메뉴 건너뛰기




Volumn 39, Issue 1, 2004, Pages 1-83

Aquaporins: Water channel proteins of the cell membrane

Author keywords

Antidiuretic hormone; AQP; AQP1; AQP2; AQP3; Aquaporin; Cell membrane; Epithelium; Kidney; Knockout experiment; Secretion; Water channel; Water transfer

Indexed keywords

AQUAPORIN; AQUAPORIN 1; AQUAPORIN 10; AQUAPORIN 2; AQUAPORIN 3; AQUAPORIN 4; AQUAPORIN 5; AQUAPORIN 6; AQUAPORIN 7; AQUAPORIN 8; AQUAPORIN 9; COTRANSPORTER; GREEN FLUORESCENT PROTEIN; PROTEIN; UNCLASSIFIED DRUG; VASOPRESSIN; WATER;

EID: 3042709008     PISSN: 00796336     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.proghi.2004.03.001     Document Type: Article
Times cited : (357)

References (331)
  • 1
    • 0035494421 scopus 로고    scopus 로고
    • In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4
    • Adams M.E., Mueller H.A., Froehner S.C. In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4. J. Cell Biol. 155:2001;113-122
    • (2001) J. Cell Biol. , vol.155 , pp. 113-122
    • Adams, M.E.1    Mueller, H.A.2    Froehner, S.C.3
  • 3
    • 0027431432 scopus 로고
    • Aquaporins: A family of water channel proteins
    • Agre P., Sasaki S., Chrispeels M.J. Aquaporins. a family of water channel proteins Am. J. Physiol. 265:1993;F461
    • (1993) Am. J. Physiol. , vol.265 , pp. 461
    • Agre, P.1    Sasaki, S.2    Chrispeels, M.J.3
  • 4
    • 0029151790 scopus 로고
    • Aquaporin water channels: Unanswered questions and unresolved controversies
    • Agre P., Brown D., Nielsen S. Aquaporin water channels. unanswered questions and unresolved controversies Curr. Opin. Cell Biol. 7:1995;472-483
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 472-483
    • Agre, P.1    Brown, D.2    Nielsen, S.3
  • 5
    • 0032510966 scopus 로고    scopus 로고
    • The aquaporins, blueprints for cellular plumbing systems
    • Agre P., Bonhivers M., Borgnia M.J. The aquaporins, blueprints for cellular plumbing systems. J. Biol. Chem. 273:1998;14659-14662
    • (1998) J. Biol. Chem. , vol.273 , pp. 14659-14662
    • Agre, P.1    Bonhivers, M.2    Borgnia, M.J.3
  • 10
    • 0026577151 scopus 로고
    • Ontogeny of the epidermal barrier to water loss in the rat: Correlation of function with stratum corneum structure and lipid content
    • Aszterbaum M., Menon G.K., Feingold K.R., Williams M.L. Ontogeny of the epidermal barrier to water loss in the rat. correlation of function with stratum corneum structure and lipid content Pediatr. Res. 31:1992;308-317
    • (1992) Pediatr. Res. , vol.31 , pp. 308-317
    • Aszterbaum, M.1    Menon, G.K.2    Feingold, K.R.3    Williams, M.L.4
  • 11
    • 0034613453 scopus 로고    scopus 로고
    • Presence of aquaporin-4 and muscarinic receptors in astrocytes and ependymal cells in rat brain: A clue to a common function? Neurosci
    • Badaut J., Verbavatz J.M., Freund-Mercier M.J., Lasbennes F. Presence of aquaporin-4 and muscarinic receptors in astrocytes and ependymal cells in rat brain. a clue to a common function? Neurosci Lett. 292:2000;75-78
    • (2000) Lett. , vol.292 , pp. 75-78
    • Badaut, J.1    Verbavatz, J.M.2    Freund-Mercier, M.J.3    Lasbennes, F.4
  • 14
    • 0025174799 scopus 로고
    • A common ancestor for bovine lens fiber major intrinsic protein, soybean nodulin-26 protein, and e coli glycerol facilitator
    • Baker M.E., Saier M.H. Jr. A common ancestor for bovine lens fiber major intrinsic protein, soybean nodulin-26 protein, and E coli glycerol facilitator. Cell. 60:1990;185-186
    • (1990) Cell , vol.60 , pp. 185-186
    • Baker, M.E.1    Saier Jr., M.H.2
  • 15
    • 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. Missense mutations in MIP underlie autosomal dominant 'polymorphic' and lamellar cataracts linked to 12q. Nat. Genet. 25:2000;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
  • 16
    • 0035652639 scopus 로고    scopus 로고
    • Subcellular distribution of aquaporin 5 in salivary glands in primary Sjogren's syndrome
    • Beroukas D., Hiscock J., Jonsson R., Waterman S.A., Gordon T.P. Subcellular distribution of aquaporin 5 in salivary glands in primary Sjogren's syndrome. Lancet. 358:2001;1875-1876
    • (2001) Lancet , vol.358 , pp. 1875-1876
    • Beroukas, D.1    Hiscock, J.2    Jonsson, R.3    Waterman, S.A.4    Gordon, T.P.5
  • 17
    • 0036847857 scopus 로고    scopus 로고
    • Selective down-regulation of aquaporin-1 in salivary glands in primary Sjogren's syndrome
    • Beroukas D., Hiscock J., Gannon B.J., Jonsson R., Gordon T.P., Waterman S.A. Selective down-regulation of aquaporin-1 in salivary glands in primary Sjogren's syndrome. Lab. Invest. 82:2002;1547-1552
    • (2002) Lab. Invest. , vol.82 , pp. 1547-1552
    • Beroukas, D.1    Hiscock, J.2    Gannon, B.J.3    Jonsson, R.4    Gordon, T.P.5    Waterman, S.A.6
  • 18
    • 0032853219 scopus 로고    scopus 로고
    • Cellular and molecular biology of the aquaporin water channels
    • Borgnia M., Nielsen S., Engel A., Agre P. Cellular and molecular biology of the aquaporin water channels. Annu. Rev. Biochem. 68:1999;425-458
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 425-458
    • Borgnia, M.1    Nielsen, S.2    Engel, A.3    Agre, P.4
  • 19
    • 0033756528 scopus 로고    scopus 로고
    • Nitric oxide and atrial natriuretic factor stimulate cGMP-dependent membrane insertion of aquaporin 2 in renal epithelial cells
    • Bouley R., Breton S., Sun T., McLaughlin M., Nsumu N.N., Lin H.Y., Ausiello D.A., Brown D. Nitric oxide and atrial natriuretic factor stimulate cGMP-dependent membrane insertion of aquaporin 2 in renal epithelial cells. J. Clin. Invest. 106:2000;1115-1126
    • (2000) J. Clin. Invest. , vol.106 , pp. 1115-1126
    • Bouley, R.1    Breton, S.2    Sun, T.3    McLaughlin, M.4    Nsumu, N.N.5    Lin, H.Y.6    Ausiello, D.A.7    Brown, D.8
  • 21
    • 0037404210 scopus 로고    scopus 로고
    • The ins and outs of aquaporin-2 trafficking
    • Brown D. The ins and outs of aquaporin-2 trafficking. Am. J. Physiol. Renal Physiol. 284:2003;F893-F901
    • (2003) Am. J. Physiol. Renal Physiol. , vol.284
    • Brown, D.1
  • 22
    • 0027504890 scopus 로고
    • Localization of the CHIP28 water channel in reabsorptive segments of the rat male reproductive tract
    • Brown D., Verbavatz J.M., Valenti G., Lui B., Sabolic I. Localization of the CHIP28 water channel in reabsorptive segments of the rat male reproductive tract. Eur. J. Cell Biol. 61:1993;264-273
    • (1993) Eur. J. Cell Biol. , vol.61 , pp. 264-273
    • Brown, D.1    Verbavatz, J.M.2    Valenti, G.3    Lui, B.4    Sabolic, I.5
  • 23
    • 0038460939 scopus 로고    scopus 로고
    • Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas
    • Burghardt B., Elkaer M.L., Kwon T.H., Racz G.Z., Varga G., Steward M.C., Nielsen S. Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas. Gut. 52:2003;1008-1016
    • (2003) Gut , vol.52 , pp. 1008-1016
    • Burghardt, B.1    Elkaer, M.L.2    Kwon, T.H.3    Racz, G.Z.4    Varga, G.5    Steward, M.C.6    Nielsen, S.7
  • 25
    • 0035798124 scopus 로고    scopus 로고
    • Possible involvement of aquaporin-7 and -8 in rat testis development and spermatogenesis
    • Calamita G., Mazzone A., Bizzoca A., Svelto M. Possible involvement of aquaporin-7 and -8 in rat testis development and spermatogenesis. Biochem. Biophys. Res. Commun. 288:2001;619-625
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 619-625
    • Calamita, G.1    Mazzone, A.2    Bizzoca, A.3    Svelto, M.4
  • 26
    • 0035013934 scopus 로고    scopus 로고
    • Expression and localization of the aquaporin-8 water channel in rat testis
    • Calamita G., Mazzone A., Cho Y.S., Valenti G., Svelto M. Expression and localization of the aquaporin-8 water channel in rat testis. Biol. Reprod. 64:2001;1660-1666
    • (2001) Biol. Reprod. , vol.64 , pp. 1660-1666
    • Calamita, G.1    Mazzone, A.2    Cho, Y.S.3    Valenti, G.4    Svelto, M.5
  • 28
    • 0030444934 scopus 로고    scopus 로고
    • In vivo inhibition of transcellular water channels (aquaporin-1) during acute peritoneal dialysis in rats
    • Carlsson O., Nielsen S., Zakaria E.L-R., Rippe B. In vivo inhibition of transcellular water channels (aquaporin-1) during acute peritoneal dialysis in rats. Am. J. Physiol. 271:1996;H2254-H2262
    • (1996) Am. J. Physiol. , vol.271
    • Carlsson, O.1    Nielsen, S.2    Zakaria, E.L.-R.3    Rippe, B.4
  • 29
    • 0035904236 scopus 로고    scopus 로고
    • Histamine treatment induces rearrangements of orthogonal arrays of particles (OAPs) in human AQP4-expressing gastric cells
    • Carmosino M., Procino G., Nicchia G.P., Mannucci R., Verbavatz J.M., Gobin R., Svelto M., Valenti G. Histamine treatment induces rearrangements of orthogonal arrays of particles (OAPs) in human AQP4-expressing gastric cells. J. Cell Biol. 154:2001;1235-1243
    • (2001) J. Cell Biol. , vol.154 , pp. 1235-1243
    • Carmosino, M.1    Procino, G.2    Nicchia, G.P.3    Mannucci, R.4    Verbavatz, J.M.5    Gobin, R.6    Svelto, M.7    Valenti, G.8
  • 30
    • 0030883373 scopus 로고    scopus 로고
    • Comparison of the water transporting properties of MIP and AQP1
    • Chandy G., Zampighi G.A., Kreman M., Hall J.E. Comparison of the water transporting properties of MIP and AQP1. J. Membr. Biol. 159:1997;29-39
    • (1997) J. Membr. Biol. , vol.159 , pp. 29-39
    • Chandy, G.1    Zampighi, G.A.2    Kreman, M.3    Hall, J.E.4
  • 31
    • 0035106823 scopus 로고    scopus 로고
    • Aquaporins constitute a large and highly divergent protein family in maize
    • Chaumont F., Barrieu F., Wojcik E., Chrispeels M.J., Jung R. Aquaporins constitute a large and highly divergent protein family in maize. Plant Physiol. 125:2001;1206-1215
    • (2001) Plant Physiol. , vol.125 , pp. 1206-1215
