskett JK (2002) Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter. J Biol Chem 277:12499-12502
    • (2002) J Biol Chem , vol.277 , pp. 12499-12502
    • Westhoff, C.M.1    Ferreri-Jacobia, M.2    Mak, D.D.3    Foskett, J.K.4
  • 80
    • 32444446815 scopus 로고    scopus 로고
    • Amt/MEP/Rh proteins conduct ammonia
    • Winkler FK (2006) Amt/MEP/Rh proteins conduct ammonia. Pflügers Arch 451:701-707
    • (2006) Pflügers Arch , vol.451 , pp. 701-707
    • Winkler, F.K.1
  • 81
    • 34548615966 scopus 로고    scopus 로고
    • Aquaporins with selectivity for unconventional permeants
    • Wu B, Beitz E (2007) Aquaporins with selectivity for unconventional permeants. Cell Mol Life Sci 64:2413-2421
    • (2007) Cell Mol Life Sci , vol.64 , pp. 2413-2421
    • Wu, B.1    Beitz, E.2
  • 82
    • 0032540009 scopus 로고    scopus 로고
    • Urea transporter UT3 functions as an efficient water channel
    • Yang B,Verkman AS (1998) Urea transporter UT3 functions as an efficient water channel. J Biol Chem 273:9369-9372
    • (1998) J Biol Chem , vol.273 , pp. 9369-9372
    • Yang, B.1    Verkman, A.S.2
  • 84
    • 33748430962 scopus 로고    scopus 로고
    • Evidence from knockout mice against physiologically significant aquaporin 8-facilitated ammonia transport
    • Yang B, Zhao D, Solenov E, Verkman AS (2006a) Evidence from knockout mice against physiologically significant aquaporin 8-facilitated ammonia transport. Am J Physiol 291:C417-C423
    • (2006) Am J Physiol , vol.291
    • Yang, B.1    Zhao, D.2    Solenov, E.3    Verkman, A.S.4
  • 85
    • 33745206921 scopus 로고    scopus 로고
    • Evidence against functionally significant aquaporin expression in mitochondria
    • Yang B, Zhao D, Verkman AS (2006b) Evidence against functionally significant aquaporin expression in mitochondria. J Biol Chem 281:16202-16206
    • (2006) J Biol Chem , vol.281 , pp. 16202-16206
    • Yang, B.1    Zhao, D.2    Verkman, A.S.3
  • 87
    • 0027372483 scopus 로고    scopus 로고
    • You G, Smith CG, Kanai Y, LeeW-S, Steitzer M, HedigerMA (1993) Cloning and characterization of the vasopressin-regulated urea transporter. Nature 365:844-847
    • You G, Smith CG, Kanai Y, LeeW-S, Steitzer M, HedigerMA (1993) Cloning and characterization of the vasopressin-regulated urea transporter. Nature 365:844-847
  • 88
    • 21044445996 scopus 로고    scopus 로고
    • Phylogeny and evolution of the major intrinsic protein family
    • Zardoya R (2005) Phylogeny and evolution of the major intrinsic protein family. Biol Cell 97:397-414
    • (2005) Biol Cell , vol.97 , pp. 397-414
    • Zardoya, R.1
  • 90
    • 33645846619 scopus 로고    scopus 로고
    • +-coupled cotransporters of glucose (SGLT1) and of iodide (NIS). The dependence of substrate size studied at high resolution. J Physiol 570.3:485-499
    • +-coupled cotransporters of glucose (SGLT1) and of iodide (NIS). The dependence of substrate size studied at high resolution. J Physiol 570.3:485-499


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.