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Volumn 18, Issue 6-7, 2007, Pages 452-462

Comparative functional analysis of aquaporins/glyceroporins in mammals and anurans

Author keywords

[No Author keywords available]

Indexed keywords

AQUAGLYCEROPORIN; AQUAPORIN; AQUAPORIN 1; AQUAPORIN 2; AQUAPORIN 3; AQUAPORIN 4; AQUAPORIN 5; AQUAPORIN 6; AQUAPORIN 7; AQUAPORIN 8; AQUAPORIN 9;

EID: 34548394203     PISSN: 09388990     EISSN: 14321777     Source Type: Journal    
DOI: 10.1007/s00335-007-9041-5     Document Type: Review
Times cited : (76)

References (111)
  • 1
    • 0028335265 scopus 로고
    • Sequence and functional expression of an amphibian water channel, FA-CHIP: A new member of the MIP family
    • Abrami L, Simon M, Rousselet G, Berthonaud V, Buhler J-M, et al. (1994) Sequence and functional expression of an amphibian water channel, FA-CHIP: a new member of the MIP family. Biochim Biophys Acta 1192:147-151
    • (1994) Biochim Biophys Acta , vol.1192 , pp. 147-151
    • Abrami, L.1    Simon, M.2    Rousselet, G.3    Berthonaud, V.4    Buhler, J.-M.5
  • 2
    • 4544353285 scopus 로고    scopus 로고
    • Aquaporin water channels (Nobel lecture)
    • Agre P (2004) Aquaporin water channels (Nobel lecture). Angew Chem Int Ed Engl 43:4278-4290
    • (2004) Angew Chem Int Ed Engl , vol.43 , pp. 4278-4290
    • Agre, P.1
  • 3
    • 34447504997 scopus 로고    scopus 로고
    • Gene cloning and expression of an aquaporin, AQP-h3BL, in the basolateral membrane of water-permeable epithelial cells in osmoregulatory organs of the tree frog
    • Akabane G, Ogushi Y, Hasegawa T, Suzuki M, Tanaka S (2007) Gene cloning and expression of an aquaporin, AQP-h3BL, in the basolateral membrane of water-permeable epithelial cells in osmoregulatory organs of the tree frog. Am J Physiol Regul Integr Comp Physiol 292:R2340-2351
    • (2007) Am J Physiol Regul Integr Comp Physiol , vol.292 , pp. 2340-2351
    • Akabane, G.1    Ogushi, Y.2    Hasegawa, T.3    Suzuki, M.4    Tanaka, S.5
  • 4
    • 0033557376 scopus 로고    scopus 로고
    • Lung fluid transport in aquaporin-1 and aquaporin-4 knockout mice
    • Bai C, Fukuda N, Song Y, Ma T, Matthay MA, et al. (1999) Lung fluid transport in aquaporin-1 and aquaporin-4 knockout mice. J Clin Invest 103:555-561
    • (1999) J Clin Invest , vol.103 , pp. 555-561
    • Bai, C.1    Fukuda, N.2    Song, Y.3    Ma, T.4    Matthay, M.A.5
  • 5
    • 0035652639 scopus 로고    scopus 로고
    • Subcellular distribution of aquaporin 5 in salivary glands from Sjogren's syndrome
    • Beroukas D, Hiscock J, Jonsson R, Waterman SA, Gordon TP (2001) Subcellular distribution of aquaporin 5 in salivary glands from Sjogren's syndrome. Lancet 358:1875-1877
    • (2001) Lancet , vol.358 , pp. 1875-1877
    • Beroukas, D.1    Hiscock, J.2    Jonsson, R.3    Waterman, S.A.4    Gordon, T.P.5
  • 6
    • 0034118380 scopus 로고    scopus 로고
    • Missense mutations in MIP underlie autosomal dominant polymorphic and lamellar cataracts linked to 12q
    • Berry V, Francis P, Kaushal S, Moore A, Bhattacharya S (2000) Missense mutations in MIP underlie autosomal dominant polymorphic and lamellar cataracts linked to 12q. Nat Genet 25:15-17
    • (2000) Nat Genet , vol.25 , pp. 15-17
    • Berry, V.1    Francis, P.2    Kaushal, S.3    Moore, A.4    Bhattacharya, S.5
  • 7
    • 0035956936 scopus 로고    scopus 로고
    • Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli
    • Borgnia MJ, Agre P (2001) Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli. Proc Natl Acad Sci U S A. 98:2888-2893
    • (2001) Proc Natl Acad Sci U S A. , vol.98 , pp. 2888-2893
    • Borgnia, M.J.1    Agre, P.2
  • 8
    • 0017180861 scopus 로고
    • Glycerol transport in human red cells
    • Carlsen A, Wieth JO (1976) Glycerol transport in human red cells. Acta Phys Scand 97:501-513
    • (1976) Acta Phys Scand , vol.97 , pp. 501-513
    • Carlsen, A.1    Wieth, J.O.2
  • 10
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF
    • De Groot BL, Grubmüller H (2001) Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF. Science 294:2353-2357
    • (2001) Science , vol.294 , pp. 2353-2357
    • De Groot, B.L.1    Grubmüller, H.2
  • 11
    • 0028326794 scopus 로고
    • Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine
    • Deen PM, Verdijk MA, Knoers NV, Wieringa B, Monnens LA, et al. (1994) Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine. Science 264:92-95
    • (1994) Science , vol.264 , pp. 92-95
    • Deen, P.M.1    Verdijk, M.A.2    Knoers, N.V.3    Wieringa, B.4    Monnens, L.A.5
  • 13
    • 0031726939 scopus 로고    scopus 로고
    • Aquaporins (water channels): Role in vasopressin-activated water transport
    • Dibas AI, Mia AJ, Yorio T (1998) Aquaporins (water channels): role in vasopressin-activated water transport. Proc Soc Exp Biol Med 219:183-199
    • (1998) Proc Soc Exp Biol Med , vol.219 , pp. 183-199
    • Dibas, A.I.1    Mia, A.J.2    Yorio, T.3
  • 15
    • 0037232857 scopus 로고    scopus 로고
    • Artificial expression of aquaporin-3 improves the survival of mouse oocytes after cryopreservation