    • Chaumont, F.1    Barrieu, F.2    Wojcik, E.3    Chrispeels, M.J.4    Jung, R.5
  • 34
    • 0031888078 scopus 로고    scopus 로고
    • Fourfold reduction of water permeability in inner medullary collecting duct of aquaporin-4 knockout mice
    • Chou C.L., Ma T., Yang B., Knepper M.A., Verkman A.S. Fourfold reduction of water permeability in inner medullary collecting duct of aquaporin-4 knockout mice. Am. J. Physiol. 274:1998;C549-C554
    • (1998) Am. J. Physiol. , vol.274
    • Chou, C.L.1    Ma, T.2    Yang, B.3    Knepper, M.A.4    Verkman, A.S.5
  • 35
    • 0033557374 scopus 로고    scopus 로고
    • Reduced water permeability and altered ultrastructure in thin descending limb of henle in aquaporin-1 null mice
    • Chou C.L., Knepper M.A., Hoek A.N., Brown D., Yang B., Ma T., Verkman A.S. Reduced water permeability and altered ultrastructure in thin descending limb of henle in aquaporin-1 null mice. J. Clin. Invest. 103:1999;491-496
    • (1999) J. Clin. Invest. , vol.103 , pp. 491-496
    • Chou, C.L.1    Knepper, M.A.2    Hoek, A.N.3    Brown, D.4    Yang, B.5    Ma, T.6    Verkman, A.S.7
  • 36
    • 0028135644 scopus 로고
    • Aquaporins: Water channel proteins of plant and animal cells
    • Chrispeels M.J., Agre P. Aquaporins. water channel proteins of plant and animal cells Trends Biochem. Sci. 19:1994;421-425
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 421-425
    • Chrispeels, M.J.1    Agre, P.2
  • 37
    • 0033978380 scopus 로고    scopus 로고
    • Localization and regulation of PKA-phosphorylated AQP2 in response to V(2)-receptor agonist/antagonist treatment
    • Christensen B.M., Zelenina M., Aperia A., Nielsen S. Localization and regulation of PKA-phosphorylated AQP2 in response to V(2)-receptor agonist/antagonist treatment. Am. J. Physiol. Renal Physiol. 278:2000;F29-F42
    • (2000) Am. J. Physiol. Renal Physiol. , vol.278
    • Christensen, B.M.1    Zelenina, M.2    Aperia, A.3    Nielsen, S.4
  • 38
  • 40
    • 0034779005 scopus 로고    scopus 로고
    • Water channel proteins AQP3 and AQP9 are present in syncytiotrophoblast of human term placenta
    • Damiano A., Zotta E., Goldstein J., Reisin I., Ibarra C. Water channel proteins AQP3 and AQP9 are present in syncytiotrophoblast of human term placenta. Placenta. 22:2001;776-781
    • (2001) Placenta , vol.22 , pp. 776-781
    • Damiano, A.1    Zotta, E.2    Goldstein, J.3    Reisin, I.4    Ibarra, C.5
  • 41
    • 0026458563 scopus 로고
    • Isolation of a cDNA for rat CHIP28 water channel: High mRNA expression in kidney cortex and inner medulla
    • Deen P.M., Dempster J.A., Wieringa B., Van Os C.H. Isolation of a cDNA for rat CHIP28 water channel. high mRNA expression in kidney cortex and inner medulla Biochem. Biophys. Res. Commun. 188:1992;1267-1273
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 1267-1273
    • Deen, P.M.1    Dempster, J.A.2    Wieringa, B.3    Van Os, C.H.4
  • 42
    • 0028968593 scopus 로고
    • Water channels encoded by mutant aquaporin-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing
    • Deen P.M., Croes H., van Aubel R.A., Ginsel L.A., Van Os C.H. Water channels encoded by mutant aquaporin-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing. J. Clin. Invest. 95:1995;2291-2296
    • (1995) J. Clin. Invest. , vol.95 , pp. 2291-2296
    • Deen, P.M.1    Croes, H.2    Van Aubel, R.A.3    Ginsel, L.A.4    Van Os, C.H.5
  • 43
    • 0030932758 scopus 로고    scopus 로고
    • Apical and basolateral expression of aquaporin-1 in transfected MDCK and LLC-PK cells and functional evaluation of their transcellular osmotic water permeabilities
    • Deen P.M., Nielsen S., Bindels R.J., Van Os C.H. Apical and basolateral expression of aquaporin-1 in transfected MDCK and LLC-PK cells and functional evaluation of their transcellular osmotic water permeabilities. Pflugers Arch. 433:1997;780-787
    • (1997) Pflugers Arch. , vol.433 , pp. 780-787
    • Deen, P.M.1    Nielsen, S.2    Bindels, R.J.3    Van Os, C.H.4
  • 44
    • 0034695885 scopus 로고    scopus 로고
    • The role of aquaporins in dendritic cell macropinocytosis
    • de Baey A., Lanzavecchia A. The role of aquaporins in dendritic cell macropinocytosis. J. Exp. Med. 191:2000;743-748
    • (2000) J. Exp. Med. , vol.191 , pp. 743-748
    • De Baey, A.1    Lanzavecchia, A.2
  • 45
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF
    • de Groot B.L., Grubmuller H. Water permeation across biological membranes. mechanism and dynamics of aquaporin-1 and GlpF Science. 294:2001;2353-2357
    • (2001) Science , vol.294 , pp. 2353-2357
    • De Groot, B.L.1    Grubmuller, H.2
  • 46
    • 0035979744 scopus 로고    scopus 로고
    • A refined structure of human aquaporin-1
    • de Groot B.L., Engel A., Grubmuller H. A refined structure of human aquaporin-1. FEBS Lett. 504:2001;206-211
    • (2001) FEBS Lett. , vol.504 , pp. 206-211
    • De Groot, B.L.1    Engel, A.2    Grubmuller, H.3
  • 47
    • 0023768507 scopus 로고
    • Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules
    • Denker B.M., Smith B.L., Kuhajda F.P., Agre P. Identification, purification, and partial characterization of a novel Mr 28, 000 integral membrane protein from erythrocytes and renal tubules. J. Biol. Chem. 263:1988;15634-15642
    • (1988) J. Biol. Chem. , vol.263 , pp. 15634-15642
    • Denker, B.M.1    Smith, B.L.2    Kuhajda, F.P.3    Agre, P.4
  • 50
    • 0028020911 scopus 로고
    • Cloning and expression of AQP3, a water channel from the medullary collecting duct of rat kidney
    • Echevarria M., Windhager E.E., Tate S.S., Frindt G. Cloning and expression of AQP3, a water channel from the medullary collecting duct of rat kidney. Proc. Natl. Acad. Sci. USA. 91:1994;10997-11001
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10997-11001
    • Echevarria, M.1    Windhager, E.E.2    Tate, S.S.3    Frindt, G.4
  • 52
    • 0017276134 scopus 로고
    • Studies of excitable membranes. II. a comparison of specializations at neuromuscular junctions and non-junctional sarcolemmas of mammalian fast and slow twitch muscle fibers
    • Ellisman M.H., Rash J.E., Staehelin L.A., Porter K.R. Studies of excitable membranes. II. A comparison of specializations at neuromuscular junctions and non-junctional sarcolemmas of mammalian fast and slow twitch muscle fibers. J. Cell Biol. 68:1976;752-774
    • (1976) J. Cell Biol. , vol.68 , pp. 752-774
    • Ellisman, M.H.1    Rash, J.E.2    Staehelin, L.A.3    Porter, K.R.4
  • 53
    • 0038206728 scopus 로고    scopus 로고
    • Signals that regulate GLUT4 translocation
    • Elmendorf J.S. Signals that regulate GLUT4 translocation. J. Membr. Biol. 190:2002;167-174
    • (2002) J. Membr. Biol. , vol.190 , pp. 167-174
    • Elmendorf, J.S.1
  • 54
    • 0034161393 scopus 로고    scopus 로고
    • The importance of aquaporin water channel protein structures
    • Engel A., Fujiyoshi Y., Agre P. The importance of aquaporin water channel protein structures. EMBO J. 19:2000;800-806
    • (2000) EMBO J. , vol.19 , pp. 800-806
    • Engel, A.1    Fujiyoshi, Y.2    Agre, P.3
  • 55
    • 0021064311 scopus 로고
    • Immunocytochemical localization of the main intrinsic polypeptide (MIP) in ultrathin frozen sections of rat lens
    • Fitzgerald P.G., Bok D., Horwitz J. Immunocytochemical localization of the main intrinsic polypeptide (MIP) in ultrathin frozen sections of rat lens. J. Cell Biol. 97:1983;1491-1499
    • (1983) J. Cell Biol. , vol.97 , pp. 1491-1499
    • Fitzgerald, P.G.1    Bok, D.2    Horwitz, J.3
  • 56
    • 0033863125 scopus 로고    scopus 로고
    • Water permeability in rat oocytes at different maturity stages: Aquaporin-9 expression
    • Ford P., Merot J., Jawerbaum A., Gimeno M.A., Capurro C., Parisi M. Water permeability in rat oocytes at different maturity stages. aquaporin-9 expression J. Membr. Biol. 176:2000;151-158
    • (2000) J. Membr. Biol. , vol.176 , pp. 151-158
    • Ford, P.1    Merot, J.2    Jawerbaum, A.3    Gimeno, M.A.4    Capurro, C.5    Parisi, M.6
  • 58
    • 0033675222 scopus 로고    scopus 로고
    • Congenital progressive polymorphic cataract caused by a mutation in the major intrinsic protein of the lens, MIP (AQP0)
    • Francis P., Berry V., Bhattacharya S., Moore A. Congenital progressive polymorphic cataract caused by a mutation in the major intrinsic protein of the lens, MIP (AQP0). Br. J. Ophthalmol. 84:2000;1376-1379
    • (2000) Br. J. Ophthalmol. , vol.84 , pp. 1376-1379
    • Francis, P.1    Berry, V.2    Bhattacharya, S.3    Moore, A.4
  • 60
    • 0029009408 scopus 로고
    • Immunolocalization of the mercurial-insensitive water channel and glycerol intrinsic protein in epithelial cell plasma membranes
    • Frigeri A., Gropper M.A., Turck C.W., Verkman A.S. Immunolocalization of the mercurial-insensitive water channel and glycerol intrinsic protein in epithelial cell plasma membranes. Proc. Natl. Acad. Sci. USA. 92:1995;4328-4331
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4328-4331
    • Frigeri, A.1    Gropper, M.A.2    Turck, C.W.3    Verkman, A.S.4
  • 61
    • 0029122669 scopus 로고
    • Localization of MIWC and GLIP water channel homologs in neuromuscular, epithelial and glandular tissues
    • Frigeri A., Gropper M.A., Umenishi F., Kawashima M., Brown D., Verkman A.S. Localization of MIWC and GLIP water channel homologs in neuromuscular, epithelial and glandular tissues. J. Cell Sci. 108:1995;2993-3002
    • (1995) J. Cell Sci. , vol.108 , pp. 2993-3002
    • Frigeri, A.1    Gropper, M.A.2    Umenishi, F.3    Kawashima, M.4    Brown, D.5    Verkman, A.S.6
  • 64
    • 0036636106 scopus 로고    scopus 로고
    • Altered aquaporin-4 expression in human muscular dystrophies: A common feature?
