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Volumn 287, Issue 5 56-5, 2004, Pages

Evidence for stabilization of aquaporin-2 folding mutants by N-linked glycosylation in endoplasmic reticulum

Author keywords

Endoplasmic reticulum associated degradation; Nephrogenic diabetes insipidus; Oocytes

Indexed keywords

AQUAPORIN; AQUAPORIN 2; VASOPRESSIN;

EID: 6044252407     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.00561.2003     Document Type: Article
Times cited : (45)

References (57)
  • 1
    • 0031780486 scopus 로고    scopus 로고
    • The perinatal expression of aquaporin-2 and aquaporin-3 in developing kidney
    • Baum MA, Ruddy MK, Hosselet CA, and Harris HW. The perinatal expression of aquaporin-2 and aquaporin-3 in developing kidney. Pediatr Res 43: 783-790, 1998.
    • (1998) Pediatr Res , vol.43 , pp. 783-790
    • Baum, M.A.1    Ruddy, M.K.2    Hosselet, C.A.3    Harris, H.W.4
  • 2
    • 0031722224 scopus 로고    scopus 로고
    • Glycosylation is not essential for vasopressin-dependent routing of aquaporin-2 in transfected Madin-Darby canine kidney cells
    • Baumgarten R, Van De Pol MH, Wetzels JF, van Os CH, and Been PM. Glycosylation is not essential for vasopressin-dependent routing of aquaporin-2 in transfected Madin-Darby canine kidney cells. J Am Soc Nephrol 9: 1553-1559, 1998.
    • (1998) J Am Soc Nephrol , vol.9 , pp. 1553-1559
    • Baumgarten, R.1    Van De Pol, M.H.2    Wetzels, J.F.3    Van Os, C.H.4    Been, P.M.5
  • 3
    • 0021715322 scopus 로고
    • Evidence for post-translational glycosylation of a nonglycosylated precursor protein of herpes simplex virus type 1
    • Compton T and Courtney RJ. Evidence for post-translational glycosylation of a nonglycosylated precursor protein of herpes simplex virus type 1. J Virol 52: 630-637, 1984.
    • (1984) J Virol , vol.52 , pp. 630-637
    • Compton, T.1    Courtney, R.J.2
  • 4
    • 0028968593 scopus 로고
    • Water channels encoded by mutant aquaporin-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing
    • Been PM, Croes H, van Aubel RA, Ginsel LA, and van Os CH. Water channels encoded by mutant aquaporin-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing. J Clin Invest 95: 2291-2296, 1995.
    • (1995) J Clin Invest , vol.95 , pp. 2291-2296
    • Been, P.M.1    Croes, H.2    Van Aubel, R.A.3    Ginsel, L.A.4    Van Os, C.H.5
  • 6
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and G1pF
    • De Groot BL and Grubmuller H. Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and G1pF. Science 294: 2353-2357, 2001.
    • (2001) Science , vol.294 , pp. 2353-2357
    • De Groot, B.L.1    Grubmuller, H.2
  • 7
    • 0345253853 scopus 로고    scopus 로고
    • Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: The role of N-Linked glycans and the unfolded protein response
    • De Virgilio M, Kitzmuller C, Schwaiger E, Klein M, Kreibich G, and Ivessa NE. Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-Linked glycans and the unfolded protein response. Mol Biol Cell 10: 4059-4073, 1999.
    • (1999) Mol Biol Cell , vol.10 , pp. 4059-4073
    • De Virgilio, M.1    Kitzmuller, C.2    Schwaiger, E.3    Klein, M.4    Kreibich, G.5    Ivessa, N.E.6
  • 8
    • 0037177864 scopus 로고    scopus 로고
    • Evidence that the transmembrane biogenesis of aquaporin 1 is cotranslational in intact mammalian cells
    • Dohke Y and Turner RJ. Evidence that the transmembrane biogenesis of aquaporin 1 is cotranslational in intact mammalian cells. J Biol Chem 277: 15215-15219, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 15215-15219
    • Dohke, Y.1    Turner, R.J.2
  • 9
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L and Helenius A. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4: 181-191, 2003.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 10
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan GI, Lewis GK, Ramsay G, and Bishop JM. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol Cell Biol 5: 3610-3616, 1985.