    • Edashige K, Yamaji Y, Kleinhans FW, Kasai M (2003) Artificial expression of aquaporin-3 improves the survival of mouse oocytes after cryopreservation. Biol Reprod 68:87-94
    • (2003) Biol Reprod , vol.68 , pp. 87-94
    • Edashige, K.1    Yamaji, Y.2    Kleinhans, F.W.3    Kasai, M.4
  • 16
    • 0028930178 scopus 로고
    • Cell volume measured by total internal reflection microfluorimetry: Application to water and solute transport in cells transfected with water channel homologs
    • Farinas J, Simanek V, Verkman AS (1995) Cell volume measured by total internal reflection microfluorimetry: application to water and solute transport in cells transfected with water channel homologs. Biophys J 68:1613-1620
    • (1995) Biophys J , vol.68 , pp. 1613-1620
    • Farinas, J.1    Simanek, V.2    Verkman, A.S.3
  • 17
    • 0034703396 scopus 로고    scopus 로고
    • Functional impairment of lens aquaporin in two families with dominantly inherited cataracts
    • Francis P, Chung JJ, Yasui M, Berry V, Moore A, et al. (2000) Functional impairment of lens aquaporin in two families with dominantly inherited cataracts. Hum Mol Genet 9:2329-2334
    • (2000) Hum Mol Genet , vol.9 , pp. 2329-2334
    • Francis, P.1    Chung, J.J.2    Yasui, M.3    Berry, V.4    Moore, A.5
  • 18
    • 0031777369 scopus 로고    scopus 로고
    • Prediction of functional residues in water channels and related proteins
    • Froger A, Tallur B, Thomas D, Delamarche C (1998) Prediction of functional residues in water channels and related proteins. Protein Sci 7:1458-1468
    • (1998) Protein Sci , vol.7 , pp. 1458-1468
    • Froger, A.1    Tallur, B.2    Thomas, D.3    Delamarche, C.4
  • 19
    • 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
  • 20
    • 33744978147 scopus 로고    scopus 로고
    • Aquaporin-11: A channel protein lacking apparent transport function expressed in brain
    • Gorelick DA, Praetorius J, Tsunerai T, Nielsen S, Agre P (2006) Aquaporin-11: A channel protein lacking apparent transport function expressed in brain. BMC Biochem 7:1-14
    • (2006) BMC Biochem , vol.7 , pp. 1-14
    • Gorelick, D.A.1    Praetorius, J.2    Tsunerai, T.3    Nielsen, S.4    Agre, P.5
  • 21
    • 0021712623 scopus 로고
    • The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning
    • Gorin MB, Yancey SB, Cline J, Revel JP, Horwitz J (1984) The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning. Cell 39:49-59
    • (1984) Cell , vol.39 , pp. 49-59
    • Gorin, M.B.1    Yancey, S.B.2    Cline, J.3    Revel, J.P.4    Horwitz, J.5
  • 22
    • 0036720421 scopus 로고    scopus 로고
    • Altering fish embryos with aquaporin-3: An essential step toward successful cryopreservation
    • Hagedorn M, Lance SL, Fonseca DM, Kleinhans FW (2002) Altering fish embryos with aquaporin-3: an essential step toward successful cryopreservation. Biol Reprod 67:961-966
    • (2002) Biol Reprod , vol.67 , pp. 961-966
    • Hagedorn, M.1    Lance, S.L.2    Fonseca, D.M.3    Kleinhans, F.W.4
  • 23
    • 0037195795 scopus 로고    scopus 로고
    • Selectively reduced glycerol in skin of aquaporin-3 deficient mice may account for impaired skin hydration, elasticity and barrier recovery
    • Hara M, Ma T, Verkman AS (2002) Selectively reduced glycerol in skin of aquaporin-3 deficient mice may account for impaired skin hydration, elasticity and barrier recovery. J Biol Chem 277:46616-46621
    • (2002) J Biol Chem , vol.277 , pp. 46616-46621
    • Hara, M.1    Ma, T.2    Verkman, A.S.3
  • 24
    • 33745292751 scopus 로고    scopus 로고
    • Physiological roles of glycerol-transporting aquaporins: The aquaglyceroporins
    • Hara-Chikuma M, Verkman AS (2006) Physiological roles of glycerol-transporting aquaporins: the aquaglyceroporins. 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
  • 25
    • 18144401213 scopus 로고    scopus 로고
    • Progressive adipocyte hypertrophy in aquaporin 7 deficient mice: Adipocyte glycerol permeability as a novel regulator of fat accumulation
    • Hara-Chikuma M, Sohara E, Rai T, Ikawa M, Okabe M, et al. (2005) Progressive adipocyte hypertrophy in aquaporin 7 deficient mice: adipocyte glycerol permeability as a novel regulator of fat accumulation. J Biol Chem 280:15493-15496
    • (2005) J Biol Chem , vol.280 , pp. 15493-15496
    • Hara-Chikuma, M.1    Sohara, E.2    Rai, T.3    Ikawa, M.4    Okabe, M.5
  • 26
    • 0042421729 scopus 로고    scopus 로고
    • Regulation of water absorption in the frog skins by two vasotocin-dependent water-channel aquaporins, AQP-h2 and AQP-h3
    • Hasegawa T, Tanii H, Suzuki M, Tanaka S (2003) Regulation of water absorption in the frog skins by two vasotocin-dependent water-channel aquaporins, AQP-h2 and AQP-h3. Endocrinology 144:4087-4096
    • (2003) Endocrinology , vol.144 , pp. 4087-4096
    • Hasegawa, T.1    Tanii, H.2    Suzuki, M.3    Tanaka, S.4
  • 27
    • 3042761281 scopus 로고    scopus 로고
    • Spatial and temporal expression of the ventral pelvic skin aquaporins during metamorphosis of the tree frog, Hyla japonica
    • Hasegawa T, Sugawara Y, Suzuki M, Tanaka S (2004) Spatial and temporal expression of the ventral pelvic skin aquaporins during metamorphosis of the tree frog, Hyla japonica. J Membr Biol 199:119-126