    • Frigeri A., Nicchia G.P., Repetto S., Bado M., Minetti C., Svelto M. Altered aquaporin-4 expression in human muscular dystrophies. a common feature? FASEB J. 16:2001;1120-1122
    • (2001) FASEB J. , vol.16 , pp. 1120-1122
    • Frigeri, A.1    Nicchia, G.P.2    Repetto, S.3    Bado, M.4    Minetti, C.5    Svelto, M.6
  • 66
    • 0032831435 scopus 로고    scopus 로고
    • High-resolution immunogold cytochemistry indicates that AQP4 is concentrated along the basal membrane of parietal cell in rat stomach
    • Fujita A., Horio Y., Nielsen S., Nagelhus E.A., Hata F., Ottersen O.P., Kurachi Y. High-resolution immunogold cytochemistry indicates that AQP4 is concentrated along the basal membrane of parietal cell in rat stomach. FEBS Lett. 459:1999;305-309
    • (1999) FEBS Lett. , vol.459 , pp. 305-309
    • Fujita, A.1    Horio, Y.2    Nielsen, S.3    Nagelhus, E.A.4    Hata, F.5    Ottersen, O.P.6    Kurachi, Y.7
  • 68
    • 0037128938 scopus 로고    scopus 로고
    • Claudin-based tight junctions are crucial for the mammalian epidermal barrier: A lesson from claudin-1-deficient mice
    • Furuse M., Hata M., Furuse K., Yoshida Y., Haratake A., Sugitani Y., Noda T., Kubo A., Tsukita S. Claudin-based tight junctions are crucial for the mammalian epidermal barrier. a lesson from claudin-1-deficient mice J. Cell Biol. 156:2002;1099-1111
    • (2002) J. Cell Biol. , vol.156 , pp. 1099-1111
    • Furuse, M.1    Hata, M.2    Furuse, K.3    Yoshida, Y.4    Haratake, A.5    Sugitani, Y.6    Noda, T.7    Kubo, A.8    Tsukita, S.9
  • 69
    • 0036253117 scopus 로고    scopus 로고
    • Distribution of aquaporin 1 in the rat pancreatic duct system examined with light- and electron-microscopic immunohistochemistry
    • Furuya S., Naruse S., Ko S.B., Ishiguro H., Yoshikawa T., Hayakawa T. Distribution of aquaporin 1 in the rat pancreatic duct system examined with light- and electron-microscopic immunohistochemistry. Cell Tissue Res. 308:2002;75-86
    • (2002) Cell Tissue Res. , vol.308 , pp. 75-86
    • Furuya, S.1    Naruse, S.2    Ko, S.B.3    Ishiguro, H.4    Yoshikawa, T.5    Hayakawa, T.6
  • 70
    • 0027459174 scopus 로고
    • Cloning and expression of apical membrane water channel of rat kidney collecting tubule
    • Fushimi K., Uchida S., Hara Y., Hirata Y., Marumo F., Sasaki S. Cloning and expression of apical membrane water channel of rat kidney collecting tubule. Nature. 361:1993;549-552
    • (1993) Nature , vol.361 , pp. 549-552
    • Fushimi, K.1    Uchida, S.2    Hara, Y.3    Hirata, Y.4    Marumo, F.5    Sasaki, S.6
  • 71
    • 0030965161 scopus 로고    scopus 로고
    • Phosphorylation of serine 256 is required for cAMP-dependent regulatory exocytosis of the aquaporin-2 water channel
    • Fushimi K., Sasaki S., Marumo F. Phosphorylation of serine 256 is required for cAMP-dependent regulatory exocytosis of the aquaporin-2 water channel. J. Biol. Chem. 272:1997;14800-14804
    • (1997) J. Biol. Chem. , vol.272 , pp. 14800-14804
    • Fushimi, K.1    Sasaki, S.2    Marumo, F.3
  • 72
    • 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 M.C., Gradilone S.A., Splinter P., LaRusso N.F., Marinelli R.A. The water channel aquaporin-8 is mainly intracellular in rat hepatocytes, and its plasma membrane insertion is stimulated by cyclic AMP. J. Biol. Chem. 276:2001;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
  • 73
    • 0036311144 scopus 로고    scopus 로고
    • Molecular determinants of regulated exocytosis
    • Gerber S.H., Sudhof T.C. Molecular determinants of regulated exocytosis. Diabetes. 51(Suppl 1):2002;S3-S11
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 1
    • Gerber, S.H.1    Sudhof, T.C.2
  • 74
    • 0031773249 scopus 로고    scopus 로고
    • Novel mutations in aquaporin-2 gene in female siblings with nephrogenic diabetes insipidus: Evidence of disrupted water channel function
    • Goji K., Kuwahara M., Gu Y., Matsuo M., Marumo F., Sasaki S. Novel mutations in aquaporin-2 gene in female siblings with nephrogenic diabetes insipidus. evidence of disrupted water channel function J. Clin. Endocrinol. Metab. 83:1998;3205-3209
    • (1998) J. Clin. Endocrinol. Metab. , vol.83 , pp. 3205-3209
    • Goji, K.1    Kuwahara, M.2    Gu, Y.3    Matsuo, M.4    Marumo, F.5    Sasaki, S.6
  • 75
    • 0021712623 scopus 로고
    • The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning
    • Gorin M.B., Yancey S.B., Cline J., Revel J.P., Horwitz J. The major intrinsic protein (MIP) of the bovine lens fiber membrane. characterization and structure based on cDNA cloning Cell. 39:1984;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
  • 81
    • 0036203850 scopus 로고    scopus 로고
    • Molecular mechanisms of water transport in the eye
    • Hamann S. Molecular mechanisms of water transport in the eye. Int. Rev. Cytol. 215:2002;395-431
    • (2002) Int. Rev. Cytol. , vol.215 , pp. 395-431
    • Hamann, S.1
  • 83
    • 0038132147 scopus 로고    scopus 로고
    • Glycerol replacement corrects defective skin hydration, elasticity, and barrier function in aquaporin-3-deficient mice
    • Hara M., Verkman A.S. Glycerol replacement corrects defective skin hydration, elasticity, and barrier function in aquaporin-3-deficient mice. Proc. Natl. Acad. Sci. USA. 100:2003;7360-7365
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7360-7365
    • Hara, M.1    Verkman, A.S.2
  • 84
    • 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 A.S. Selectively reduced glycerol in skin of aquaporin-3-deficient mice may account for impaired skin hydration, elasticity, and barrier recovery. J. Biol. Chem. 277:2002;46616-46621
    • (2002) J. Biol. Chem. , vol.277 , pp. 46616-46621
    • Hara, M.1    Ma, T.2    Verkman, A.S.3
  • 85
    • 0027530829 scopus 로고
    • Tissue-specific expression of mRNA encoding rat kidney water channel CHIP28k by in situ hybridization
    • Hasegawa H., Zhang R., Dohrman A., Verkman A.S. Tissue-specific expression of mRNA encoding rat kidney water channel CHIP28k by in situ hybridization. Am. J. Physiol. 264:1993;C237-C245
    • (1993) Am. J. Physiol. , vol.264
    • Hasegawa, H.1    Zhang, R.2    Dohrman, A.3    Verkman, A.S.4
  • 86
    • 0028276633 scopus 로고
    • Extrarenal tissue distribution of CHIP28 water channels by in situ hybridization and antibody staining
    • Hasegawa H., Lian S.C., Finkbeiner W.E., Verkman A.S. Extrarenal tissue distribution of CHIP28 water channels by in situ hybridization and antibody staining. Am. J. Physiol. 266:1994;C893-C903
    • (1994) Am. J. Physiol. , vol.266
    • Hasegawa, H.1    Lian, S.C.2    Finkbeiner, W.E.3    Verkman, A.S.4
  • 87
    • 0027989801 scopus 로고
    • Molecular cloning of a mercurial-insensitive water channel expressed in selected water-transporting tissues
    • Hasegawa H., Ma T., Skach W., Matthay M.A., Verkman A.S. Molecular cloning of a mercurial-insensitive water channel expressed in selected water-transporting tissues. J. Biol. Chem. 269:1994;5497-5500
    • (1994) J. Biol. Chem. , vol.269 , pp. 5497-5500
    • Hasegawa, H.1    Ma, T.2    Skach, W.3    Matthay, M.A.4    Verkman, A.S.5
  • 91
    • 0031021974 scopus 로고    scopus 로고
    • Polarized distribution of key membrane transport proteins in the rat submandibular gland
    • He X., Tse C.M., Donowitz M., Alper S.L., Gabriel S.E., Baum B.J. Polarized distribution of key membrane transport proteins in the rat submandibular gland. Pflugers Arch. 433:1997;260-268
    • (1997) Pflugers Arch. , vol.433 , pp. 260-268
    • He, X.1    Tse, C.M.2    Donowitz, M.3    Alper, S.L.4    Gabriel, S.E.5    Baum, B.J.6
  • 93
    • 0036101324 scopus 로고    scopus 로고
    • Expression patterns of aquaporins in the inner ear: Evidence for concerted actions of multiple types of aquaporins to facilitate water transport in the cochlea
    • Huang D., Chen P., Chen S., Nagura M., Lim D.J., Lin X. Expression patterns of aquaporins in the inner ear. evidence for concerted actions of multiple types of aquaporins to facilitate water transport in the cochlea Hear. Res. 165:2002;85-95
    • (2002) Hear. Res. , vol.165 , pp. 85-95
    • Huang, D.1    Chen, P.2    Chen, S.3    Nagura, M.4    Lim, D.J.5    Lin, X.6
  • 95
    • 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 W.B., Agre P., Yasui M. Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63. J. Biol. Chem. 277:2002;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    Yasui, M.6
  • 96
    • 0036623103 scopus 로고    scopus 로고
    • Ultrastructural localization of aquaporin 4 and alpha1-syntrophin in the vascular feet of brain astrocytes
    • Inoue M., Wakayama Y., Liu J.W., Murahashi M., Shibuya S., Oniki H. Ultrastructural localization of aquaporin 4 and alpha1-syntrophin in the vascular feet of brain astrocytes. Tohoku J. Exp. Med. 197:2002;87-93
    • (2002) Tohoku J. Exp. Med. , vol.197 , pp. 87-93
    • Inoue, M.1    Wakayama, Y.2    Liu, J.W.3    Murahashi, M.4    Shibuya, S.5    Oniki, H.6
  • 97
    • 22044457833 scopus 로고    scopus 로고
    • The dichotomy of MIP family suggests two separate origins of water channels
    • Ishibashi K., Sasaki S. The dichotomy of MIP family suggests two separate origins of water channels. News Physiol. Sci. 13:1998;137-142
    • (1998) News Physiol. Sci. , vol.13 , pp. 137-142
    • Ishibashi, K.1    Sasaki, S.2
  • 98
    • 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 Y., Gojobori T., Maruo F. 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. USA. 91:1994;6269-6273
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6269-6273
    • 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, Y.9    Gojobori, T.10    Maruo, F.11
  • 100
    • 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. Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea. J. Biol. Chem. 272:1997;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
  • 101
    • 0030851768 scopus 로고    scopus 로고
    • Immunolocalization and effect of dehydration on AQP3, a basolateral water channel of kidney collecting ducts
    • Ishibashi K., Sasaki S., Fushimi K., Yamamoto T., Kuwahara M., Marumo F. Immunolocalization and effect of dehydration on AQP3, a basolateral water channel of kidney collecting ducts. Am. J. Physiol. 272:1997;F235-F241
    • (1997) Am. J. Physiol. , vol.272
    • Ishibashi, K.1    Sasaki, S.2    Fushimi, K.3    Yamamoto, T.4    Kuwahara, M.5    Marumo, F.6
  • 102
    • 0032489241 scopus 로고    scopus 로고
    • Cloning and functional expression of a new aquaporin (AQP9) abundantly expressed in the peripheral leukocytes permeable to water and urea, but not to glycerol
    • Ishibashi K., Kuwahara M., Gu Y., Tanaka Y., Marumo F., Sasaki S. Cloning and functional expression of a new aquaporin (AQP9) abundantly expressed in the peripheral leukocytes permeable to water and urea, but not to glycerol. Biochem. Biophys. Res. Commun. 244:1998;268-274
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 268-274
    • Ishibashi, K.1    Kuwahara, M.2    Gu, Y.3    Tanaka, Y.4    Marumo, F.5    Sasaki, S.6
  • 104
    • 0033848711 scopus 로고    scopus 로고
    • Cellular localization of aquaporin 7 in the rat kidney
    • Ishibashi K., Imai M., Sasaki S. Cellular localization of aquaporin 7 in the rat kidney. Exp. Nephrol. 8:2000;252-257
    • (2000) Exp. Nephrol. , vol.8 , pp. 252-257
    • Ishibashi, K.1    Imai, M.2    Sasaki, S.3
  • 106
    • 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. Cloning and identification of a new member of water channel (AQP10) as an aquaglyceroporin. Biochim. Biophys. Acta. 1576:2002;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
  • 107
    • 0031590299 scopus 로고    scopus 로고
    • Immunolocalization of aquaporin homologs in mouse lacrimal glands
    • Ishida N., Hirai S.I., Mita S. Immunolocalization of aquaporin homologs in mouse lacrimal glands. Biochem. Biophys. Res. Commun. 238:1997;891-895
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 891-895
    • Ishida, N.1    Hirai, S.I.2    Mita, S.3
  • 111
    • 0028558703 scopus 로고
    • Molecular characterization of an aquaporin cDNA from brain: Candidate osmoreceptor and regulator of water balance
    • Jung J.S., Bhat R.V., Preston G.M., Guggino W.B., Baraban J.M., Agre P. Molecular characterization of an aquaporin cDNA from brain. candidate osmoreceptor and regulator of water balance Proc. Natl. Acad. Sci. USA. 91:1994;13052-13056
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 13052-13056
    • Jung, J.S.1    Bhat, R.V.2    Preston, G.M.3    Guggino, W.B.4    Baraban, J.M.5    Agre, P.6
  • 112
    • 0033522389 scopus 로고    scopus 로고
    • An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus
    • Kamsteeg E.J., Wormhoudt T.A., Rijss J.P., van Os C.H., Deen P.M. An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus. EMBO J. 18:1999;2394-2400
    • (1999) EMBO J. , vol.18 , pp. 2394-2400
    • Kamsteeg, E.J.1    Wormhoudt, T.A.2    Rijss, J.P.3    Van Os, C.H.4    Deen, P.M.5
  • 113
    • 0034645068 scopus 로고    scopus 로고
    • The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and non-phosphorylated monomers