    • (1985) Mol Cell Biol , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 11
    • 0034602391 scopus 로고    scopus 로고
    • Identification of sequence determinants that direct different intracellular folding pathways for aquaporin-1 and aquaporin-4
    • Foster W, Helm A, Turnbull I, Gulati H, Yang B, Verkman AS, and Skach WR. Identification of sequence determinants that direct different intracellular folding pathways for aquaporin-1 and aquaporin-4. J Biol Chem 275: 34157-34165, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 34157-34165
    • Foster, W.1    Helm, A.2    Turnbull, I.3    Gulati, H.4    Yang, B.5    Verkman, A.S.6    Skach, W.R.7
  • 14
    • 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, and 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: 3205-3209, 1998.
    • (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
  • 15
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond C, Braakman I, and Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci USA 91: 913-917, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 16
    • 0034709549 scopus 로고    scopus 로고
    • Protein kinase A-dependent phosphorylation of aquaporin-1
    • Han Z and Patil RV. Protein kinase A-dependent phosphorylation of aquaporin-1. Biochem Biophys Res Commun 273: 328-332, 2000.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 328-332
    • Han, Z.1    Patil, R.V.2
  • 17
    • 0034075306 scopus 로고    scopus 로고
    • Molecular identification of functional water channel protein in cultured human nonpigmented ciliary epithelial cells
    • Han ZB, Yang JB, Wax MB, and Patil RV. Molecular identification of functional water channel protein in cultured human nonpigmented ciliary epithelial cells. Curr Eye Res 20: 242-247, 2000.
    • (2000) Curr Eye Res , vol.20 , pp. 242-247
    • Han, Z.B.1    Yang, J.B.2    Wax, M.B.3    Patil, R.V.4
  • 19
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-Linked glycans
    • Helenius A and Aebi M. Intracellular functions of N-Linked glycans. Science 291: 2364-2369, 2001.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 20
    • 1642494672 scopus 로고    scopus 로고
    • Glycosylation is important for cell surface expression of the water channel aquaporin-2 but is not essential for tetramerization in the endoplasmic reticulum
    • Hendriks G, Koudijs M, van Balkom BW, Oorschot V, Klumperman J, Deen PM, and van der Sluijs P. Glycosylation is important for cell surface expression of the water channel aquaporin-2 but is not essential for tetramerization in the endoplasmic reticulum. J Biol Chem 279: 2975-2983, 2003.
    • (2003) J Biol Chem , vol.279 , pp. 2975-2983
    • Hendriks, G.1    Koudijs, M.2    Van Balkom, B.W.3    Oorschot, V.4    Klumperman, J.5    Deen, P.M.6    Van Der Sluijs, P.7
  • 21
    • 0038307139 scopus 로고    scopus 로고
    • The proteasome is involved in the degradation of different aquaporin-2 mutants causing nephrogenic diabetes insipidus
    • Hirano K, Zuber C, Roth J, and Ziak M. The proteasome is involved in the degradation of different aquaporin-2 mutants causing nephrogenic diabetes insipidus. Am J Pathol 163: 111-120, 2003.
    • (2003) Am J Pathol , vol.163 , pp. 111-120
    • Hirano, K.1    Zuber, C.2    Roth, J.3    Ziak, M.4
  • 22
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, and Pease LR. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77: 51-59, 1989.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 23
    • 0032494135 scopus 로고    scopus 로고
    • Degradation of misfolded endoplasmic retsculum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
    • Jakob CA, Burda P, Roth J, and Aebi M. Degradation of misfolded endoplasmic retsculum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 142: 1223-1233, 1998.