    • (2004) J Membr Biol , vol.199 , pp. 119-126
    • Hasegawa, T.1    Sugawara, Y.2    Suzuki, M.3    Tanaka, S.4
  • 28
    • 27944453911 scopus 로고    scopus 로고
    • Immunocytochemical studies on translocation of phosphorylated aquaporin-h2 protein in granular cells of the frog urinary bladder before and after stimulation with vasotocin
    • Hasegawa T, Suzuki M, Tanaka S (2005) Immunocytochemical studies on translocation of phosphorylated aquaporin-h2 protein in granular cells of the frog urinary bladder before and after stimulation with vasotocin. Cell Tissue Res 322:407-415
    • (2005) Cell Tissue Res , vol.322 , pp. 407-415
    • Hasegawa, T.1    Suzuki, M.2    Tanaka, S.3
  • 29
    • 0019195926 scopus 로고
    • The substrate specificity and transport properties of the glycerol facilitator of Escherichia coli
    • Heller KB, Lin EC, Wilson TH (1980) The substrate specificity and transport properties of the glycerol facilitator of Escherichia coli. J Bacteriol 144:274-278
    • (1980) J Bacteriol , vol.144 , pp. 274-278
    • Heller, K.B.1    Lin, E.C.2    Wilson, T.H.3
  • 30
    • 0034723156 scopus 로고    scopus 로고
    • Structural clues in the sequences of the aquaporins
    • Heymann JB, Engel A (2000) Structural clues in the sequences of the aquaporins. J Mol Biol 295:1039-1053
    • (2000) J Mol Biol , vol.295 , pp. 1039-1053
    • Heymann, J.B.1    Engel, A.2
  • 31
    • 23344437899 scopus 로고    scopus 로고
    • Aquaporin 7 deficiency is associated with development of obesity through activation of adipose glycerol kinase
    • Hibuse T, Maeda N, Funahashi T, Yamamoto K, Nagasawa A, et al. (2005) Aquaporin 7 deficiency is associated with development of obesity through activation of adipose glycerol kinase. Proc Natl Acad Sci U S A 102:10993-10998
    • (2005) Proc Natl Acad Sci U S a , vol.102 , pp. 10993-10998
    • Hibuse, T.1    Maeda, N.2    Funahashi, T.3    Yamamoto, K.4    Nagasawa, A.5
  • 32
    • 0034708617 scopus 로고    scopus 로고
    • Hypertonic induction of aquaporin-5 expression through an ERK-dependent pathway.
    • Hoffert JD, Leitch V, Agre P, King LS (2000) Hypertonic induction of aquaporin-5 expression through an ERK-dependent pathway. J Biol Chem 275:9070-9077
    • (2000) J Biol Chem , vol.275 , pp. 9070-9077
    • Hoffert, J.D.1    Leitch, V.2    Agre, P.3    King, L.S.4
  • 34
    • 0037131175 scopus 로고    scopus 로고
    • Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63
    • Ikeda M, Beitz E, Kozono D, Guggino WB, Agre P, et al. (2002) Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63. J Biol Chem 277:39873-39879
    • (2002) J Biol Chem , vol.277 , pp. 39873-39879
    • Ikeda, M.1    Beitz, E.2    Kozono, D.3    Guggino, W.B.4    Agre, P.5
  • 35
    • 0031590299 scopus 로고    scopus 로고
    • Immunolocalization of aquaporin homologs in mouse lacrimal glands
    • Ishida N, Hirai SI, Mita S (1997) Immunolocalization of aquaporin homologs in mouse lacrimal glands. Biochem Biophys Res Commun 238:891-895
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 891-895
    • Ishida, N.1    Hirai, S.I.2    Mita, S.3
  • 36
    • 0033547393 scopus 로고    scopus 로고
    • Alpha(1)-adrenoceptor-induced trafficking of aquapoin-5 to the apical plasma membrane of rat parotid cells
    • Ishikawa Y, Skowronshi MT, Inoue N, Ishida H (1998) Alpha(1)- adrenoceptor-induced trafficking of aquapoin-5 to the apical plasma membrane of rat parotid cells. Biochem Biophys Res Commun 265:194-200
    • (1998) Biochem Biophys Res Commun , vol.265 , pp. 194-200
    • Ishikawa, Y.1    Skowronshi, M.T.2    Inoue, N.3    Ishida, H.4
  • 37
    • 0036262411 scopus 로고    scopus 로고
    • The muscarinic acetylcholine receptor-stimulated increase in aquaporin 5 levels in the apical plasma membrane in rat parotid acinar cells is coupled with activation of nitric oxide/ cGMP signal transduction
    • Ishikawa Y, Iida H, Ishida H (2002) The muscarinic acetylcholine receptor-stimulated increase in aquaporin 5 levels in the apical plasma membrane in rat parotid acinar cells is coupled with activation of nitric oxide/ cGMP signal transduction. Mol Pharmacol 61:1423-1434
    • (2002) Mol Pharmacol , vol.61 , pp. 1423-1434
    • Ishikawa, Y.1    Iida, H.2    Ishida, H.3
  • 38
    • 16244383536 scopus 로고    scopus 로고
    • Identification of a novel aquaporin AQP12, expressed in pancreatic acinar cells
    • Itoh T, Rai T, Kuwahara M, Ko SBH, Uchida S, et al. (2005) Identification of a novel aquaporin AQP12, expressed in pancreatic acinar cells. Biochem Biophys Res Commun 330:832-838
    • (2005) Biochem Biophys Res Commun , vol.330 , pp. 832-838
    • Itoh, T.1    Rai, T.2    Kuwahara, M.3    Ko, S.B.H.4    Uchida, S.5
  • 39
    • 0028318868 scopus 로고
    • Molecular structure of the water channel through aquaporin CHIP. the hourglass model
    • Jung JS, Preston GM, Smith BL, Guggino WB, Agre P (1994) Molecular structure of the water channel through aquaporin CHIP. The hourglass model. J Biol Chem 269:14648-14654
    • (1994) J Biol Chem , vol.269 , pp. 14648-14654
