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Volumn 65, Issue , 2003, Pages 531-542

Regulation of Na/Pi Transporter in the Proximal Tubule

Author keywords

Inorganic phosphate; Kidney; Na Pi cotransport; PDZ proteins; Protein interactions; Reabsorption

Indexed keywords

CARRIER PROTEIN; EPITOPE; PDZ PROTEIN; PHOSPHATE; PROTEIN DERIVATIVE; PROTEIN KINASE; SODIUM; SODIUM PROTON EXCHANGE PROTEIN 1; SODIUM PROTON EXCHANGE PROTEIN 3; COTRANSPORTER; SLC34A1 PROTEIN, HUMAN; SODIUM PHOSPHATE COTRANSPORTER; SODIUM PHOSPHATE COTRANSPORTER 2A;

EID: 0038311933     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.physiol.65.042902.092424     Document Type: Review
Times cited : (138)

References (72)
  • 1
    • 0022460725 scopus 로고
    • Cellular mechanisms of inorganic phosphate transport in kidney
    • Gmaj P, Murer H. 1986. Cellular mechanisms of inorganic phosphate transport in kidney. Physiol. Rev. 66:36-70
    • (1986) Physiol. Rev. , vol.66 , pp. 36-70
    • Gmaj, P.1    Murer, H.2
  • 2
    • 0033775213 scopus 로고    scopus 로고
    • Proximal tubular phosphate reabsorption: Molecular mechanisms
    • Murer H, Hernando N, Forster I, Biber J. 2000. Proximal tubular phosphate reabsorption: molecular mechanisms. Physiol. Rev. 80:1373-409
    • (2000) Physiol. Rev. , vol.80 , pp. 1373-1409
    • Murer, H.1    Hernando, N.2    Forster, I.3    Biber, J.4
  • 3
    • 0032446940 scopus 로고    scopus 로고
    • Na-dependent phosphate cotransporters: The NaPi protein families
    • Werner A, Dehmet L, Nalbant P. 1998. Na-dependent phosphate cotransporters: the NaPi protein families. J. Exp. Biol. 201:3135-42
    • (1998) J. Exp. Biol. , vol.201 , pp. 3135-3142
    • Werner, A.1    Dehmet, L.2    Nalbant, P.3
  • 5
    • 0002518901 scopus 로고    scopus 로고
    • Cellular mechanisms in proximal tubular handling of phosphate
    • ed. DW Seldin, G Giebisch, New York: Lippincott Williams & Wilkins
    • Murer H, Kaissling B, Forster I, Biber J. 2000. Cellular mechanisms in proximal tubular handling of phosphate. In The Kidney: Physiology and Pathophysiology, ed. DW Seldin, G Giebisch, pp. 1869-84. New York: Lippincott Williams & Wilkins
    • (2000) The Kidney: Physiology and Pathophysiology , pp. 1869-1884
    • Murer, H.1    Kaissling, B.2    Forster, I.3    Biber, J.4
  • 6
    • 1342334909 scopus 로고    scopus 로고
    • Renal handling of phosphate
    • ed. SG Massry, RJ Glassocks, London: Lippincott Williams & Wilkins
    • Murer H, Silve C, Friedlander G, Biber J. 2001. Renal handling of phosphate. In Textbook of Nephrology, ed. SG Massry, RJ Glassocks, pp. 362-67. London: Lippincott Williams & Wilkins
    • (2001) Textbook of Nephrology , pp. 362-367
    • Murer, H.1    Silve, C.2    Friedlander, G.3    Biber, J.4
  • 7
    • 0036448310 scopus 로고    scopus 로고
    • Novel Pi regulating genes in the pathogenesis of renal Pi wasting disorders
    • Tenenhouse HS, Sabbagh Y. 2002. Novel Pi regulating genes in the pathogenesis of renal Pi wasting disorders. Eur. J. Physiol. 444:317-36
    • (2002) Eur. J. Physiol. , vol.444 , pp. 317-336
    • Tenenhouse, H.S.1    Sabbagh, Y.2
  • 8
    • 0031755898 scopus 로고    scopus 로고
    • Differential expression, abundance, and regulation of Na-phosphate cotransporter genes in murine kidneys
    • Tenenhouse HS, Roy S, Martel J, Gauthier C. 1998. Differential expression, abundance, and regulation of Na-phosphate cotransporter genes in murine kidneys. Am. J. Physiol. Renal Physiol. 275:F527-F34
    • (1998) Am. J. Physiol. Renal Physiol. , vol.275
    • Tenenhouse, H.S.1    Roy, S.2    Martel, J.3    Gauthier, C.4