    • Kamsteeg E.J., Heijnen I., van Os C.H., Deen P.M. The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and non-phosphorylated monomers. J. Cell Biol. 151:2000;919-930
    • (2000) J. Cell Biol. , vol.151 , pp. 919-930
    • Kamsteeg, E.J.1    Heijnen, I.2    Van Os, C.H.3    Deen, P.M.4
  • 115
    • 0029085386 scopus 로고
    • Constitutive and regulated membrane expression of aquaporin 1 and aquaporin 2 water channels in stably transfected LLC-PK1 epithelial cells
    • Katsura T., Verbavatz J.M., Farinas J., Ma T., Ausiello D.A., Verkman A.S., Brown D. Constitutive and regulated membrane expression of aquaporin 1 and aquaporin 2 water channels in stably transfected LLC-PK1 epithelial cells. Proc. Natl. Acad. Sci. USA. 92:1995;7212-7216
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7212-7216
    • Katsura, T.1    Verbavatz, J.M.2    Farinas, J.3    Ma, T.4    Ausiello, D.A.5    Verkman, A.S.6    Brown, D.7
  • 116
    • 0029867986 scopus 로고    scopus 로고
    • Direct demonstration of aquaporin-2 water channel recycling in stably transfected LLC-PK1 epithelial cells
    • Katsura T., Ausiello D.A., Brown D. Direct demonstration of aquaporin-2 water channel recycling in stably transfected LLC-PK1 epithelial cells. Am. J. Physiol. 270:1996;F548-F553
    • (1996) Am. J. Physiol. , vol.270
    • Katsura, T.1    Ausiello, D.A.2    Brown, D.3
  • 117
    • 0030772349 scopus 로고    scopus 로고
    • Protein kinase a phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells
    • Katsura T., Gustafson C.E., Ausiello D.A., Brown D. Protein kinase a phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells. Am. J. Physiol. 272:1997;F817-F822
    • (1997) Am. J. Physiol. , vol.272
    • Katsura, T.1    Gustafson, C.E.2    Ausiello, D.A.3    Brown, D.4
  • 118
    • 0029942399 scopus 로고    scopus 로고
    • Pathophysiology of the aquaporin water channels
    • King L.S, Agre P. Pathophysiology of the aquaporin water channels. Annu. Rev. Physiol. 58:1996;619-648
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 619-648
    • King, L.S.1    Agre, P.2
  • 119
    • 0030666976 scopus 로고    scopus 로고
    • Aquaporins in complex tissues. I. Developmental patterns in respiratory and glandular tissues of rat
    • King L.S., Nielsen S., Agre P. Aquaporins in complex tissues. I. Developmental patterns in respiratory and glandular tissues of rat. Am. J. Physiol. 273:1997;C1541-C1548
    • (1997) Am. J. Physiol. , vol.273
    • King, L.S.1    Nielsen, S.2    Agre, P.3
  • 120
    • 0035913207 scopus 로고    scopus 로고
    • Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1
    • King L.S., Choi M., Fernandez P.C., Cartron J.P., Agre P. Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1. N. Engl. J. Med. 345:2001;175-179
    • (2001) N. 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
  • 121
    • 0037154182 scopus 로고    scopus 로고
    • Decreased pulmonary vascular permeability in aquaporin-1-null humans
    • King L.S., Nielsen S., Agre P., Brown R.H. Decreased pulmonary vascular permeability in aquaporin-1-null humans. Proc. Natl. Acad. Sci. USA. 99:2002;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
  • 125
    • 0035827567 scopus 로고    scopus 로고
    • An inhibitory role of Rho in the vasopressin-mediated translocation of aquaporin-2 into cell membranes of renal principal cells
    • Klussmann E., Tamma G., Lorenz D., Wiesner B., Maric K., Hofmann F., Aktories K., Valenti G., Rosenthal W. An inhibitory role of Rho in the vasopressin-mediated translocation of aquaporin-2 into cell membranes of renal principal cells. J. Biol. Chem. 276:2001;20451-20457
    • (2001) J. Biol. Chem. , vol.276 , pp. 20451-20457
    • Klussmann, E.1    Tamma, G.2    Lorenz, D.3    Wiesner, B.4    Maric, K.5    Hofmann, F.6    Aktories, K.7    Valenti, G.8    Rosenthal, W.9
  • 127
    • 0035807795 scopus 로고    scopus 로고
    • Dynamic mechanisms of the membrane water channel aquaporin-1 (AQP1)
    • Kong Y., Ma J. Dynamic mechanisms of the membrane water channel aquaporin-1 (AQP1). Proc. Natl. Acad. Sci. USA. 98:2001;14345-14349
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14345-14349
    • Kong, Y.1    Ma, J.2
  • 131
    • 0035968332 scopus 로고    scopus 로고
    • Salivary acinar cells from aquaporin 5-deficient mice have decreased membrane water permeability and altered cell volume regulation
    • Krane C.M., Melvin J.E., Nguyen H.V., Richardson L., Towne J.E., Doetschman T., Menon A.G. Salivary acinar cells from aquaporin 5-deficient mice have decreased membrane water permeability and altered cell volume regulation. J. Biol. Chem. 276:2001;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    Doetschman, T.6    Menon, A.G.7
  • 135
    • 0031989356 scopus 로고    scopus 로고
    • Aquaporin-2, a vasopressin-sensitive water channel, and nephrogenic diabetes insipidus
    • Kuwahara M. Aquaporin-2, a vasopressin-sensitive water channel, and nephrogenic diabetes insipidus. Intern. Med. 37:1998;215-217
    • (1998) Intern. Med. , vol.37 , pp. 215-217
    • Kuwahara, M.1
  • 137
    • 0035035681 scopus 로고    scopus 로고
    • Expression of aquaporin-1 in human peritoneal mesothelial cells and its upregulation by glucose in vitro
    • Lai K.N., Li F.K., Lan H.Y., Tang S., Tsang A.W., Chan D.T., Leung J.C. Expression of aquaporin-1 in human peritoneal mesothelial cells and its upregulation by glucose in vitro. J. Am. Soc. Nephrol. 12:2001;1036-1045
    • (2001) J. Am. Soc. Nephrol. , vol.12 , pp. 1036-1045
    • Lai, K.N.1    Li, F.K.2    Lan, H.Y.3    Tang, S.4    Tsang, A.W.5    Chan, D.T.6    Leung, J.C.7
  • 138
    • 0015978691 scopus 로고
    • Arrays of particles in freeze-fractured astrocytic membranes
    • Landis D.M., Reese T.S. Arrays of particles in freeze-fractured astrocytic membranes. J. Cell Biol. 60:1974;316-320
    • (1974) J. Cell Biol. , vol.60 , pp. 316-320
    • Landis, D.M.1    Reese, T.S.2
  • 140
    • 0035903098 scopus 로고    scopus 로고
    • Impaired hearing in mice lacking aquaporin-4 water channels
    • Li J., Verkman A.S. Impaired hearing in mice lacking aquaporin-4 water channels. J. Biol. Chem. 276:2001;31233-31237
    • (2001) J. Biol. Chem. , vol.276 , pp. 31233-31237
    • Li, J.1    Verkman, A.S.2
  • 141
    • 0036156831 scopus 로고    scopus 로고
    • Mildly abnormal retinal function in transgenic mice without Muller cell aquaporin-4 water channels
    • Li J., Patil R.V., Verkman A.S. Mildly abnormal retinal function in transgenic mice without Muller cell aquaporin-4 water channels. Invest. Ophthalmol. Vis. Sci. 43:2002;573-579
    • (2002) Invest. Ophthalmol. Vis. Sci. , vol.43 , pp. 573-579
    • Li, J.1    Patil, R.V.2    Verkman, A.S.3
  • 147
    • 0037223654 scopus 로고    scopus 로고
    • Cyclic AMP is sufficient for triggering the exocytic recruitment of aquaporin-2 in renal epithelial cells
    • Lorenz D., Krylov A., Hahm D., Hagen V., Rosenthal W., Pohl P., Maric K. Cyclic AMP is sufficient for triggering the exocytic recruitment of aquaporin-2 in renal epithelial cells. EMBO Rep. 4:2003;88-93
    • (2003) EMBO Rep. , vol.4 , pp. 88-93
    • Lorenz, D.1    Krylov, A.2    Hahm, D.3    Hagen, V.4    Rosenthal, W.5    Pohl, P.6    Maric, K.7
  • 149
    • 0027729983 scopus 로고
    • Cloning of a novel rat kidney cDNA homologous to CHIP28 and WCH-CD water channels
    • Ma T., Frigeri A., Skach W., Verkman A.S. Cloning of a novel rat kidney cDNA homologous to CHIP28 and WCH-CD water channels. Biochem. Biophys. Res. Commun. 197:1993;654-659
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 654-659
    • Ma, T.1    Frigeri, A.2    Skach, W.3    Verkman, A.S.4
  • 150
    • 0027441901 scopus 로고
    • Localization and functional analysis of CHIP28k water channels in stably transfected chinese hamster ovary cells
    • Ma T., Frigeri A., Tsai S.T., Verbavatz J.M., Verkman A.S. Localization and functional analysis of CHIP28k water channels in stably transfected chinese hamster ovary cells. J. Biol. Chem. 268:1993;22756-22764
    • (1993) J. Biol. Chem. , vol.268 , pp. 22756-22764
    • Ma, T.1    Frigeri, A.2    Tsai, S.T.3    Verbavatz, J.M.4    Verkman, A.S.5
  • 151
    • 0028059494 scopus 로고
    • Cloning of a water channel homolog expressed in brain meningeal cells and kidney collecting duct that functions as a stilbene-sensitive glycerol transporter
    • Ma T., Frigeri A., Hasegawa H., Verkman A.S. Cloning of a water channel homolog expressed in brain meningeal cells and kidney collecting duct that functions as a stilbene-sensitive glycerol transporter. J. Biol. Chem. 269:1994;21845-21849
    • (1994) J. Biol. Chem. , vol.269 , pp. 21845-21849
    • Ma, T.1    Frigeri, A.2    Hasegawa, H.3    Verkman, A.S.4
  • 152
    • 0030219815 scopus 로고    scopus 로고
    • CDNA cloning and gene structure of a novel water channel expressed exclusively in human kidney: Evidence for a gene cluster of aquaporins at chromosome locus 12q13
    • Ma T., Yang B., Kuo W.L., Verkman A.S. cDNA cloning and gene structure of a novel water channel expressed exclusively in human kidney. evidence for a gene cluster of aquaporins at chromosome locus 12q13 Genomics. 35:1996;543-550
    • (1996) Genomics , vol.35 , pp. 543-550
    • Ma, T.1    Yang, B.2    Kuo, W.L.3    Verkman, A.S.4
  • 153
    • 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 E.J., Epstein C.J., Verkman A.S. Generation and phenotype of a transgenic knockout mouse lacking the mercurial-insensitive water channel aquaporin-4. J. Clin. Invest. 100:1997;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    Verkman, A.S.6
  • 154
    • 0031576555 scopus 로고    scopus 로고
    • Cloning of a novel water and urea-permeable aquaporin from mouse expressed strongly in colon, placenta, liver, and heart
    • Ma T., Yang B., Verkman A.S. Cloning of a novel water and urea-permeable aquaporin from mouse expressed strongly in colon, placenta, liver, and heart. Biochem. Biophys. Res. Commun. 240:1997;324-328
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 324-328
    • Ma, T.1    Yang, B.2    Verkman, A.S.3
  • 155
    • 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 E.J., Epstein C.J., Verkman A.S. Severely impaired urinary concentrating ability in transgenic mice lacking aquaporin-1 water channels. J. Biol. Chem. 273:1998;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    Verkman, A.S.6
  • 156
    • 0033575326 scopus 로고    scopus 로고
    • Defective secretion of saliva in transgenic mice lacking aquaporin-5 water channels
    • Ma T., Song Y., Gillespie A., Carlson E.J., Epstein C.J., Verkman A.S. Defective secretion of saliva in transgenic mice lacking aquaporin-5 water channels. J. Biol. Chem. 274:1999;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
  • 160
    • 0037053303 scopus 로고    scopus 로고
    • Impaired stratum corneum hydration in mice lacking epidermal water channel aquaporin-3
    • Ma T., Hara M., Sougrat R., Verbavatz J.M., Verkman A.S. Impaired stratum corneum hydration in mice lacking epidermal water channel aquaporin-3. J. Biol. Chem. 277:2002;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
  • 161
    • 0037126631 scopus 로고    scopus 로고
    • Polarized trafficking and surface expression of the AQP4 water channel are coordinated by serial and regulated interactions with different clathrin-adaptor complexes
    • Madrid R., Le Maout S., Barrault M.B., Janvier K., Benichou S., Merot J. Polarized trafficking and surface expression of the AQP4 water channel are coordinated by serial and regulated interactions with different clathrin-adaptor complexes. EMBO J. 20:2001;7008-7021
    • (2001) EMBO J. , vol.20 , pp. 7008-7021
    • Madrid, R.1    Le Maout, S.2    Barrault, M.B.3    Janvier, K.4    Benichou, S.5    Merot, J.6
  • 162
    • 0028840171 scopus 로고
    • Quantification of aquaporin-CHIP water channel protein in microdissected renal tubules by fluorescence-based ELISA
    • Maeda Y., Smith B.L., Agre P., Knepper M.A. Quantification of aquaporin-CHIP water channel protein in microdissected renal tubules by fluorescence-based ELISA. J. Clin. Invest. 95:1995;422-428
    • (1995) J. Clin. Invest. , vol.95 , pp. 422-428
    • Maeda, Y.1    Smith, B.L.2    Agre, P.3    Knepper, M.A.4
  • 163
    • 0029813157 scopus 로고    scopus 로고
    • Syntaxin-4 is localized to the apical plasma membrane of rat renal collecting duct cells: Possible role in aquaporin-2 trafficking
    • Mandon B., Chou C.L., Nielsen S., Knepper M.A. Syntaxin-4 is localized to the apical plasma membrane of rat renal collecting duct cells. possible role in aquaporin-2 trafficking J. Clin. Invest. 98:1996;906-913
    • (1996) J. Clin. Invest. , vol.98 , pp. 906-913
    • Mandon, B.1    Chou, C.L.2    Nielsen, S.3    Knepper, M.A.4
  • 164
  • 165
    • 0031011414 scopus 로고    scopus 로고
    • Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1
    • Marinelli R.A., Pham L., Agre P., LaRusso N.F. Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1. J. Biol. Chem. 272:1997;12984-12988
    • (1997) J. Biol. Chem. , vol.272 , pp. 12984-12988
    • Marinelli, R.A.1    Pham, L.2    Agre, P.3    Larusso, N.F.4
  • 167
    • 0034612107 scopus 로고    scopus 로고
    • Water channels: Who needs them anyway?