    • Jung, J.S.1    Preston, G.M.2    Smith, B.L.3    Guggino, W.B.4    Agre, P.5
  • 40
    • 0030013048 scopus 로고    scopus 로고
    • Aquaporin-1 water channel protein in lung: Ontogeny, steroid-induced expression, and distribution in rat
    • King LS, Nielsen S, Agre P (1996) Aquaporin-1 water channel protein in lung: ontogeny, steroid-induced expression, and distribution in rat. J Clin Invest 97:2183-2191
    • (1996) J Clin Invest , vol.97 , pp. 2183-2191
    • King, L.S.1    Nielsen, S.2    Agre, P.3
  • 41
    • 0035913207 scopus 로고    scopus 로고
    • Defective urinary-concentrating ability due to a complete deficiency of aquaporin -1
    • King LS, Choi M, Fernandez PC, Cartron JP, Agre P (2001) Defective urinary-concentrating ability due to a complete deficiency of aquaporin -1. New Engl J Med 345:175-179
    • (2001) New Engl J Med , vol.345 , pp. 175-179
    • King, L.S.1    Choi, M.2    Fernandez, P.C.3    Cartron, J.P.4    Agre, P.5
  • 42
    • 0037154182 scopus 로고    scopus 로고
    • Decreased pulmonary vascular permeability in aquaporin-1-null humans
    • King LS, Nielsen S, Agre P, Brown RH (2002) Decreased pulmonary vascular permeability in aquaporin-1-null humans. Proc Natl Acad Sci USA 99:1059-1063
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1059-1063
    • King, L.S.1    Nielsen, S.2    Agre, P.3    Brown, R.H.4
  • 43
    • 0029775026 scopus 로고    scopus 로고
    • Quantitation of aquaporin-2 abundance in microdissected collecting ducts: Axial distribution and control by AVP
    • Kishore BK, Terris JM, Knepper MA (1996) Quantitation of aquaporin-2 abundance in microdissected collecting ducts: Axial distribution and control by AVP. Am J Physiol 271:F62-F70
    • (1996) Am J Physiol , vol.271
    • Kishore, B.K.1    Terris, J.M.2    Knepper, M.A.3
  • 44
    • 0035661085 scopus 로고    scopus 로고
    • Molecular and cellular defects in nephrogenic diabetes insipidus
    • Knoers NV, Deen PM (2001) Molecular and cellular defects in nephrogenic diabetes insipidus. Pediatr Nephrol 16:1146-1152
    • (2001) Pediatr Nephrol , vol.16 , pp. 1146-1152
    • Knoers, N.V.1    Deen, P.M.2
  • 45
    • 0037729269 scopus 로고    scopus 로고
    • Aquaporins: Membrane water channels of the biological world
    • Krane CM, Kishore BK (2003) Aquaporins: membrane water channels of the biological world. Biologist 50:81-86
    • (2003) Biologist , vol.50 , pp. 81-86
    • Krane, C.M.1    Kishore, B.K.2
  • 47
    • 0035968332 scopus 로고    scopus 로고
    • Salivary acinar cells from aquaporin 5-deficient mice have decreased membrane water permeability and altered cell volume regulation
    • 26
    • Krane CM, Melvin JE, Nguyen HV, Richardson L, Towne JE, et al. (2001b) Salivary acinar cells from aquaporin 5-deficient mice have decreased membrane water permeability and altered cell volume regulation. J Biol Chem. 276(26):23413-23420
    • (2001) J Biol Chem. , vol.276 , pp. 23413-23420
    • Krane, C.M.1    Melvin, J.E.2    Nguyen, H.V.3    Richardson, L.4    Towne, J.E.5
  • 48
    • 0031714294 scopus 로고    scopus 로고
    • Sensitivity of kidney perfusion protocol design to physical and physiological parameters
    • Lachenbruch CA, Diller KR, Pegg DE (1998) Sensitivity of kidney perfusion protocol design to physical and physiological parameters. Ann N Y Acad Sci 858:298-309
    • (1998) Ann N Y Acad Sci , vol.858 , pp. 298-309
    • Lachenbruch, C.A.1    Diller, K.R.2    Pegg, D.E.3
  • 49
    • 0028835866 scopus 로고
    • + symport in the halotolerant yeast Pichia sorbitolophila
    • + symport in the halotolerant yeast Pichia sorbitolophila. Yeast 11:111-119
    • (1995) Yeast , vol.11 , pp. 111-119
    • Lages, F.1    Lucas, C.2
  • 50
    • 0032524648 scopus 로고    scopus 로고
    • A yeast recombinant aquaporin mutant that is not expressed or mistargeted in Xenopus oocyte can be functionally analyzed in reconstituted proteoliposomes
    • Lagree V, Pellerin I, Hubert JF, Tacnet F, Le Caherec F, et al. (1998) A yeast recombinant aquaporin mutant that is not expressed or mistargeted in Xenopus oocyte can be functionally analyzed in reconstituted proteoliposomes. J Biol Chem 273:12422-12426
    • (1998) J Biol Chem , vol.273 , pp. 12422-12426
    • Lagree, V.1    Pellerin, I.2    Hubert, J.F.3    Tacnet, F.4    Le Caherec, F.5
  • 51
    • 0033548466 scopus 로고    scopus 로고
    • Switch from an aquaporin to a glycerol channel by two amino acids substitution
    • Lagree V, Froger A, Deschamps S, Hubert JF, Delamarche C, et al. (1999) Switch from an aquaporin to a glycerol channel by two amino acids substitution. J Biol Chem 274:6817-6819
    • (1999) J Biol Chem , vol.274 , pp. 6817-6819
    • Lagree, V.1    Froger, A.2    Deschamps, S.3    Hubert, J.F.4    Delamarche, C.5
  • 52
    • 0030424749 scopus 로고    scopus 로고
    • Post-hibernation excretion of glucose in urine of the freeze tolerant frog Rana sylvatica
    • Layne JR, Lee RE, Cutwa MM (1996) Post-hibernation excretion of glucose in urine of the freeze tolerant frog Rana sylvatica. J Herp 30:85-87
    • (1996) J Herp , vol.30 , pp. 85-87
    • Layne, J.R.1    Lee, R.E.2    Cutwa, M.M.3
  • 53
    • 0008237137 scopus 로고