  • 9
    • 0027213541 scopus 로고
    • Localization of NaPi-1, a Na/Pi cotransporter, in rabbit kidney proximal tubules. II. Localization by immunohistochemistry
    • Biber J, Custer M, Werner A, Kaissling B, Murer H. 1993. Localization of NaPi-1, a Na/Pi cotransporter, in rabbit kidney proximal tubules. II. Localization by immunohistochemistry. Pflügers Arch. 424:210-15
    • (1993) Pflügers Arch. , vol.424 , pp. 210-215
    • Biber, J.1    Custer, M.2    Werner, A.3    Kaissling, B.4    Murer, H.5
  • 10
    • 0028814091 scopus 로고
    • Cloning, genetic mapping and expression analysis of a mouse renal sodium-dependent phosphate cotranpsorter
    • Chong SS, Kozak CA, Liu L, Kristjansson K, Dunn ST, et al. 1995. Cloning, genetic mapping and expression analysis of a mouse renal sodium-dependent phosphate cotranpsorter. Am. J. Physiol. Renal Physiol. 268:F1038-F45
    • (1995) Am. J. Physiol. Renal Physiol. , vol.268
    • Chong, S.S.1    Kozak, C.A.2    Liu, L.3    Kristjansson, K.4    Dunn, S.T.5
  • 11
  • 12
    • 0028874157 scopus 로고
    • Cloning and functional expression of a Na-dependent phosphate cotransporter from human kidney: cDNA cloning and functional expression
    • Miyamoto K, Tatsumi S, Sonoda T, Yamamoto H, Minami H, et al. 1995. Cloning and functional expression of a Na-dependent phosphate cotransporter from human kidney: cDNA cloning and functional expression. Biochem. J. 305:81-85
    • (1995) Biochem. J. , vol.305 , pp. 81-85
    • Miyamoto, K.1    Tatsumi, S.2    Sonoda, T.3    Yamamoto, H.4    Minami, H.5
  • 13
    • 0029896232 scopus 로고    scopus 로고
    • Expression of a renal type sodium/phosphate transporter (NaPi-1) induces a conductance in Xenopus oocytes permeable for organic and inorganic anions
    • Busch AE, Schuster A, Waldegger S, Wagner CA, Zempel G, et al. 1996. Expression of a renal type sodium/phosphate transporter (NaPi-1) induces a conductance in Xenopus oocytes permeable for organic and inorganic anions. Proc. Natl. Acad. Sci. USA 93:5347-51
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5347-5351
    • Busch, A.E.1    Schuster, A.2    Waldegger, S.3    Wagner, C.A.4    Zempel, G.5
  • 14
    • 0032160713 scopus 로고    scopus 로고
    • Hepatic sinusoidal membrane transport of anionic drugs mediated by anion transporter Nptl
    • Yabuuchi H, Tamai I, Monta K, Kouda T, Miyamoto K, et al. 1998. Hepatic sinusoidal membrane transport of anionic drugs mediated by anion transporter Nptl. J. Pharmacol. Exp. Ther. 286:1391-96
    • (1998) J. Pharmacol. Exp. Ther. , vol.286 , pp. 1391-1396
    • Yabuuchi, H.1    Tamai, I.2    Monta, K.3    Kouda, T.4    Miyamoto, K.5
  • 16
    • 15644377400 scopus 로고    scopus 로고
    • Identification of three isoforms for the Na-dependent phosphate cotransporter (NaPi-2) in rat kidney
    • Tatsumi S, Miyamoto K, Kouda T, Motonaga K, Katai K, et al. 1998. Identification of three isoforms for the Na-dependent phosphate cotransporter (NaPi-2) in rat kidney. J. Biol. Chem. 273:28568-75
    • (1998) J. Biol. Chem. , vol.273 , pp. 28568-28575
    • Tatsumi, S.1    Miyamoto, K.2    Kouda, T.3    Motonaga, K.4    Katai, K.5
  • 17
    • 0032564338 scopus 로고    scopus 로고
    • Characterization of a new murine type II sodium-phosphate cotransporter expressed in mammalian small intestine
    • Hilfiker H, Hattenhauer O, Traebert M, Forster I, Murer H, et al. 1998. Characterization of a new murine type II sodium-phosphate cotransporter expressed in mammalian small intestine. Proc. Natl. Acad. Sci. USA 95:14564-69
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14564-14569