    • (1998) J Cell Biol , vol.142 , pp. 1223-1233
    • Jakob, C.A.1    Burda, P.2    Roth, J.3    Aebi, M.4
  • 25
    • 0023919087 scopus 로고
    • Glycosylation of CD4. Tunicamycin inhibits surface expression
    • Keonig R, Ashwell G, and Hanover JA. Glycosylation of CD4. Tunicamycin inhibits surface expression. J Biol Chem 263: 9502-9507, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 9502-9507
    • Keonig, R.1    Ashwell, G.2    Hanover, J.A.3
  • 26
    • 0034235737 scopus 로고    scopus 로고
    • Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein
    • Li J, Quilty J, Popov M, and Reithmeier RA. Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein. Biochem J 349: 51-57, 2000.
    • (2000) Biochem J , vol.349 , pp. 51-57
    • Li, J.1    Quilty, J.2    Popov, M.3    Reithmeier, R.A.4
  • 27
    • 0034492193 scopus 로고    scopus 로고
    • Reorientation of aquaporin-1 topology during maturation in the endoplasmic reticulum
    • Lu Y, Turnbull IR, Bragin A, Carveth K, Verkman AS, and Skach WR. Reorientation of aquaporin-1 topology during maturation in the endoplasmic reticulum. Mol Biol Cell 11: 2973-2985, 2000.
    • (2000) Mol Biol Cell , vol.11 , pp. 2973-2985
    • Lu, Y.1    Turnbull, I.R.2    Bragin, A.3    Carveth, K.4    Verkman, A.S.5    Skach, W.R.6
  • 28
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • Marquardt T and Helenius A. Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. J Cell Biol 117: 505-513, 1992.
    • (1992) J Cell Biol , vol.117 , pp. 505-513
    • Marquardt, T.1    Helenius, A.2
  • 29
    • 0035046505 scopus 로고    scopus 로고
    • Functionality of aquaporin-2 missense mutants in recessive nephrogenic diabetes insipidus
    • Marr N, Kamsteeg EJ, van Raak M, van Os CH, and Deen PM. Functionality of aquaporin-2 missense mutants in recessive nephrogenic diabetes insipidus. Pflügers Arch 442: 73-77, 2001.
    • (2001) Pflügers Arch , vol.442 , pp. 73-77
    • Marr, N.1    Kamsteeg, E.J.2    Van Raak, M.3    Van Os, C.H.4    Deen, P.M.5
  • 30
    • 0042318739 scopus 로고    scopus 로고
    • Evolving questions and paradigm shifts in endoplasmic-reticulum- associated degradation (ERAD)
    • McCracken AA and Brodsky JL. Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). Bioessays 25: 868-877, 2003.
    • (2003) Bioessays , vol.25 , pp. 868-877
    • McCracken, A.A.1    Brodsky, J.L.2
  • 31
  • 35
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson IM and von Heijne G. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J Biol Chem 268: 5798-5801, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 5798-5801
    • Nilsson, I.M.1    Von Heijne, G.2
  • 36
    • 0034657712 scopus 로고    scopus 로고
    • Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation
    • Parodi AJ. Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation. Biochem J 348: 1-13, 2000.