    • Integrated physiological responses promoting anuran freeze tolerance
    • Carey C, et al. (eds.) (Boulder, CO: Westview Press)
    • Lee RE, Costanzo JP (1993) Integrated physiological responses promoting anuran freeze tolerance. In: Life in the Cold, Carey C, et al. (eds.) (Boulder, CO: Westview Press), pp 501-510
    • (1993) Life in the Cold , pp. 501-510
    • Lee, R.E.1    Costanzo, J.P.2
  • 54
    • 0021029839 scopus 로고
    • Glycerol transport and phosphorylation by rat hepatocytes
    • Li C-C, Lin EC (1983) Glycerol transport and phosphorylation by rat hepatocytes. J Cell Physiol 117:230-234
    • (1983) J Cell Physiol , vol.117 , pp. 230-234
    • Li, C.-C.1    Lin, E.C.2
  • 55
    • 0035903098 scopus 로고    scopus 로고
    • Impaired hearing in mice lacking aquaporin-4 water channels
    • Li J, Verkman AS (2001) Impaired hearing in mice lacking aquaporin-4 water channels. J Biol Chem 276:31233-31237
    • (2001) J Biol Chem , vol.276 , pp. 31233-31237
    • Li, J.1    Verkman, A.S.2
  • 57
    • 0242332305 scopus 로고    scopus 로고
    • Glycerol conductance and physical asymmetry of the Escherichia coli glycerol facilitator GlpF
    • Lu D, Grayson P, Schulten K (2003) Glycerol conductance and physical asymmetry of the Escherichia coli glycerol facilitator GlpF. Biophys J 85:2977-2987
    • (2003) Biophys J , vol.85 , pp. 2977-2987
    • Lu, D.1    Grayson, P.2    Schulten, K.3
  • 58
    • 84990703755 scopus 로고
    • Osmoregulatory active sodium-glycerol co-transport in the halotolerant yeast Debaryomyces hansenii.
    • Lucas C, Costa MD, VanUden N (1990) Osmoregulatory active sodium-glycerol co-transport in the halotolerant yeast Debaryomyces hansenii. Yeast 6:187-192
    • (1990) Yeast , vol.6 , pp. 187-192
    • Lucas, C.1    Costa, M.D.2    Vanuden, N.3
  • 59
    • 0029852885 scopus 로고    scopus 로고
    • CDNA cloning of a functional water channel from toad urinary bladder epithelium
    • Ma T, Baoxue Y, Verkman AS (1996) cDNA cloning of a functional water channel from toad urinary bladder epithelium. Am J Phys 271:C1699-C1704
    • (1996) Am J Phys , vol.271
    • Ma, T.1    Baoxue, Y.2    Verkman, A.S.3
  • 60
    • 0030955183 scopus 로고    scopus 로고
    • Generation and phenotype of a transgenic knockout mouse lacking the mercurial-insensitive water channel aquaporin-4
    • Ma T, Yang B, Gillespie A, Carlson EJ, Epstein CJ, et al. (1997) Generation and phenotype of a transgenic knockout mouse lacking the mercurial-insensitive water channel aquaporin-4. J Clin Invest 100:957-962
    • (1997) J Clin Invest , vol.100 , pp. 957-962
    • Ma, T.1    Yang, B.2    Gillespie, A.3    Carlson, E.J.4    Epstein, C.J.5
  • 61
    • 0032549031 scopus 로고    scopus 로고
    • Severely impaired urinary concentrating ability in transgenic mice lacking aquaporin-1 water channels
    • Ma T, Yang B, Gillespie A, Carlson EJ, Epstein CJ, et al. (1998) Severely impaired urinary concentrating ability in transgenic mice lacking aquaporin-1 water channels. J Biol Chem 273:4296-4299
    • (1998) J Biol Chem , vol.273 , pp. 4296-4299
    • Ma, T.1    Yang, B.2    Gillespie, A.3    Carlson, E.J.4    Epstein, C.J.5
  • 62
    • 0033575326 scopus 로고    scopus 로고
    • Defective secretion of saliva in transgenic mice lacking aquaporin-5 water channels
    • Ma T, Song Y, Gillespie A, Carlson EJ, Epstein CJ, Verkman AS (1999) Defective secretion of saliva in transgenic mice lacking aquaporin-5 water channels. J Biol Chem 274:20071-20074
    • (1999) J Biol Chem , vol.274 , pp. 20071-20074
    • Ma, T.1    Song, Y.2    Gillespie, A.3    Carlson, E.J.4    Epstein, C.J.5    Verkman, A.S.6
  • 64
    • 0034636160 scopus 로고    scopus 로고
    • Nephrogenic diabetes insipidus in mice lacking aquaporin-3 water channels
    • Ma T, Song Y, Yang B, Gillespie A, Carlson EJ, et al. (2000b) Nephrogenic diabetes insipidus in mice lacking aquaporin-3 water channels. Proc Natl Acad Sci U S A 97:4386-4391
    • (2000) Proc Natl Acad Sci U S a , vol.97 , pp. 4386-4391
    • Ma, T.1    Song, Y.2    Yang, B.3    Gillespie, A.4    Carlson, E.J.5
  • 65
    • 0037053303 scopus 로고    scopus 로고
    • Impaired stratum corneum hydration in mice lacking epidermal water channel aquaporin-3
    • Ma T, Hara M, Sougrat R, Verbavatz JM, Verkman AS (2002) Impaired stratum corneum hydration in mice lacking epidermal water channel aquaporin-3. J Biol Chem 277:17147-17153
    • (2002) J Biol Chem , vol.277 , pp. 17147-17153
    • Ma, T.1    Hara, M.2    Sougrat, R.3    Verbavatz, J.M.4    Verkman, A.S.5
  • 66
    • 0033966090 scopus 로고    scopus 로고
    • Aquaporin-4 deletion in mice reduces brain edema after acute water intoxication and ischemic stroke
    • Manley GT, Fujimura M, Ma T, Noshita N, Filiz F, et al. (2000) Aquaporin-4 deletion in mice reduces brain edema after acute water intoxication and ischemic stroke. Nat Med 6:159-163
    • (2000) Nat Med , vol.6 , pp. 159-163
    • Manley, G.T.1    Fujimura, M.2    Ma, T.3    Noshita, N.4    Filiz, F.5
  • 67
    • 0028200818 scopus 로고
    • Functional characterization of the Escherichia coli glycerol facilitator, GlpF,in Xenopus oocytes