    • Hilfiker, H.1    Hattenhauer, O.2    Traebert, M.3    Forster, I.4    Murer, H.5
  • 20
    • 0032574725 scopus 로고    scopus 로고
    • Targeted inactivation of Npt2 in mice leads to severe renal phosphate wasting, hypercalciuria and skeletal abnormalities
    • Beck L, Karaplis AC, Amizuka N, Hewson AS, Ozawa H, et al. 1998. Targeted inactivation of Npt2 in mice leads to severe renal phosphate wasting, hypercalciuria and skeletal abnormalities. Proc. Natl. Acad. Sci. USA 95:5372-77
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5372-5377
    • Beck, L.1    Karaplis, A.C.2    Amizuka, N.3    Hewson, A.S.4    Ozawa, H.5
  • 21
    • 0034456670 scopus 로고    scopus 로고
    • Npt2 gene disruption confers resistance to the inhibitory action of PTH on renal Na-phosphate cotransport
    • Zhao N, Tenenhouse HS. 2000. Npt2 gene disruption confers resistance to the inhibitory action of PTH on renal Na-phosphate cotransport. Endocrinology 141:2159-65
    • (2000) Endocrinology , vol.141 , pp. 2159-2165
    • Zhao, N.1    Tenenhouse, H.S.2
  • 22
    • 0032743354 scopus 로고    scopus 로고
    • Effects of Npt2 gene ablation and low-phosphate diet on renal Na/phosphate cotransport and cotransporter expression
    • Hoag HM, Martel J, Gauthier C, Tenenhouse HS. 1999. Effects of Npt2 gene ablation and low-phosphate diet on renal Na/phosphate cotransport and cotransporter expression. J. Clin. Invest. 104:679-86
    • (1999) J. Clin. Invest. , vol.104 , pp. 679-686
    • Hoag, H.M.1    Martel, J.2    Gauthier, C.3    Tenenhouse, H.S.4
  • 23
    • 0344416980 scopus 로고    scopus 로고
    • Distribution of the sodium/phosphate transporter during postnatal ontogeny of the rat kidney
    • Traebert M, Lötscher M, Aschwanden R, Ritthaler T, Biber J, et al. 1999. Distribution of the sodium/phosphate transporter during postnatal ontogeny of the rat kidney. J. Am. Soc. Nephrol. 10:1407-15
    • (1999) J. Am. Soc. Nephrol. , vol.10 , pp. 1407-1415
    • Traebert, M.1    Lötscher, M.2    Aschwanden, R.3    Ritthaler, T.4    Biber, J.5
  • 24
    • 0031014557 scopus 로고    scopus 로고
    • Posttranscriptional mechanisms regulate ontogenic changes in rat renal sodium-phosphate transporter
    • Taufiq S, Collins JF, Ghishan FK. 1997. Posttranscriptional mechanisms regulate ontogenic changes in rat renal sodium-phosphate transporter. Am. J. Physiol. Renal Physiol. 272:F134-F41
    • (1997) Am. J. Physiol. Renal Physiol. , vol.272
    • Taufiq, S.1    Collins, J.F.2    Ghishan, F.K.3
  • 26
    • 0028341123 scopus 로고
    • Cell-surface receptors for gibbon ape leukaemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters
    • Kavanaugh MP, Miller DG, Zhang W, Law W, Kozak SL, et al. 1994. Cell-surface receptors for gibbon ape leukaemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters. Proc. Natl. Acad. Sci. USA 91: 7071-75
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7071-7075
    • Kavanaugh, M.P.1    Miller, D.G.2    Zhang, W.3    Law, W.4    Kozak, S.L.5
  • 27
    • 0032724829 scopus 로고    scopus 로고
    • Na/Pi cotransport type III (PiT1) expression in human embryonic kidney cells and regulation by PTH
    • Fernandes I, Beliveau R, Friedlander G, Silve C. 1999. Na/Pi cotransport type III (PiT1) expression in human embryonic kidney cells and regulation by PTH. Am. J. Physiol. Renal Physiol. 277:F543-F51
    • (1999) Am. J. Physiol. Renal Physiol. , vol.277
    • Fernandes, I.1    Beliveau, R.2    Friedlander, G.3    Silve, C.4
  • 29
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: A novel approach to structure-function relationships in polytopic membrane proteins