    • Marples D. Water channels. who needs them anyway? Lancet. 355:2000;1571-1572
    • (2000) Lancet , vol.355 , pp. 1571-1572
    • Marples, D.1
  • 168
    • 0028935612 scopus 로고
    • Lithium-induced downregulation of aquaporin-2 water channel expression in rat kidney medulla
    • Marples D., Christensen S., Christensen E.I., Ottosen P.D., Nielsen S. Lithium-induced downregulation of aquaporin-2 water channel expression in rat kidney medulla. J. Clin. Invest. 95:1995;1838-1845
    • (1995) J. Clin. Invest. , vol.95 , pp. 1838-1845
    • Marples, D.1    Christensen, S.2    Christensen, E.I.3    Ottosen, P.D.4    Nielsen, S.5
  • 170
    • 0036537523 scopus 로고    scopus 로고
    • Heteroligomerization of an aquaporin-2 mutant with wild-type aquaporin-2 and their misrouting to late endosomes/lysosomes explains dominant nephrogenic diabetes insipidus
    • Marr N., Bichet D.G., Lonergan M., Arthus M.F., Jeck N., Seyberth H.W., Rosenthal W., van Os C.H., Oksche A., Deen P.M. Heteroligomerization of an aquaporin-2 mutant with wild-type aquaporin-2 and their misrouting to late endosomes/lysosomes explains dominant nephrogenic diabetes insipidus. Hum. Mol. Genet. 11:2002;779-789
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 779-789
    • Marr, N.1    Bichet, D.G.2    Lonergan, M.3    Arthus, M.F.4    Jeck, N.5    Seyberth, H.W.6    Rosenthal, W.7    Van Os, C.H.8    Oksche, A.9    Deen, P.M.10
  • 173
    • 0032868691 scopus 로고    scopus 로고
    • Water channel protein AQP3 is present in epithelia exposed to the environment of possible water loss
    • Matsuzaki T., Suzuki T., Koyama H., Tanaka S., Takata K. Water channel protein AQP3 is present in epithelia exposed to the environment of possible water loss. J. Histochem. Cytochem. 47:1999;1275-1286
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 1275-1286
    • Matsuzaki, T.1    Suzuki, T.2    Koyama, H.3    Tanaka, S.4    Takata, K.5
  • 174
    • 0033009356 scopus 로고    scopus 로고
    • Aquaporin-5 (AQP5), a water channel protein, in the rat salivary and lacrimal glands: Immunolocalization and effect of secretory stimulation
    • Matsuzaki T., Suzuki T., Koyama H., Tanaka S., Takata K. Aquaporin-5 (AQP5), a water channel protein, in the rat salivary and lacrimal glands. immunolocalization and effect of secretory stimulation Cell Tissue Res. 295:1999;513-521
    • (1999) Cell Tissue Res. , vol.295 , pp. 513-521
    • Matsuzaki, T.1    Suzuki, T.2    Koyama, H.3    Tanaka, S.4    Takata, K.5
  • 175
    • 0000226723 scopus 로고    scopus 로고
    • Water channel protein, aquaporin 3, in epithelial cells
    • S. Hohmann, S. Nielsen (Ed)., Kluwer Academic/Plenum, New York, 2000
    • Matsuzaki, T., Suzuki, T., Takata, K., 2000. Water channel protein, aquaporin 3, in epithelial cells. In: S. Hohmann, S. Nielsen (Ed)., Molecular Biology and Physiology of water and Solute Transport, Kluwer Academic/Plenum, New York, 2000 pp. 167-172.
    • (2000) Molecular Biology and Physiology of Water and Solute Transport , pp. 167-172
    • Matsuzaki, T.1    Suzuki, T.2    Takata, K.3
  • 181
    • 0036720941 scopus 로고    scopus 로고
    • Unimpaired osmotic water permeability and fluid secretion in bile duct epithelia of AQP1 null mice
    • Mennone A., Verkman A.S., Boyer J.L. Unimpaired osmotic water permeability and fluid secretion in bile duct epithelia of AQP1 null mice. Am. J. Physiol. Gastrointest. Liver Physiol. 283:2002;G739-G746
    • (2002) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.283
    • Mennone, A.1    Verkman, A.S.2    Boyer, J.L.3
  • 182
    • 0037633983 scopus 로고    scopus 로고
    • Expression of aquaporin 1 and 5 in the developing mouse inner ear and audiovestibular assessment of an Aqp5 null mutant
    • Merves M., Krane C.M., Dou H., Greinwald J.H., Menon A.G., Choo D. Expression of aquaporin 1 and 5 in the developing mouse inner ear and audiovestibular assessment of an Aqp5 null mutant. J. Assoc. Res. Otolaryngol. 4:2003;264-275
    • (2003) J. Assoc. Res. Otolaryngol. , vol.4 , pp. 264-275
    • Merves, M.1    Krane, C.M.2    Dou, H.3    Greinwald, J.H.4    Menon, A.G.5    Choo, D.6
  • 184
    • 0036696545 scopus 로고    scopus 로고
    • Aquaporin-2 expression in the mammalian cochlea and investigation of its role in meniere's disease
    • Mhatre A.N., Jero J., Chiappini I., Bolasco G., Barbara M., Lalwani A.K. Aquaporin-2 expression in the mammalian cochlea and investigation of its role in meniere's disease. Hear. Res. 170:2002;59-69
    • (2002) Hear. Res. , vol.170 , pp. 59-69
    • Mhatre, A.N.1    Jero, J.2    Chiappini, I.3    Bolasco, G.4    Barbara, M.5    Lalwani, A.K.6
  • 185
  • 186
    • 0031595899 scopus 로고    scopus 로고
    • Selective expression of mercurial-insensitive water channel (AQP-4) gene in Hensen and Claudius cells in the rat cochlea
    • Minami Y., Shimada S., Miyahara H., Matsunaga T., Tohyama M. Selective expression of mercurial-insensitive water channel (AQP-4) gene in Hensen and Claudius cells in the rat cochlea. Acta Otolaryngol. Suppl. 533:1998;19-21
    • (1998) Acta Otolaryngol. Suppl. , vol.533 , pp. 19-21
    • Minami, Y.1    Shimada, S.2    Miyahara, H.3    Matsunaga, T.4    Tohyama, M.5
  • 188
    • 0029947414 scopus 로고    scopus 로고
    • A water channel closely related to rat brain aquaporin 4 is expressed in acid- and pepsinogen-secretory cells of human stomach
    • Misaka T., Abe K., Iwabuchi K., Kusakabe Y., Ichinose M., Miki K., Emori Y., Arai S. A water channel closely related to rat brain aquaporin 4 is expressed in acid- and pepsinogen-secretory cells of human stomach. FEBS Lett. 381:1996;208-212
    • (1996) FEBS Lett. , vol.381 , pp. 208-212
    • Misaka, T.1    Abe, K.2    Iwabuchi, K.3    Kusakabe, Y.4    Ichinose, M.5    Miki, K.6    Emori, Y.7    Arai, S.8
  • 189
    • 0027185799 scopus 로고
    • The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization
    • Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P. The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization. J. Biol. Chem. 268:1993;15772-15778
    • (1993) J. Biol. Chem. , vol.268 , pp. 15772-15778
    • Moon, C.1    Preston, G.M.2    Griffin, C.A.3    Jabs, E.W.4    Agre, P.5
  • 190
    • 0033844419 scopus 로고    scopus 로고
    • Tear secretion by lacrimal glands in transgenic mice lacking water channels AQP1, AQP3, AQP4 and AQP5
    • Moore M., Ma T., Yang B., Verkman A.S. Tear secretion by lacrimal glands in transgenic mice lacking water channels AQP1, AQP3, AQP4 and AQP5. Exp. Eye Res. 70:2000;557-562
    • (2000) Exp. Eye Res. , vol.70 , pp. 557-562
    • Moore, M.1    Ma, T.2    Yang, B.3    Verkman, A.S.4
  • 197
    • 0032053965 scopus 로고    scopus 로고
    • Aquaporin-4 water channel protein in the rat retina and optic nerve: Polarized expression in Muller cells and fibrous astrocytes
    • Nagelhus E.A., Veruki M.L., Torp R., Haug F.M., Laake J.H., Nielsen S., Agre P., Ottersen O.P. Aquaporin-4 water channel protein in the rat retina and optic nerve. polarized expression in Muller cells and fibrous astrocytes J. Neurosci. 18:1998;2506-2519
    • (1998) J. Neurosci. , vol.18 , pp. 2506-2519
    • Nagelhus, E.A.1    Veruki, M.L.2    Torp, R.3    Haug, F.M.4    Laake, J.H.5    Nielsen, S.6    Agre, P.7    Ottersen, O.P.8
  • 198
    • 0033104066 scopus 로고    scopus 로고
    • Immunogold evidence suggests that coupling of K+ siphoning and water transport in rat retinal muller cells is mediated by a coenrichment of Kir4.1 and AQP4 in specific membrane domains
    • Nagelhus E.A., Horio Y., Inanobe A., Fujita A., Haug F.M., Nielsen S., Kurachi Y., Ottersen O.P. Immunogold evidence suggests that coupling of K+ siphoning and water transport in rat retinal muller cells is mediated by a coenrichment of Kir4.1 and AQP4 in specific membrane domains. Glia. 26:1999;47-54
    • (1999) Glia. , vol.26 , pp. 47-54
    • Nagelhus, E.A.1    Horio, Y.2    Inanobe, A.3    Fujita, A.4    Haug, F.M.5    Nielsen, S.6    Kurachi, Y.7    Ottersen, O.P.8
  • 200
    • 0033600555 scopus 로고    scopus 로고
    • Heterotetrameric composition of aquaporin- water channels
    • Neely J.D., Christensen B.M., Nielsen S., Agre P. Heterotetrameric composition of aquaporin- water channels. Biochemistry. 38:1999;11156-11163
    • (1999) Biochemistry , vol.38 , pp. 11156-11163
    • Neely, J.D.1    Christensen, B.M.2    Nielsen, S.3    Agre, P.4
  • 202
  • 204
    • 0041721625 scopus 로고    scopus 로고
    • PH and calcium regulate the water permeability of aquaporin 0
    • Nemeth-Cahalan K.L., Hall J.E. pH and calcium regulate the water permeability of aquaporin 0. J. Biol. Chem. 275:2000;6777-6782
    • (2000) J. Biol. Chem. , vol.275 , pp. 6777-6782
    • Nemeth-Cahalan, K.L.1    Hall, J.E.2
  • 205
    • 0035697123 scopus 로고    scopus 로고
    • Tissue distribution and membrane localization of aquaporin-9 water channel: Evidence for sex-linked differences in liver
    • Nicchia G.P., Frigeri A., Nico B., Ribatti D., Svelto M. Tissue distribution and membrane localization of aquaporin-9 water channel. evidence for sex-linked differences in liver J. Histochem. Cytochem. 49:2001;1547-1556
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 1547-1556
    • Nicchia, G.P.1    Frigeri, A.2    Nico, B.3    Ribatti, D.4    Svelto, M.5
  • 207
    • 0027306170 scopus 로고
    • Distribution of the aquaporin CHIP in secretory and resorptive epithelia and capillary endothelia
    • Nielsen S., Smith B.L., Christensen E.I., Agre P. Distribution of the aquaporin CHIP in secretory and resorptive epithelia and capillary endothelia. Proc. Natl. Acad. Sci. USA. 90:1993;7275-7279
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7275-7279
    • Nielsen, S.1    Smith, B.L.2    Christensen, E.I.3    Agre, P.4
  • 208
    • 0027475944 scopus 로고
    • CHIP28 water channels are localized in constitutively water-permeable segments of the nephron
    • Nielsen S., Smith B.L., Christensen E.I., Knepper M.A., Agre P. CHIP28 water channels are localized in constitutively water-permeable segments of the nephron. J. Cell Biol. 120:1993;371-383
    • (1993) J. Cell Biol. , vol.120 , pp. 371-383
    • Nielsen, S.1    Smith, B.L.2    Christensen, E.I.3    Knepper, M.A.4    Agre, P.5
  • 209
    • 0028889112 scopus 로고