    • Maurel C, Reizer J, Schroeder JI, Chrispeels MJ, Saier MH Jr (1994) Functional characterization of the Escherichia coli glycerol facilitator, GlpF,in Xenopus oocytes. J Biol Chem 269:11869-11872
    • (1994) J Biol Chem , vol.269 , pp. 11869-11872
    • Maurel, C.1    Reizer, J.2    Schroeder, J.I.3    Chrispeels, M.J.4    Saier Jr., M.H.5
  • 68
    • 0033757195 scopus 로고    scopus 로고
    • Developmental expression of aquaporin 2 in the mouse inner ear
    • Merves M, Bobbitt B, Parker K, Kishore BK, Choo D (2000) Developmental expression of aquaporin 2 in the mouse inner ear. Laryngoscope 110:192-1930
    • (2000) Laryngoscope , vol.110 , pp. 192-1930
    • Merves, M.1    Bobbitt, B.2    Parker, K.3    Kishore, B.K.4    Choo, D.5
  • 69
    • 10944255127 scopus 로고    scopus 로고
    • Molecular mechanisms and drug development in aquaporin water channel diseases: Aquaporin superfamily (superaquaporins): Expansion of aquaporins restricted to multicellular organisms
    • Morishita Y, Sakube Y, Sasaki S, Ishibashi K (2004) Molecular mechanisms and drug development in aquaporin water channel diseases: aquaporin superfamily (superaquaporins): expansion of aquaporins restricted to multicellular organisms. J Pharmacol Sci 96:276-279
    • (2004) J Pharmacol Sci , vol.96 , pp. 276-279
    • Morishita, Y.1    Sakube, Y.2    Sasaki, S.3    Ishibashi, K.4
  • 70
    • 23844498483 scopus 로고    scopus 로고
    • Disruption of aquaporin-11 produces polycystic kidneys following vacuolization of the proximal tubule
    • Morishita Y, Matsuzaki T, Hara-Chikuma M, Andoo A, Shimono M, et al. (2005) Disruption of aquaporin-11 produces polycystic kidneys following vacuolization of the proximal tubule. Mol Cell Biol 25:7770-7779
    • (2005) Mol Cell Biol , vol.25 , pp. 7770-7779
    • Morishita, Y.1    Matsuzaki, T.2    Hara-Chikuma, M.3    Andoo, A.4    Shimono, M.5
  • 71
    • 33846537977 scopus 로고    scopus 로고
    • Nitric oxide decreases cell surface expression of aquaporin-5 and membrane water permeability in lung epithelial cells
    • Nagai K, Watanabe M, Seto M, Hisatsune A, Miyata T, et al. (2007) Nitric oxide decreases cell surface expression of aquaporin-5 and membrane water permeability in lung epithelial cells. Biochem Biophys Res Commun 354:579-584
    • (2007) Biochem Biophys Res Commun , vol.354 , pp. 579-584
    • Nagai, K.1    Watanabe, M.2    Seto, M.3    Hisatsune, A.4    Miyata, T.5
  • 73
    • 0031827765 scopus 로고    scopus 로고
    • Expression of an AQP2 Cre recombinase transgene in kidney and male reproductive system of transgenic mice
    • Nelson RD, Stricklett P, Gustafson C, Stevens A, Ausiello D, et al. (1998) Expression of an AQP2 Cre recombinase transgene in kidney and male reproductive system of transgenic mice. Am J Physiol 275:C216-C226
    • (1998) Am J Physiol , vol.275
    • Nelson, R.D.1    Stricklett, P.2    Gustafson, C.3    Stevens, A.4    Ausiello, D.5
  • 74
    • 0028889112 scopus 로고
    • Vasopressing increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane
    • Nielsen S, Chou C-L, Marples D, Chirstensen EI, Kishore BK, et al. (1995) Vasopressing increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane. Proc Natl Acad Sci U S A 92:1013-1017
    • (1995) Proc Natl Acad Sci U S a , vol.92 , pp. 1013-1017
    • Nielsen, S.1    Chou, C.-L.2    Marples, D.3    Chirstensen, E.I.4    Kishore, B.K.5
  • 75
    • 0020619394 scopus 로고
    • Radioimmunoassay of arginine vasotocin and mesotocin in serum of the frog Rana ridibunda
    • Nouwen EJ, Kuhn ER (1983) Radioimmunoassay of arginine vasotocin and mesotocin in serum of the frog Rana ridibunda. Gen Comp Endocrinol 50:242-251
    • (1983) Gen Comp Endocrinol , vol.50 , pp. 242-251
    • Nouwen, E.J.1    Kuhn, E.R.2
  • 76
    • 0020973003 scopus 로고
    • Evolution of control of epithelial transport in vertebrates
    • Pang PKT (1983) Evolution of control of epithelial transport in vertebrates. J Exp Biol 106:283-299
    • (1983) J Exp Biol , vol.106 , pp. 283-299
    • Pang, P.K.T.1
  • 78
    • 0029910115 scopus 로고    scopus 로고
    • Phylogenetics characterization of the MIP family of transmembrane channel proteins
    • Park JH, Saier MH Jr (1996) Phylogenetics characterization of the MIP family of transmembrane channel proteins. J Membr Biol 153:171-180
    • (1996) J Membr Biol , vol.153 , pp. 171-180
    • Park, J.H.1    Saier Jr., M.H.2
  • 80
    • 0026332210 scopus 로고
    • Isolation of a cDNA from erythrocyte integral membrane protein of 28 kilodalton: Member of an ancient channel family
    • Preston GM, Agre P (1991) Isolation of a cDNA from erythrocyte integral membrane protein of 28 kilodalton: member of an ancient channel family. Proc Nat Acad Sci U S A 88:11110-11114
    • (1991) Proc Nat Acad Sci U S a , vol.88 , pp. 11110-11114
    • Preston, G.M.1    Agre, P.2
  • 81
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 proteins
    • Preston GM, Carroll TP, Guggino WB, Agre P (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 proteins. Science 256:385-387
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 82
    • 0027472168 scopus 로고