    • Frillingos S, Sahin-Toth M, Wu J, Kaback HR. 1998. Cys-scanning mutagenesis: a novel approach to structure-function relationships in polytopic membrane proteins. FASEB J. 12:1281-99
    • (1998) FASEB J. , vol.12 , pp. 1281-1299
    • Frillingos, S.1    Sahin-Toth, M.2    Wu, J.3    Kaback, H.R.4
  • 32
    • 0036080731 scopus 로고    scopus 로고
    • Identification of functionally important sites in the first intracellular loop of the Na/Pi-IIa cotransporter
    • Köhler K, Forster IC, Stange G, Biber J, Murer H. 2002. Identification of functionally important sites in the first intracellular loop of the Na/Pi-IIa cotransporter. Am. J. Physiol. Renal Physiol. 282:F687-F96
    • (2002) Am. J. Physiol. Renal Physiol. , vol.282
    • Köhler, K.1    Forster, I.C.2    Stange, G.3    Biber, J.4    Murer, H.5
  • 34
    • 0032522430 scopus 로고    scopus 로고
    • The Na-phosphate cotransport system (NaPi-II) with a cleaved protein backbone: Implications on function and membrane insertion
    • Kohl B, Wagner CA, Huelseweh B, Busch A, Werner A. 1998. The Na-phosphate cotransport system (NaPi-II) with a cleaved protein backbone: implications on function and membrane insertion. J. Physiol. 508:341-50
    • (1998) J. Physiol. , vol.508 , pp. 341-350
    • Kohl, B.1    Wagner, C.A.2    Huelseweh, B.3    Busch, A.4    Werner, A.5
  • 37
    • 0031849866 scopus 로고    scopus 로고
    • Regulation of renal phosphate transport by acute and chronic metabolic acidosis in the rat
    • Ambuhl PM, Zajicek HK, Wang H, Puttaparthi K, Levi M. 1998. Regulation of renal phosphate transport by acute and chronic metabolic acidosis in the rat. Kidney Int. 53:1288-98
    • (1998) Kidney Int. , vol.53 , pp. 1288-1298
    • Ambuhl, P.M.1    Zajicek, H.K.2    Wang, H.3    Puttaparthi, K.4    Levi, M.5
  • 38
    • 0034050537 scopus 로고    scopus 로고
    • Molecular determinants of pH sensitivity of the type IIa Na/Pi-cotransporter
    • De La Horra C, Hernando N, Lambert G, Forster I, Biber J, et al. 2000. Molecular determinants of pH sensitivity of the type IIa Na/Pi-cotransporter. J. Biol. Chem. 275:6284-87
    • (2000) J. Biol. Chem. , vol.275 , pp. 6284-6287
    • De La Horra, C.1    Hernando, N.2    Lambert, G.3    Forster, I.4    Biber, J.5
  • 39
    • 0033969677 scopus 로고    scopus 로고
    • Internalization of proximal tubular type II Na/Pi-cotransporter by parathyroid hormone: An immunogold electron-microscopy study
    • Traebert M, Roth J, Biber J, Murer H, Kaissling B. 2000. Internalization of proximal tubular type II Na/Pi-cotransporter by parathyroid hormone: an immunogold electron-microscopy study. Am. J. Physiol. Renal Physiol. 278:F148-F54
    • (2000) Am. J. Physiol. Renal Physiol. , vol.278
    • Traebert, M.1    Roth, J.2    Biber, J.3    Murer, H.4    Kaissling, B.5
  • 40
    • 0031660004 scopus 로고    scopus 로고
    • Parathyroid hormone and dietary phosphate provoke lysosomal routing of the proximal tubular Na/Pi-cotransporter type II
    • Keusch I, Traebert M, Lötscher M, Kaissling B, Murer H, et al. 1998. Parathyroid hormone and dietary phosphate provoke lysosomal routing of the proximal tubular Na/Pi-cotransporter type II. Kidney Int. 54:1224-32
    • (1998) Kidney Int. , vol.54 , pp. 1224-1232
    • Keusch, I.1    Traebert, M.2    Lötscher, M.3    Kaissling, B.4    Murer, H.5
  • 43
    • 0034076355 scopus 로고    scopus 로고
    • Luminal and contraluminal action of 1-34 and 3-34 PTH peptides on renal type IIa Na/Pi-cotransporter
    • Traebert M, Völkl H, Biber J, Murer H, Kaissling B. 2000. Luminal and contraluminal action of 1-34 and 3-34 PTH peptides on renal type IIa Na/Pi-cotransporter. Am. J. Physiol. Renal Physiol. 278:F792-F98