    • Vasopressin 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., Christensen E.I., Kishore B.K., Knepper M.A. Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane. Proc. Natl. Acad. Sci. USA. 92:1995;1013-1017
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1013-1017
    • Nielsen, S.1    Chou, C.L.2    Marples, D.3    Christensen, E.I.4    Kishore, B.K.5    Knepper, M.A.6
  • 210
    • 0028972114 scopus 로고
    • Expression of VAMP-2-like protein in kidney collecting duct intracellular vesicles. Colocalization with aquaporin-2 water channels
    • Nielsen S., Marples D., Birn H., Mohtashami M., Dalby N.O., Trimble M., Knepper M. Expression of VAMP-2-like protein in kidney collecting duct intracellular vesicles. Colocalization with aquaporin-2 water channels. J. Clin. Invest. 96:1995;1834-1844
    • (1995) J. Clin. Invest. , vol.96 , pp. 1834-1844
    • Nielsen, S.1    Marples, D.2    Birn, H.3    Mohtashami, M.4    Dalby, N.O.5    Trimble, M.6    Knepper, M.7
  • 211
    • 0029045996 scopus 로고
    • Aquaporin-1 water channels in short and long loop descending thin limbs and in descending vasa recta in rat kidney
    • Nielsen S., Pallone T., Smith B.L., Christensen E.I., Agre P., Maunsbach A.B. Aquaporin-1 water channels in short and long loop descending thin limbs and in descending vasa recta in rat kidney. Am. J. Physiol. 268:1995;F1023-F1037
    • (1995) Am. J. Physiol. , vol.268
    • Nielsen, S.1    Pallone, T.2    Smith, B.L.3    Christensen, E.I.4    Agre, P.5    Maunsbach, A.B.6
  • 212
    • 0030657804 scopus 로고    scopus 로고
    • Aquaporins in complex tissues. II. Subcellular distribution in respiratory and glandular tissues of rat
    • Nielsen S., King L.S., Christensen B.M., Agre P. Aquaporins in complex tissues. II. Subcellular distribution in respiratory and glandular tissues of rat. Am. J. Physiol. 273:1997;C1549-C1561
    • (1997) Am. J. Physiol. , vol.273
    • Nielsen, S.1    King, L.S.2    Christensen, B.M.3    Agre, P.4
  • 213
    • 0031022918 scopus 로고    scopus 로고
    • Specialized membrane domains for water transport in glial cells: High-resolution immunogold cytochemistry of aquaporin-4 in rat brain
    • Nielsen S., Nagelhus E.A., Amiry-Moghaddam M., Bourque C., Agre P., Ottersen O.P. Specialized membrane domains for water transport in glial cells. high-resolution immunogold cytochemistry of aquaporin-4 in rat brain J. Neurosci. 17:1997;171-180
    • (1997) J. Neurosci. , vol.17 , pp. 171-180
    • Nielsen, S.1    Nagelhus, E.A.2    Amiry-Moghaddam, M.3    Bourque, C.4    Agre, P.5    Ottersen, O.P.6
  • 218
    • 0141867750 scopus 로고    scopus 로고
    • Fluid and cellular pathways of rat lymph nodes in relation to lymphatic labyrinths and aquaporin-1 expression
    • Ohtani O., Ohtani Y., Carati C.J., Gannon B.J. Fluid and cellular pathways of rat lymph nodes in relation to lymphatic labyrinths and aquaporin-1 expression. Arch. Histol. Cytol. 66:2003;261-272
    • (2003) Arch. Histol. Cytol. , vol.66 , pp. 261-272
    • Ohtani, O.1    Ohtani, Y.2    Carati, C.J.3    Gannon, B.J.4
  • 219
    • 0037431062 scopus 로고    scopus 로고
    • Aquaporin-9 is expressed in a mucus-secreting goblet cell subset in the small intestine
    • Okada S., Misaka T., Matsumoto I., Watanabe H., Abe K. Aquaporin-9 is expressed in a mucus-secreting goblet cell subset in the small intestine. FEBS Lett. 540:2003;157-162
    • (2003) FEBS Lett. , vol.540 , pp. 157-162
    • Okada, S.1    Misaka, T.2    Matsumoto, I.3    Watanabe, H.4    Abe, K.5
  • 220
    • 0037379798 scopus 로고    scopus 로고
    • Bilateral congenital cataracts result from a gain-of-function mutation in the gene for aquaporin-0 in mice
    • Okamura T., Miyoshi I., Takahashi K., Mototani Y., Ishigaki S., Kon Y., Kasai N. Bilateral congenital cataracts result from a gain-of-function mutation in the gene for aquaporin-0 in mice. Genomics. 81:2003;361-368
    • (2003) Genomics , vol.81 , pp. 361-368
    • Okamura, T.1    Miyoshi, I.2    Takahashi, K.3    Mototani, Y.4    Ishigaki, S.5    Kon, Y.6    Kasai, N.7
  • 221
    • 0033955098 scopus 로고    scopus 로고
    • Requirement of aquaporin-1 for NaCl-driven water transport across descending vasa recta
    • Pallone T.L., Edwards A., Ma T., Silldorff E.P., Verkman A.S. Requirement of aquaporin-1 for NaCl-driven water transport across descending vasa recta. J. Clin. Invest. 105:2000;215-222
    • (2000) J. Clin. Invest. , vol.105 , pp. 215-222
    • Pallone, T.L.1    Edwards, A.2    Ma, T.3    Silldorff, E.P.4    Verkman, A.S.5
  • 223
    • 0029910115 scopus 로고    scopus 로고
    • Phylogenetic characterization of the MIP family of transmembrane channel proteins
    • Park J.H., Saier., M.H. Jr. Phylogenetic characterization of the MIP family of transmembrane channel proteins. J. Membr. Biol. 153:1996;171-180
    • (1996) J. Membr. Biol. , vol.153 , pp. 171-180
    • Park, J.H.1    Saier2    Jr., M.H.3
  • 227
    • 0026332210 scopus 로고
    • Isolation of the cDNA for erythrocyte integral membrane protein of 28 kDa: Member of an ancient channel family
    • Preston G.M., Agre P. Isolation of the cDNA for erythrocyte integral membrane protein of 28. kDa member of an ancient channel family Proc. Natl. Acad. Sci. USA. 88:1991;11110-11114
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11110-11114
    • Preston, G.M.1    Agre, P.2
  • 228
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • Preston G.M., Carroll T.P., Guggino W.B., Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science. 256:1992;385-387
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 229
    • 0027472168 scopus 로고
    • The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel
    • Preston G.M., Jung J.S., Guggino W.B., Agre P. The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel. J. Biol. Chem. 268:1993;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
  • 230
    • 0028088012 scopus 로고
    • Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels
    • Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P. Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels. Science. 265:1994;1585-1587
    • (1994) Science , vol.265 , pp. 1585-1587
    • Preston, G.M.1    Smith, B.L.2    Zeidel, M.L.3    Moulds, J.J.4    Agre, P.5
  • 232
    • 0028919341 scopus 로고
    • Molecular cloning and characterization of an aquaporin cDNA from salivary, lacrimal, and respiratory tissues
    • Raina S., Preston G.M., Guggino W.B., Agre P. Molecular cloning and characterization of an aquaporin cDNA from salivary, lacrimal, and respiratory tissues. J. Biol. Chem. 270:1995;1908-1912
    • (1995) J. Biol. Chem. , vol.270 , pp. 1908-1912
    • Raina, S.1    Preston, G.M.2    Guggino, W.B.3    Agre, P.4
  • 234
    • 0032578454 scopus 로고    scopus 로고
    • Direct immunogold labeling of aquaporin-4 in square arrays of astrocyte and ependymocyte plasma membranes in rat brain and spinal cord
    • Rash J.E., Yasumura T., Hudson C.S., Agre P., Nielsen S. Direct immunogold labeling of aquaporin-4 in square arrays of astrocyte and ependymocyte plasma membranes in rat brain and spinal cord. Proc. Natl. Acad. Sci. USA. 95:1998;11981-11986
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11981-11986
    • Rash, J.E.1    Yasumura, T.2    Hudson, C.S.3    Agre, P.4    Nielsen, S.5
  • 235
    • 0034636971 scopus 로고    scopus 로고
    • Three-dimensional fold of the human AQP1 water channel determined at 4 Å resolution by electron crystallography of two-dimensional crystals embedded in ice
    • Ren G., Cheng A., Reddy V., Melnyk P., Mitra A.K. Three-dimensional fold of the human AQP1 water channel determined at 4. Å resolution by electron crystallography of two-dimensional crystals embedded in ice J. Mol. Biol. 301:2000;369-387
    • (2000) J. Mol. Biol. , vol.301 , pp. 369-387
    • Ren, G.1    Cheng, A.2    Reddy, V.3    Melnyk, P.4    Mitra, A.K.5
  • 236
    • 0035852730 scopus 로고    scopus 로고
    • Visualization of a water-selective pore by electron crystallography in vitreous ice
    • Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K. Visualization of a water-selective pore by electron crystallography in vitreous ice. Proc. Natl. Acad. Sci. USA. 98:2001;1398-1403
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1398-1403
    • Ren, G.1    Reddy, V.S.2    Cheng, A.3    Melnyk, P.4    Mitra, A.K.5
  • 242
    • 0031919153 scopus 로고    scopus 로고
    • Aquaporin-2 and -3: Representatives of two subgroups of the aquaporin family colocalized in the kidney collecting duct
    • Sasaki S., Ishibashi K., Marumo F. Aquaporin-2 and -3. representatives of two subgroups of the aquaporin family colocalized in the kidney collecting duct Annu. Rev. Physiol. 60:1998;199-220
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 199-220
    • Sasaki, S.1    Ishibashi, K.2    Marumo, F.3
  • 245
    • 0030031158 scopus 로고    scopus 로고
    • Mutations in the founder of the MIP gene family underlie cataract development in the mouse
    • Shiels A., Bassnett S. Mutations in the founder of the MIP gene family underlie cataract development in the mouse. Nat. Genet. 12:1996;212-215
    • (1996) Nat. Genet. , vol.12 , pp. 212-215
    • Shiels, A.1    Bassnett, S.2
  • 246
    • 0033729222 scopus 로고    scopus 로고
    • Disruption of lens fiber cell architecture in mice expressing a chimeric AQP0-LTR protein
    • Shiels A., Mackay D., Bassnett S., Al-Ghoul K., Kuszak J. Disruption of lens fiber cell architecture in mice expressing a chimeric AQP0-LTR protein. FASEB J. 14:2000;2207-2212
    • (2000) FASEB J. , vol.14 , pp. 2207-2212
    • Shiels, A.1    MacKay, D.2    Bassnett, S.3    Al-Ghoul, K.4    Kuszak, J.5
  • 249
    • 0027980902 scopus 로고
    • Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens
    • Smith B.L., Preston G.M., Spring F.A., Anstee D.J., Agre P. Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens. J. Clin. Invest. 94:1994;1043-1049
    • (1994) J. Clin. Invest. , vol.94 , pp. 1043-1049
    • Smith, B.L.1    Preston, G.M.2    Spring, F.A.3    Anstee, D.J.4    Agre, P.5
  • 250
    • 0030472792 scopus 로고    scopus 로고
    • Molecular machinery mediating vesicle budding, docking and fusion
    • Sollner T.H., Rothman J.E. Molecular machinery mediating vesicle budding, docking and fusion. Cell Struct Funct. 21:1996;407-412
    • (1996) Cell Struct Funct. , vol.21 , pp. 407-412
    • Sollner, T.H.1    Rothman, J.E.2
  • 251