    • The mercury-sensitive residue at cysteine 189 in the CHIP 28 water channel
    • Preston GM, Jung JS, Guggino WB, Agre P (1993) The mercury-sensitive residue at cysteine 189 in the CHIP 28 water channel. J Biol Chem 268:17-20
    • (1993) J Biol Chem , vol.268 , pp. 17-20
    • Preston, G.M.1    Jung, J.S.2    Guggino, W.B.3    Agre, P.4
  • 83
    • 33645809329 scopus 로고    scopus 로고
    • Severe urinary concentrating defect in renal collecting duct-selective AQP2 conditional-knockout mice
    • Rojek A, Fuchtbauer EM, Kwon TH, Frokiaer J, Nielsen S (2006) Severe urinary concentrating defect in renal collecting duct-selective AQP2 conditional-knockout mice. Proc Natl Acad Sci U S A 103:6037-6042
    • (2006) Proc Natl Acad Sci U S a , vol.103 , pp. 6037-6042
    • Rojek, A.1    Fuchtbauer, E.M.2    Kwon, T.H.3    Frokiaer, J.4    Nielsen, S.5
  • 84
    • 0016277588 scopus 로고
    • Radioimmunoassay of arginine vasotocin
    • Rosenbloom AA, Fisher DA (1974) Radioimmunoassay of arginine vasotocin. Endocrinology 95:1726-1732
    • (1974) Endocrinology , vol.95 , pp. 1726-1732
    • Rosenbloom, A.A.1    Fisher, D.A.2
  • 85
    • 17144379334 scopus 로고    scopus 로고
    • Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption
    • Saadoun S, Papadopoulos MC, Hara-Chikuma M, Verkman AS (2005) Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption. Nature 434:786-792
    • (2005) Nature , vol.434 , pp. 786-792
    • Saadoun, S.1    Papadopoulos, M.C.2    Hara-Chikuma, M.3    Verkman, A.S.4
  • 86
    • 34247104106 scopus 로고    scopus 로고
    • Fast and selective ammonia transport by aquaporin-8
    • Saparov SM, 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, S.M.1    Liu, K.2    Agre, P.3    Pohl, P.4
  • 87
    • 0034705704 scopus 로고    scopus 로고
    • Aquaporin 3 cloned from Xenopus laevis is regulated by the cystic fibrosis transmembrane conductance regulator
    • Schreiber R, Pavenstadt H, Greger R, Kunzelmann K (2000) Aquaporin 3 cloned from Xenopus laevis is regulated by the cystic fibrosis transmembrane conductance regulator. FEBS Lett 475:291-295
    • (2000) FEBS Lett , vol.475 , pp. 291-295
    • Schreiber, R.1    Pavenstadt, H.2    Greger, R.3    Kunzelmann, K.4
  • 88
    • 0030031158 scopus 로고    scopus 로고
    • Mutations in the founder of the MIP gene family underlie cataract development in the mouse
    • Shiels A, Bassnett S (1996) Mutations in the founder of the MIP gene family underlie cataract development in the mouse. Nat Genet 12:212-215
    • (1996) Nat Genet , vol.12 , pp. 212-215
    • Shiels, A.1    Bassnett, S.2
  • 89
    • 0035798592 scopus 로고    scopus 로고
    • Aquaporin-5 dependent fluid secretion in airway submucosal glands
    • Song Y, Verkman AS (2001) Aquaporin-5 dependent fluid secretion in airway submucosal glands. J Biol Chem 276:41288-41292
    • (2001) J Biol Chem , vol.276 , pp. 41288-41292
    • Song, Y.1    Verkman, A.S.2
  • 90
    • 0034745705 scopus 로고    scopus 로고
    • Abnormal distribution of aquaporin-5 water channel protein in salivary glands from Sjogren's syndrome patients
    • Steinfeld S, Cogan E, King LS, Agre P, Kiss R, et al. (2001) Abnormal distribution of aquaporin-5 water channel protein in salivary glands from Sjogren's syndrome patients. Lab Invest 81:143-148
    • (2001) Lab Invest , vol.81 , pp. 143-148
    • Steinfeld, S.1    Cogan, E.2    King, L.S.3    Agre, P.4    Kiss, R.5
  • 91
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui H, Han B-G, Lee JK, Walian P, Jap BK (2001) Structural basis of water-specific transport through the AQP1 water channel. Nature 414:872-878
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.-G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 93
    • 0037134267 scopus 로고    scopus 로고
    • Control of the selectivity of the aquaporin water channel family by global orientational tuning
    • Tajkhorshid E, Nollert P, Jensen MO, Miercke LJ, O'Connell J, et al. (2002) Control of the selectivity of the aquaporin water channel family by global orientational tuning. Science 296:525-530
    • (2002) Science , vol.296 , pp. 525-530
    • Tajkhorshid, E.1    Nollert, P.2    Jensen, M.O.3    Miercke, L.J.4    O'Connell, J.5
  • 94
    • 0036952087 scopus 로고    scopus 로고
    • Aquaporin expression correlates with freeze tolerance in baker's yeast, and overexpression improves freeze tolerance in industrial strains
    • Tanghe A, Van Dijck P, Dumortier F, Teunissen A, Hohmann S, et al. (2002) Aquaporin expression correlates with freeze tolerance in baker's yeast, and overexpression improves freeze tolerance in industrial strains. Appl Environ Microbiol 6:5981-5989
    • (2002) Appl Environ Microbiol , vol.6 , pp. 5981-5989
    • Tanghe, A.1    Van Dijck, P.2    Dumortier, F.3    Teunissen, A.4    Hohmann, S.5
  • 96
    • 0036628858 scopus 로고    scopus 로고
    • Molecular and cellular characterization of a water-channel protein, AQP-h3, specifically expressed in the frog ventral skin
    • Tanii H, Hasegawa T, Hirakawa N, Suzuki M, Tanaka S (2002) Molecular and cellular characterization of a water-channel protein, AQP-h3, specifically expressed in the frog ventral skin. J Membr Biol 188:43-53