    • (2000) Am. J. Physiol. Renal Physiol. , vol.278
    • Traebert, M.1    Völkl, H.2    Biber, J.3    Murer, H.4    Kaissling, B.5
  • 45
    • 0033983568 scopus 로고    scopus 로고
    • Parathyroid hormone stimulates extracellular signal-regulated kinase (ERK) activity through two independent signal transduction pathways: Role of ERK in sodium-phosphate cotransport
    • Lederer ED, Sohl SS, McLeish KR. 2000. Parathyroid hormone stimulates extracellular signal-regulated kinase (ERK) activity through two independent signal transduction pathways: role of ERK in sodium-phosphate cotransport. J. Am. Soc. Nephrol. 11:222-31
    • (2000) J. Am. Soc. Nephrol. , vol.11 , pp. 222-231
    • Lederer, E.D.1    Sohl, S.S.2    McLeish, K.R.3
  • 48
    • 0033761067 scopus 로고    scopus 로고
    • PTH-induced downregulation of the type IIa Na/Pi-cotransporter is independent of known endocytic motifs
    • Hernando N, Forgo J, Biber J, Murer H. 2000. PTH-induced downregulation of the type IIa Na/Pi-cotransporter is independent of known endocytic motifs. J. Am. Soc. Nephrol. 11:1961-68
    • (2000) J. Am. Soc. Nephrol. , vol.11 , pp. 1961-1968
    • Hernando, N.1    Forgo, J.2    Biber, J.3    Murer, H.4
  • 49
    • 0034859579 scopus 로고    scopus 로고
    • Molecular determinants for apical expression of the renal type IIa NaPi-cotransporter
    • Karim-Jimenez Z, Hernando N, Biber J, Murer H. 2001. Molecular determinants for apical expression of the renal type IIa NaPi-cotransporter. Pflügers Arch. 442:782-90
    • (2001) Pflügers Arch. , vol.442 , pp. 782-790
    • Karim-Jimenez, Z.1    Hernando, N.2    Biber, J.3    Murer, H.4
  • 50
    • 0026766162 scopus 로고
    • Molecular genetics of mineral metabolic disorders
    • Thakker RV. 1992. Molecular genetics of mineral metabolic disorders. J. Inherit. Metab. Dis. 15:592-609
    • (1992) J. Inherit. Metab. Dis. , vol.15 , pp. 592-609
    • Thakker, R.V.1
  • 51
    • 0032893855 scopus 로고    scopus 로고
    • X-linked hypophosphatemia - A homologous disorder in humans and mice
    • Tenenhouse HS. 1999. X-linked hypophosphatemia - a homologous disorder in humans and mice. Nephrol. Dialysis Transplant. 14:333-41
    • (1999) Nephrol. Dialysis Transplant. , vol.14 , pp. 333-341
    • Tenenhouse, H.S.1
  • 52
    • 0031452349 scopus 로고    scopus 로고
    • Autosomal dominant hypophosphatemic rickets is linked to chromosome 12p13
    • Econs MJ, McEnery PT, Lennon F, Speer MC. 1997. Autosomal dominant hypophosphatemic rickets is linked to chromosome 12p13. J. Clin. Invest. 100:2653-57
    • (1997) J. Clin. Invest. , vol.100 , pp. 2653-2657
    • Econs, M.J.1    McEnery, P.T.2    Lennon, F.3    Speer, M.C.4
  • 53
    • 0033763097 scopus 로고    scopus 로고
    • Autosomal dominant hypophosphatemic rickets is associated with mutations in FGF-23
    • ADHR consortium.2000.Autosomal dominant hypophosphatemic rickets is associated with mutations in FGF-23. Nat. Genet. 26:345-48
    • (2000) Nat. Genet. , vol.26 , pp. 345-348
  • 54
    • 14344279878 scopus 로고    scopus 로고
    • Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia
    • Shimada T, Mizutani S, Muto T, Yoneya T, Hino R, et al. 2001. Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia. Proc. Natl. Acad. Sci. USA 98:6500-5
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6500-6505
    • Shimada, T.1    Mizutani, S.2    Muto, T.3    Yoneya, T.4    Hino, R.5
  • 55
    • 0037008747 scopus 로고    scopus 로고
    • Fibroblast growth factor (FGF)-23 inhibits renal phosphate reabsorption by activation of the mitogen-activated kinase pathway