    • 0035798592 scopus 로고    scopus 로고
    • Aquaporin-5 dependent fluid secretion in airway submucosal glands
    • Song Y., Verkman A.S. Aquaporin-5 dependent fluid secretion in airway submucosal glands. J. Biol. Chem. 276:2001;41288-41292
    • (2001) J. Biol. Chem. , vol.276 , pp. 41288-41292
    • Song, Y.1    Verkman, A.S.2
  • 252
    • 0034659494 scopus 로고    scopus 로고
    • Role of aquaporins in alveolar fluid clearance in neonatal and adult lung, and in oedema formation following acute lung injury: Studies in transgenic aquaporin null mice
    • Song Y., Fukuda N., Bai C., Ma T., Matthay M.A., Verkman A.S. Role of aquaporins in alveolar fluid clearance in neonatal and adult lung, and in oedema formation following acute lung injury. studies in transgenic aquaporin null mice J. Physiol. 525:2000;771-779
    • (2000) J. Physiol. , vol.525 , pp. 771-779
    • Song, Y.1    Fukuda, N.2    Bai, C.3    Ma, T.4    Matthay, M.A.5    Verkman, A.S.6
  • 254
    • 0034971953 scopus 로고    scopus 로고
    • Role of aquaporin water channels in airway fluid transport, humidification, and surface liquid hydration
    • Song Y., Jayaraman S., Yang B., Matthay M.A., Verkman A.S. Role of aquaporin water channels in airway fluid transport, humidification, and surface liquid hydration. J. Gen. Physiol. 117:2001;573-582
    • (2001) J. Gen. Physiol. , vol.117 , pp. 573-582
    • Song, Y.1    Jayaraman, S.2    Yang, B.3    Matthay, M.A.4    Verkman, A.S.5
  • 255
    • 0036623643 scopus 로고    scopus 로고
    • Localization of aquaporin-5 in sweat glands and functional analysis using knockout mice
    • Song Y., Sonawane N., Verkman A.S. Localization of aquaporin-5 in sweat glands and functional analysis using knockout mice. J. Physiol. 54:2002;561-568
    • (2002) J. Physiol. , vol.54 , pp. 561-568
    • Song, Y.1    Sonawane, N.2    Verkman, A.S.3
  • 258
    • 0033466768 scopus 로고    scopus 로고
    • Epithelial fluid transport - A century of investigation
    • Spring K.R. Epithelial fluid transport - a century of investigation. News Physiol. Sci. 14:1999;92-98
    • (1999) News Physiol. Sci. , vol.14 , pp. 92-98
    • Spring, K.R.1
  • 259
    • 0030455493 scopus 로고    scopus 로고
    • Characterization of the transmembrane orientation of aquaporin-1 using antibodies to recombinant fusion proteins
    • Stamer W.D., Snyder R.W., Regan J.W. Characterization of the transmembrane orientation of aquaporin-1 using antibodies to recombinant fusion proteins. Biochemistry. 35:1996;16313-16318
    • (1996) Biochemistry , vol.35 , pp. 16313-16318
    • Stamer, W.D.1    Snyder, R.W.2    Regan, J.W.3
  • 261
    • 0029188011 scopus 로고
    • Immunolocalization of aquaporin chip in the guinea pig inner ear
    • Stankovic K.M., Adams J.C., Brown D. Immunolocalization of aquaporin chip in the guinea pig inner ear. Am. J. Physiol. 269:1995;C1450-C1456
    • (1995) Am. J. Physiol. , vol.269
    • Stankovic, K.M.1    Adams, J.C.2    Brown, D.3
  • 262
    • 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 L.S., Agre P., Kiss R., Delporte C. Abnormal distribution of aquaporin-5 water channel protein in salivary glands from Sjogren's syndrome patients. Lab. Invest. 81:2001;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    Delporte, C.6
  • 264
    • 0035803910 scopus 로고    scopus 로고
    • Osmotic stress up-regulates aquaporin-3 gene expression in cultured human keratinocytes
    • Sugiyama Y., Ota Y., Hara M., Inoue S. Osmotic stress up-regulates aquaporin-3 gene expression in cultured human keratinocytes. Biochim. Biophys. Acta. 1522:2001;82-88
    • (2001) Biochim. Biophys. Acta , vol.1522 , pp. 82-88
    • Sugiyama, Y.1    Ota, Y.2    Hara, M.3    Inoue, S.4
  • 265
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui H., Han B.G., Lee J.K., Walian P., Jap B.K. Structural basis of water-specific transport through the AQP1 water channel. Nature. 414:2001;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
  • 267
    • 0032970957 scopus 로고    scopus 로고
    • Immunohistochemical localization of a water channel, aquaporin 7 (AQP7), in the rat testis
    • Suzuki-Toyota F., Ishibashi K., Yuasa S. Immunohistochemical localization of a water channel, aquaporin 7 (AQP7), in the rat testis. Cell Tissue. Res. 295:1999;279-285
    • (1999) Cell Tissue. Res. , vol.295 , pp. 279-285
    • Suzuki-Toyota, F.1    Ishibashi, K.2    Yuasa, S.3
  • 270
    • 0025980323 scopus 로고
    • +-dependent active type and erythrocyte/HepG2-type glucose transporters in rat kidney: Immunofluorescence and immunogold study
    • +-dependent active type and erythrocyte/HepG2-type glucose transporters in rat kidney. immunofluorescence and immunogold study J. Histochem. Cytochem. 39:1991;287-298
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 287-298
    • Takata, K.1    Kasahara, T.2    Kasahara, M.3    Ezaki, O.4    Hirano, H.5
  • 272
    • 0001346505 scopus 로고
    • Mammalian sugar transporters: Their localization and link to cellular functions
    • Takata K., Kasahara M., Oka Y., Hirano H. Mammalian sugar transporters. their localization and link to cellular functions Acta Histochem. Cytochem. 26:1993;165-178
    • (1993) Acta Histochem. Cytochem. , vol.26 , pp. 165-178
    • Takata, K.1    Kasahara, M.2    Oka, Y.3    Hirano, H.4
  • 273
    • 0344484852 scopus 로고    scopus 로고
    • Glucose transporters in the transepithelial transport of glucose
    • Takata K. Glucose transporters in the transepithelial transport of glucose. J. Electron Microsc. (Tokyo). 45:1996;275-284
    • (1996) J. Electron Microsc. (Tokyo) , vol.45 , pp. 275-284
    • Takata, K.1
  • 274
    • 0030890825 scopus 로고    scopus 로고
    • Transport of glucose across the blood-tissue barriers
    • Takata K., Hirano H., Kasahara M. Transport of glucose across the blood-tissue barriers. Int Rev Cytol. 172:1997;1-53
    • (1997) Int Rev Cytol. , vol.172 , pp. 1-53
    • Takata, K.1    Hirano, H.2    Kasahara, M.3
  • 277
    • 0037730396 scopus 로고    scopus 로고
    • CAMP-induced AQP2 translocation is associated with RhoA inhibition through RhoA phosphorylation and interaction with RhoGDI
    • Tamma G., Klussmann E., Procino G., Svelto M., Rosenthal W., Valenti G. cAMP-induced AQP2 translocation is associated with RhoA inhibition through RhoA phosphorylation and interaction with RhoGDI. J. Cell Sci. 116:2003;1519-1525
    • (2003) J. Cell Sci. , vol.116 , pp. 1519-1525
    • Tamma, G.1    Klussmann, E.2    Procino, G.3    Svelto, M.4    Rosenthal, W.5    Valenti, G.6
  • 278
    • 0032524048 scopus 로고    scopus 로고
    • Defective aquaporin-2 trafficking in nephrogenic diabetes insipidus and correction by chemical chaperones
    • Tamarappoo B.K., Verkman A.S. Defective aquaporin-2 trafficking in nephrogenic diabetes insipidus and correction by chemical chaperones. J. Clin. Invest. 101:1998;2257-2267
    • (1998) J. Clin. Invest. , vol.101 , pp. 2257-2267
    • Tamarappoo, B.K.1    Verkman, A.S.2
  • 279
    • 0033521139 scopus 로고    scopus 로고
    • Misfolding of mutant aquaporin-2 water channels in nephrogenic diabetes insipidus
    • Tamarappoo B.K., Yang B., Verkman A.S. Misfolding of mutant aquaporin-2 water channels in nephrogenic diabetes insipidus. J. Biol. Chem. 274:1999;34825-34831
    • (1999) J. Biol. Chem. , vol.274 , pp. 34825-34831
    • Tamarappoo, B.K.1    Yang, B.2    Verkman, A.S.3
  • 281
    • 0037166326 scopus 로고    scopus 로고
    • Aquaporin deletion in mice reduces corneal water permeability and delays restoration of transparency after swelling
    • Thiagarajah J.R., Verkman A.S. Aquaporin deletion in mice reduces corneal water permeability and delays restoration of transparency after swelling. J. Biol. Chem. 277:2002;19139-19144
    • (2002) J. Biol. Chem. , vol.277 , pp. 19139-19144
    • Thiagarajah, J.R.1    Verkman, A.S.2
  • 282
    • 0035799116 scopus 로고    scopus 로고
    • Defective cellular trafficking of lacrimal gland aquaporin-5 in Sjogren's syndrome
    • Tsubota K., Hirai S., King L.S., Agre P., Ishida N. Defective cellular trafficking of lacrimal gland aquaporin-5 in Sjogren's syndrome. Lancet. 357:2001;688-689
    • (2001) Lancet , vol.357 , pp. 688-689
    • Tsubota, K.1    Hirai, S.2    King, L.S.3    Agre, P.4    Ishida, N.5
  • 284
    • 0032739871 scopus 로고    scopus 로고
    • Functional and molecular characterization of the human neutral solute channel aquaporin-9
    • Tsukaguchi H., Weremowicz S., Morton C.C., Hediger M.A. Functional and molecular characterization of the human neutral solute channel aquaporin-9. Am. J. Physiol. 277:1999;F685-F696
    • (1999) Am. J. Physiol. , vol.277
    • Tsukaguchi, H.1    Weremowicz, S.2    Morton, C.C.3    Hediger, M.A.4
  • 285
    • 0029937266 scopus 로고    scopus 로고
    • Quantitative analysis of aquaporin mRNA expression in rat tissues by RNase protection assay
    • Umenishi F., Verkman A.S., Gropper M.A. Quantitative analysis of aquaporin mRNA expression in rat tissues by RNase protection assay. DNA Cell Biol. 15:1996;475-480
    • (1996) DNA Cell Biol. , vol.15 , pp. 475-480
    • Umenishi, F.1    Verkman, A.S.2    Gropper, M.A.3
  • 286
    • 0034075677 scopus 로고    scopus 로고
    • Camp regulated membrane diffusion of a green fluorescent protein-aquaporin 2 chimera
    • Umenishi F., Verbavatz J.M., Verkman A.S. Camp regulated membrane diffusion of a green fluorescent protein-aquaporin 2 chimera. Biophys. J. 78:2000;1024-1035
    • (2000) Biophys. J. , vol.78 , pp. 1024-1035
    • Umenishi, F.1    Verbavatz, J.M.2    Verkman, A.S.3
  • 290
    • 0037428485 scopus 로고    scopus 로고
    • Hypertonicity is involved in redirecting the aquaporin-2 water channel into the basolateral, instead of the apical, plasma membrane of renal epithelial cells
    • van Balkom B.W., van Raak M., Breton S., Pastor-Soler N., Bouley R., van der Sluijsm P., Brown D., Deen P.M. Hypertonicity is involved in redirecting the aquaporin-2 water channel into the basolateral, instead of the apical, plasma membrane of renal epithelial cells. J. Biol. Chem. 278:2003;1101-1107
    • (2003) J. Biol. Chem. , vol.278 , pp. 1101-1107
    • Van Balkom, B.W.1    Van Raak, M.2    Breton, S.3    Pastor-Soler, N.4    Bouley, R.5    Van Der Sluijsm, P.6    Brown, D.7    Deen, P.M.8
  • 291
    • 0026639874 scopus 로고
    • Functional reconstitution of the isolated erythrocyte water channel CHIP28