    • (2002) J Membr Biol , vol.188 , pp. 43-53
    • Tanii, H.1    Hasegawa, T.2    Hirakawa, N.3    Suzuki, M.4    Tanaka, S.5
  • 98
    • 0035377194 scopus 로고    scopus 로고
    • Tumor necrosis factor-β inhibits aquaporin 5 expression in mouse lung epithelial cells
    • Towne JE, Krane CM, Bachurski CJ, Menon AG (2001) Tumor necrosis factor-β inhibits aquaporin 5 expression in mouse lung epithelial cells. J Biol Chem 276:18657-18664
    • (2001) J Biol Chem , vol.276 , pp. 18657-18664
    • Towne, J.E.1    Krane, C.M.2    Bachurski, C.J.3    Menon, A.G.4
  • 99
    • 0035799116 scopus 로고    scopus 로고
    • Defective cellular trafficking of lacrimal gland aquaporin-5 in Sjogren's syndrome
    • Tsubota K (2001) Defective cellular trafficking of lacrimal gland aquaporin-5 in Sjogren's syndrome. Lancet 357:688-689
    • (2001) Lancet , vol.357 , pp. 688-689
    • Tsubota, K.1
  • 100
    • 0028342916 scopus 로고
    • Sites of action of arginine vasotocin in the nephron of the bullfrog kidney
    • Uchiyama M (1994) Sites of action of arginine vasotocin in the nephron of the bullfrog kidney. Gen Comp Endocrinol 94:366-373
    • (1994) Gen Comp Endocrinol , vol.94 , pp. 366-373
    • Uchiyama, M.1
  • 101
    • 0030956447 scopus 로고    scopus 로고
    • Evidence for a phloretin-sensitive glycerol transport mechanism in the perfused rat liver
    • Vom Dahl S, Häussinger D (1997) Evidence for a phloretin-sensitive glycerol transport mechanism in the perfused rat liver. Am J Physiol 272:G563-G574
    • (1997) Am J Physiol , vol.272
    • Vom Dahl, S.1    Häussinger, D.2
  • 102
    • 0037175047 scopus 로고    scopus 로고
    • Cloning and functional characterization of a novel aquaporin from Xenopus laevis oocytes
    • Virkki LV, Franke C, Somieski P, Boron WF (2002) Cloning and functional characterization of a novel aquaporin from Xenopus laevis oocytes. J Biol Chem 277:40610-40616
    • (2002) J Biol Chem , vol.277 , pp. 40610-40616
    • Virkki, L.V.1    Franke, C.2    Somieski, P.3    Boron, W.F.4
  • 103
    • 0024409008 scopus 로고
    • Dynamics of apical membrane responses to ADH in amphibian bladder
    • Wade JB (1989) Dynamics of apical membrane responses to ADH in amphibian bladder. Am J Physiol 257:R998-R1003
    • (1989) Am J Physiol , vol.257
    • Wade, J.B.1
  • 104
    • 0019732284 scopus 로고
    • ADH action: Evidence for a membrane shuttle mechanism
    • Wade JB, Stetson DL, Lewis SA (1981) ADH action: evidence for a membrane shuttle mechanism. Ann N Y Acad Sci 372:106-117
    • (1981) Ann N Y Acad Sci , vol.372 , pp. 106-117
    • Wade, J.B.1    Stetson, D.L.2    Lewis, S.A.3
  • 105
    • 0042858145 scopus 로고    scopus 로고
    • Cyclic AMP regulates aquaporin 5 expression at both transcriptional and post-transcriptional levels through a protein kinase a pathway
    • Yang F, Kawedia JD, Menon AG (2003) Cyclic AMP regulates aquaporin 5 expression at both transcriptional and post-transcriptional levels through a protein kinase A pathway. J Biol Chem 278:32173-32180
    • (2003) J Biol Chem , vol.278 , pp. 32173-32180
    • Yang, F.1    Kawedia, J.D.2    Menon, A.G.3
  • 107
    • 0033547240 scopus 로고    scopus 로고
    • Rapid gating and anion permeability of an intracellular aquaporin
    • Yasui M, Hazama A, Kwon TH, Nielsen S, Guggino WB, et al. (1999) Rapid gating and anion permeability of an intracellular aquaporin. Nature 402:184-187
    • (1999) Nature , vol.402 , pp. 184-187
    • Yasui, M.1    Hazama, A.2    Kwon, T.H.3    Nielsen, S.4    Guggino, W.B.5
  • 108
    • 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
  • 109
    • 0026806764 scopus 로고
    • Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
    • Zeidel ML, Ambudkar SV, Smith BL, Agre P (1992) Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein. Biochemistry 31:7436-7440
    • (1992) Biochemistry , vol.31 , pp. 7436-7440
    • Zeidel, M.L.1    Ambudkar, S.V.2    Smith, B.L.3    Agre, P.4
  • 110
    • 0027503110 scopus 로고
    • A point mutation at cysteine 189 blocks the water permeability of rat kidney water channel CHIP28k
    • Zhang R, van Hoek AN, Biwersi J, Verkman AS (1993) A point mutation at cysteine 189 blocks the water permeability of rat kidney water channel CHIP28k. Biochemistry 32:2938-2941
    • (1993) Biochemistry , vol.32 , pp. 2938-2941
    • Zhang, R.1    Van Hoek, A.N.2    Biwersi, J.3    Verkman, A.S.4
  • 111
    • 33846127793 scopus 로고    scopus 로고
    • Excretion and conservation of glycerol, and expression of aquaporins and glyceroporins, during cold acclimation in Cope's gray tree frog Hyla chrysoscelis
    • Zimmerman SL, Frisbie J, Goldstein DL, West J, Rivera K, et al. (2007) Excretion and conservation of glycerol, and expression of aquaporins and glyceroporins, during cold acclimation in Cope's gray tree frog Hyla chrysoscelis. Am J Physiol Regul Integr Comp Physiol 292:R544-R555
    • (2007) Am J Physiol Regul Integr Comp Physiol , vol.292
    • Zimmerman, S.L.1    Frisbie, J.2    Goldstein, D.L.3    West, J.4    Rivera, K.5


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