    • (2000) Biochem J , vol.348 , pp. 1-13
    • Parodi, A.J.1
  • 37
    • 0032478644 scopus 로고    scopus 로고
    • Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin
    • Pipe SW, Morris JA, Shah J, and Kaufman RJ. Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J Biol Chem 273: 8537-8544, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 8537-8544
    • Pipe, S.W.1    Morris, J.A.2    Shah, J.3    Kaufman, R.J.4
  • 38
    • 0021241353 scopus 로고
    • Role of glycosylation in the processing of newly translated insulin proreceptor in 3T3-L1 adipocytes
    • Ronnett GV, Knutson VP, Kohanski RA, Simpson TL, and Lane MD. Role of glycosylation in the processing of newly translated insulin proreceptor in 3T3-L1 adipocytes. J Biol Chem 259: 4566-4575, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 4566-4575
    • Ronnett, G.V.1    Knutson, V.P.2    Kohanski, R.A.3    Simpson, T.L.4    Lane, M.D.5
  • 39
    • 0023729159 scopus 로고
    • Construction of defined polytopic integral transmembrane proteins. The role of signal and stop transfer sequence permutations
    • Rothman RE, Andrews DW, Calayag MC, and Lingappa VR. Construction of defined polytopic integral transmembrane proteins. The role of signal and stop transfer sequence permutations. J Biol Chem 263: 10470-10480, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 10470-10480
    • Rothman, R.E.1    Andrews, D.W.2    Calayag, M.C.3    Lingappa, V.R.4
  • 41
    • 0029069427 scopus 로고
    • Distinct biogenesis mechanisms for the water channels MIWC and CHIP28 at the endoplasmic reticulum
    • Shi LB, Skach WR, Ma T, and Verkman AS. Distinct biogenesis mechanisms for the water channels MIWC and CHIP28 at the endoplasmic reticulum. Biochemistry 34: 8250-8256, 1995.
    • (1995) Biochemistry , vol.34 , pp. 8250-8256
    • Shi, L.B.1    Skach, W.R.2    Ma, T.3    Verkman, A.S.4
  • 42
    • 0032739403 scopus 로고    scopus 로고
    • Functional analysis of aquaporin-2 mutants associated with nephrogenic diabetes insipidus by yeast expression
    • Shinbo I, Fushimi K, Kasahara M, Yamauchi K, Sasaki S, and Marumo F. Functional analysis of aquaporin-2 mutants associated with nephrogenic diabetes insipidus by yeast expression. Am J Physiol Renal Physiol 277: F734-F741, 1999.
    • (1999) Am J Physiol Renal Physiol , vol.277
    • Shinbo, I.1    Fushimi, K.2    Kasahara, M.3    Yamauchi, K.4    Sasaki, S.5    Marumo, F.6
  • 43
    • 0027519416 scopus 로고
    • Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences
    • Skach WR and Lingappa VR, Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences. J Biol Chem 268: 23552-23561, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 23552-23561
    • Skach, W.R.1    Lingappa, V.R.2
  • 44
    • 0028318283 scopus 로고
    • Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum
    • Skach WR, Shi LB, Calayag MC, Frigeri A, Lingappa VR, and Verkman AS. Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum. J Cell Biol 125: 803-815, 1994.
    • (1994) J Cell Biol , vol.125 , pp. 803-815
    • Skach, W.R.1    Shi, L.B.2    Calayag, M.C.3    Frigeri, A.4    Lingappa, V.R.5    Verkman, A.S.6
  • 45
    • 0022979880 scopus 로고
    • Synthesis of epidermal growth factor receptor in human A431 cells. Glycosylation-dependent acquisition of ligand binding activity occurs post-translationally in the endoplasmic reticulum
    • Slieker LJ, Martensen TM, and Lane MD. Synthesis of epidermal growth factor receptor in human A431 cells. Glycosylation-dependent acquisition of ligand binding activity occurs post-translationally in the endoplasmic reticulum. J Biol Chem 261: 15233-15241, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 15233-15241
    • Slieker, L.J.1    Martensen, T.M.2    Lane, M.D.3
  • 46
    • 0027980902 scopus 로고
    • Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens
    • Smith BL, Preston GM, Spring FA, Anstee DJ, and Agre P. Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens. J Clin Invest 94: 1043-1049, 1994.
    • (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
  • 47
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui H, Han BG, Lee JK, Walian P, and Jap BK. Structural basis of water-specific transport through the AQP1 water channel. Nature 414: 872-878, 2001.
    • (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
  • 48
    • 0032524048 scopus 로고    scopus 로고
    • Defective aquaporin-2 trafficking in nephrogenic diabetes insipidus and correction by chemical chaperones
    • Tamarappoo BK and Verkman AS. Defective aquaporin-2 trafficking in nephrogenic diabetes insipidus and correction by chemical chaperones. J Clin Invest 101: 2257-2267, 1998.