    • van Hoek A.N., Verkman A.S. Functional reconstitution of the isolated erythrocyte water channel CHIP28. J. Biol. Chem. 267:1992;18267-18269
    • (1992) J. Biol. Chem. , vol.267 , pp. 18267-18269
    • Van Hoek, A.N.1    Verkman, A.S.2
  • 292
    • 0031668235 scopus 로고    scopus 로고
    • Freeze-fracture analysis of plasma membranes of CHO cells stably expressing aquaporins 1-5
    • van Hoek A.N., Yang B., Kirmiz S., Brown D. Freeze-fracture analysis of plasma membranes of CHO cells stably expressing aquaporins 1-5. J. Membr. Biol. 165:1998;243-254
    • (1998) J. Membr. Biol. , vol.165 , pp. 243-254
    • Van Hoek, A.N.1    Yang, B.2    Kirmiz, S.3    Brown, D.4
  • 293
    • 0034014277 scopus 로고    scopus 로고
    • Aquaporin-4 is expressed in basolateral membranes of proximal tubule S3 segments in mouse kidney
    • van Hoek A.N., Ma T., Yang B., Verkman A.S., Brown D. Aquaporin-4 is expressed in basolateral membranes of proximal tubule S3 segments in mouse kidney. Am. J. Physiol. Renal Physiol. 278:2000;F310-F316
    • (2000) Am. J. Physiol. Renal Physiol. , vol.278
    • Van Hoek, A.N.1    Ma, T.2    Yang, B.3    Verkman, A.S.4    Brown, D.5
  • 296
    • 0031429315 scopus 로고    scopus 로고
    • Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12 families with congenital nephrogenic diabetes insipidus
    • Vargas-Poussou R., Forestier L., Dautzenberg M.D., Niaudet P., Dechaux M., Antignac C. Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12 families with congenital nephrogenic diabetes insipidus. J. Am. Soc. Nephrol. 8:1997;1855-1862
    • (1997) J. Am. Soc. Nephrol. , vol.8 , pp. 1855-1862
    • Vargas-Poussou, R.1    Forestier, L.2    Dautzenberg, M.D.3    Niaudet, P.4    Dechaux, M.5    Antignac, C.6
  • 299
    • 0030775672 scopus 로고    scopus 로고
    • Absence of orthogonal arrays in kidney, brain and muscle from transgenic knockout mice lacking water channel aquaporin-4
    • Verbavatz J.-M., Ma T., Gobin R., Verkman A.S. Absence of orthogonal arrays in kidney, brain and muscle from transgenic knockout mice lacking water channel aquaporin-4. J. Cell Sci. 110:1997;2855-2860
    • (1997) J. Cell Sci. , vol.110 , pp. 2855-2860
    • Verbavatz, J.-M.1    Ma, T.2    Gobin, R.3    Verkman, A.S.4
  • 300
    • 0024377217 scopus 로고
    • Mechanisms and regulation of water permeability in renal epithelia
    • Verkman A.S. Mechanisms and regulation of water permeability in renal epithelia. Am. J. Physiol. 257:1989;C837-C850
    • (1989) Am. J. Physiol. , vol.257
    • Verkman, A.S.1
  • 301
    • 0032905870 scopus 로고    scopus 로고
    • Lessons on renal physiology from transgenic mice lacking aquaporin water channels
    • Verkman A.S. Lessons on renal physiology from transgenic mice lacking aquaporin water channels. J. Am. Soc. Nephrol. 10:1999;1126-1135
    • (1999) J. Am. Soc. Nephrol. , vol.10 , pp. 1126-1135
    • Verkman, A.S.1
  • 302
    • 0033862584 scopus 로고    scopus 로고
    • Physiological importance of aquaporins: Lessons from knockout mice
    • Verkman A.S. Physiological importance of aquaporins. lessons from knockout mice Curr. Opin. Nephrol. Hypertens. 9:2000;517-522
    • (2000) Curr. Opin. Nephrol. Hypertens. , vol.9 , pp. 517-522
    • Verkman, A.S.1
  • 303
    • 0037331359 scopus 로고    scopus 로고
    • Role of aquaporin water channels in eye function
    • Verkman A.S. Role of aquaporin water channels in eye function. Exp. Eye Res. 76:2003;137-143
    • (2003) Exp. Eye Res. , vol.76 , pp. 137-143
    • Verkman, A.S.1
  • 307
    • 0034103872 scopus 로고    scopus 로고
    • Role of water channels in fluid transport studied by phenotype analysis of aquaporin knockout mice
    • Verkman A.S., Yang B., Song Y., Manley G.T., Ma T. Role of water channels in fluid transport studied by phenotype analysis of aquaporin knockout mice. Exp. Physiol. 85:2000;233S-241S
    • (2000) Exp. Physiol. , vol.85
    • Verkman, A.S.1    Yang, B.2    Song, Y.3    Manley, G.T.4    Ma, T.5
  • 308
    • 0032886241 scopus 로고    scopus 로고
    • Differential upregulation of aquaporin-4 mRNA expression in reactive astrocytes after brain injury: Potential role in brain edema
    • Vizuete M.L., Venero J.L., Vargas C., Ilundain A.A., Echevarria M., Machado A., Cano J. Differential upregulation of aquaporin-4 mRNA expression in reactive astrocytes after brain injury. potential role in brain edema Neurobiol. Dis. 6:1999;245-258
    • (1999) Neurobiol. Dis. , vol.6 , pp. 245-258
    • Vizuete, M.L.1    Venero, J.L.2    Vargas, C.3    Ilundain, A.A.4    Echevarria, M.5    MacHado, A.6    Cano, J.7
  • 313
    • 0035787305 scopus 로고    scopus 로고
    • Intracellular organization of insulin signaling and GLUT4 translocation
    • Watson R.T., Pessin J.E. Intracellular organization of insulin signaling and GLUT4 translocation. Recent Prog. Horm. Res. 56:2001;175-193
    • (2001) Recent Prog. Horm. Res. , vol.56 , pp. 175-193
    • Watson, R.T.1    Pessin, J.E.2
  • 314
    • 0034488737 scopus 로고    scopus 로고
    • Evidence that aquaporin-8 is located in the basolateral membrane of rat submandibular gland acinar cells
    • Wellner R.B., Hoque A.T., Goldsmith C.M., Baum B.J. Evidence that aquaporin-8 is located in the basolateral membrane of rat submandibular gland acinar cells. Pflugers Arch. 441:2000;49-56
    • (2000) Pflugers Arch. , vol.441 , pp. 49-56
    • Wellner, R.B.1    Hoque, A.T.2    Goldsmith, C.M.3    Baum, B.J.4
  • 315
    • 0032991514 scopus 로고    scopus 로고
    • Urinary excretion of aquaporin-2 in rat is mediated by a vasopressin-dependent apical pathway
    • Wen H., Frokiaer J., Kwon T.H., Nielsen S. Urinary excretion of aquaporin-2 in rat is mediated by a vasopressin-dependent apical pathway. J. Am. Soc. Nephrol. 10:1999;1416-1429
    • (1999) J. Am. Soc. Nephrol. , vol.10 , pp. 1416-1429
    • Wen, H.1    Frokiaer, J.2    Kwon, T.H.3    Nielsen, S.4
  • 317
    • 0029086229 scopus 로고
    • CDNA cloning, gene organization, and chromosomal localization of a human mercurial insensitive water channel
    • Yang B., Ma T., Verkman A.S. cDNA cloning, gene organization, and chromosomal localization of a human mercurial insensitive water channel. Evidence for distinct transcriptional units. J. Biol. Chem. 270:1995;22907-22913
    • (1995) Evidence for Distinct Transcriptional Units. J. Biol. Chem. , vol.270 , pp. 22907-22913
    • Yang, B.1    Ma, T.2    Verkman, A.S.3
  • 318
    • 0029926097 scopus 로고    scopus 로고
    • The mercurial insensitive water channel (AQP-4) forms orthogonal arrays in stably transfected Chinese hamster ovary cells
    • Yang B., Brown D., Verkman A.S. The mercurial insensitive water channel (AQP-4) forms orthogonal arrays in stably transfected Chinese hamster ovary cells. J. Biol. Chem. 271:1996;4577-4580
    • (1996) J. Biol. Chem. , vol.271 , pp. 4577-4580
    • Yang, B.1    Brown, D.2    Verkman, A.S.3
  • 319
    • 0032946860 scopus 로고    scopus 로고
    • Reduced osmotic water permeability of the peritoneal barrier in aquaporin-1 knockout mice
    • Yang B., Folkesson H.G., Yang J., Matthay M.A., Ma T., Verkman A.S. Reduced osmotic water permeability of the peritoneal barrier in aquaporin-1 knockout mice. Am. J. Physiol. 276:1999;C76-C81
    • (1999) Am. J. Physiol. , vol.276
    • Yang, B.1    Folkesson, H.G.2    Yang, J.3    Matthay, M.A.4    Ma, T.5    Verkman, A.S.6
  • 320
    • 0034104076 scopus 로고    scopus 로고
    • Partial correction of the urinary concentrating defect in aquaporin-1 null mice by adenovirus-mediated gene delivery
    • Yang B., Ma T., Dong J.Y., Verkman A.S. Partial correction of the urinary concentrating defect in aquaporin-1 null mice by adenovirus-mediated gene delivery. Hum. Gene Ther. 11:2000;567-575
    • (2000) Hum. Gene Ther. , vol.11 , pp. 567-575
    • Yang, B.1    Ma, T.2    Dong, J.Y.3    Verkman, A.S.4
  • 322
    • 0035951776 scopus 로고    scopus 로고
    • Neonatal mortality in an aquaporin-2 knock-in mouse model of recessive nephrogenic diabetes insipidus
    • Yang B., Gillespie A., Carlson E.J., Epstein C.J., Verkman A.S. Neonatal mortality in an aquaporin-2 knock-in mouse model of recessive nephrogenic diabetes insipidus. J. Biol. Chem. 276:2001;2775-2779
    • (2001) J. Biol. Chem. , vol.276 , pp. 2775-2779
    • Yang, B.1    Gillespie, A.2    Carlson, E.J.3    Epstein, C.J.4    Verkman, A.S.5
  • 323
    • 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 J.D., Menon A.G. Cyclic amp regulates aquaporin 5 expression at both transcriptional and post-transcriptional levels through a protein kinase a pathway. J. Biol. Chem. 278:2003;32173-32180
    • (2003) J. Biol. Chem. , vol.278 , pp. 32173-32180
    • Yang, F.1    Kawedia, J.D.2    Menon, A.G.3
  • 324
    • 0033547240 scopus 로고    scopus 로고
    • Rapid gating and anion permeability of an intracellular aquaporin
    • Yasui M., Hazama A., Kwon T.H., Nielsen S., Guggino W.B., Agre P. Rapid gating and anion permeability of an intracellular aquaporin. Nature. 402:1999;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    Agre, P.6
  • 325
  • 328
    • 0036211732 scopus 로고    scopus 로고
    • Passive water transport in biological pores
    • Zeuthen T., MacAulay N. Passive water transport in biological pores. Int. Rev. Cytol. 215:2002;203-230
    • (2002) Int. Rev. Cytol. , vol.215 , pp. 203-230
    • Zeuthen, T.1    MacAulay, N.2
  • 329
    • 0027472037 scopus 로고
    • Cloning, functional analysis and cell localization of a kidney proximal tubule water transporter homologous to CHIP28
    • Zhang R., Skach W., Hasegawa H., van Hoek A.N., Verkman A.S. Cloning, functional analysis and cell localization of a kidney proximal tubule water transporter homologous to CHIP28. J. Cell Biol. 120:1993;359-369
    • (1993) J. Cell Biol. , vol.120 , pp. 359-369
    • Zhang, R.1    Skach, W.2    Hasegawa, H.3    Van Hoek, A.N.4    Verkman, A.S.5
  • 330
    • 0036016542 scopus 로고    scopus 로고
    • Aquaporin deletion in mice reduces intraocular pressure and aqueous fluid production
    • Zhang D., Vetrivel L., Verkman A.S. Aquaporin deletion in mice reduces intraocular pressure and aqueous fluid production. J. Gen. Physiol. 119:2002;561-569
    • (2002) J. Gen. Physiol. , vol.119 , pp. 561-569
    • Zhang, D.1    Vetrivel, L.2    Verkman, A.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.