    • (1998) J Clin Invest , vol.101 , pp. 2257-2267
    • Tamarappoo, B.K.1    Verkman, A.S.2
  • 49
    • 0033521139 scopus 로고    scopus 로고
    • Misfolding of mutant aquaporin-2 water channels in nephrogenic diabetes insipidus
    • Tamarappoo BK, Yang B, and Verkman AS. Misfolding of mutant aquaporin-2 water channels in nephrogenic diabetes insipidus. J Biol Chem 274: 34825-34831, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 34825-34831
    • Tamarappoo, B.K.1    Yang, B.2    Verkman, A.S.3
  • 50
    • 0028914847 scopus 로고
    • Purification and structure-function analysis of native, PNGase F-treated, and endo-beta-galactosidase-treated CHIP28 water channels
    • Van Hoek AN, Wiener MC, Verbavatz JM, Brown D, Lipniunas PH, Townsend RR, and Verkman AS. Purification and structure-function analysis of native, PNGase F-treated, and endo-beta-galactosidase-treated CHIP28 water channels. Biochemistry 34: 2212-2219, 1995.
    • (1995) Biochemistry , vol.34 , pp. 2212-2219
    • Van Hoek, A.N.1    Wiener, M.C.2    Verbavatz, J.M.3    Brown, D.4    Lipniunas, P.H.5    Townsend, R.R.6    Verkman, A.S.7
  • 52
    • 0030447659 scopus 로고    scopus 로고
    • Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
    • Werner ED, Brodsky JL, and McCracken AA. Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc Natl Acad Sci USA 93: 13797-13801, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13797-13801
    • Werner, E.D.1    Brodsky, J.L.2    McCracken, A.A.3
  • 53
    • 0026014164 scopus 로고
    • A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein
    • Williams AM and Enns CA. A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein. J Biol Chem 266: 17648-17654, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 17648-17654
    • Williams, A.M.1    Enns, C.A.2
  • 54
    • 0034647539 scopus 로고    scopus 로고
    • Pivotal role of calnexin and mannose trimming in regulating the endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain
    • Wilson CM, Farmery MR, and Bulleid NJ. Pivotal role of calnexin and mannose trimming in regulating the endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain. J Biol Chem 275: 21224-21232, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 21224-21232
    • Wilson, C.M.1    Farmery, M.R.2    Bulleid, N.J.3
  • 55
    • 0030931382 scopus 로고    scopus 로고
    • Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator
    • Xiong X, Bragin A, Widdicombe JH, Cohn J, and Skach WR. Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator. J Clin Invest 100: 1079-1088, 1997.
    • (1997) J Clin Invest , vol.100 , pp. 1079-1088
    • Xiong, X.1    Bragin, A.2    Widdicombe, J.H.3    Cohn, J.4    Skach, W.R.5
  • 56
    • 0033002039 scopus 로고    scopus 로고
    • Effects of missense mutations on rat aquaporin-2 in LLC-PK1 porcine kidney cells
    • Yamauchi K, Fushimi K, Yamashita Y, Shinbo I, Sasaki S, and Marumo F. Effects of missense mutations on rat aquaporin-2 in LLC-PK1 porcine kidney cells. Kidney Int 56: 164-171, 1999.
    • (1999) Kidney Int , vol.56 , pp. 164-171
    • Yamauchi, K.1    Fushimi, K.2    Yamashita, Y.3    Shinbo, I.4    Sasaki, S.5    Marumo, F.6
  • 57
    • 0035716877 scopus 로고    scopus 로고
    • The proteasome: A supramolecular assembly designed for controlled proteolysis
    • Zwickl P, Seemeuller E, Kapelari B, and Baumeister W. The proteasome: a supramolecular assembly designed for controlled proteolysis. Adv Protein Chem 59: 187-222, 2001.
    • (2001) Adv Protein Chem , vol.59 , pp. 187-222
    • Zwickl, P.1    Seemeuller, E.2    Kapelari, B.3    Baumeister, W.4


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