    • Yamashita T, Konishi M, Miyake A, Inui K, Itoh N. 2002. Fibroblast growth factor (FGF)-23 inhibits renal phosphate reabsorption by activation of the mitogen-activated kinase pathway. J. Biol. Chem. 277:28265-70
    • (2002) J. Biol. Chem. , vol.277 , pp. 28265-28270
    • Yamashita, T.1    Konishi, M.2    Miyake, A.3    Inui, K.4    Itoh, N.5
  • 56
    • 0035723074 scopus 로고    scopus 로고
    • Evidence for a PTH-independent humoral mechanism in post-transplant hypophosphatemia and phosphaturia
    • Green J, Debby H, Lederer E, Levi M, Zajicek HK, et al. 2001. Evidence for a PTH-independent humoral mechanism in post-transplant hypophosphatemia and phosphaturia. Kidney Int. 60:1182-96
    • (2001) Kidney Int. , vol.60 , pp. 1182-1196
    • Green, J.1    Debby, H.2    Lederer, E.3    Levi, M.4    Zajicek, H.K.5
  • 57
    • 0032408559 scopus 로고    scopus 로고
    • A PDZ domain containing protein with homology to Diphor-1 maps to human chromosome Iq21
    • White KE, Biber J, Murer H, Econms MJ. 1998. A PDZ domain containing protein with homology to Diphor-1 maps to human chromosome Iq21. Ann. Hum. Genet. 62:287-90
    • (1998) Ann. Hum. Genet. , vol.62 , pp. 287-290
    • White, K.E.1    Biber, J.2    Murer, H.3    Econms, M.J.4
  • 58
    • 0031883886 scopus 로고    scopus 로고
    • Identification and partial characterization of PDZK1: A novel protein containing PDZ interaction domains
    • Kocher O, Comella N, Tognazzi K, Brown LF. 1998. Identification and partial characterization of PDZK1: a novel protein containing PDZ interaction domains. Lab Invest. 78:117-25
    • (1998) Lab. Invest. , vol.78 , pp. 117-125
    • Kocher, O.1    Comella, N.2    Tognazzi, K.3    Brown, L.F.4
  • 59
    • 0035937814 scopus 로고    scopus 로고
    • Interaction of the type IIa Na/Pi-cotransporter with PDZ proteins
    • Gisler SM, Stagljar I, Traebert M, Bacic D, Biber J, et al. 2001. Interaction of the type IIa Na/Pi-cotransporter with PDZ proteins. J. Biol. Chem. 276:9206-13
    • (2001) J. Biol. Chem. , vol.276 , pp. 9206-9213
    • Gisler, S.M.1    Stagljar, I.2    Traebert, M.3    Bacic, D.4    Biber, J.5
  • 61
    • 0030017442 scopus 로고    scopus 로고
    • Identification and partial characterization of a novel membrane associated protein (MAP17) up-regulated in human carcinomas and modulating cell replication and tumor growth
    • Kocher O, Cheresh P, Lee SW 1996. Identification and partial characterization of a novel membrane associated protein (MAP17) up-regulated in human carcinomas and modulating cell replication and tumor growth. Am. J. Pathol. 149:493-400
    • (1996) Am. J. Pathol. , vol.149 , pp. 493-1400
    • Kocher, O.1    Cheresh, P.2    Lee, S.W.3
  • 63
    • 0030938112 scopus 로고    scopus 로고
    • The neuronal calcium-sensor protein VILIP modulates cyclic AMP accumulation in stably transfected C6 glioma cells: Amino-terminal myristoylation determines functional activity
    • Braunewell KH, Spilker C, Behnisch T, Grundelfinger ED. 1997. The neuronal calcium-sensor protein VILIP modulates cyclic AMP accumulation in stably transfected C6 glioma cells: amino-terminal myristoylation determines functional activity. J. Neurochem. 68:2129-39
    • (1997) J. Neurochem. , vol.68 , pp. 2129-2139
    • Braunewell, K.H.1    Spilker, C.2    Behnisch, T.3    Grundelfinger, E.D.4
  • 64
    • 0034806716 scopus 로고    scopus 로고
    • Intracellular neuronal calcium sensor (NCS) protein VILIP-1 modulates cGMP signalling pathways in transfected neural cells and cerebellar granule neurones
    • Braunewell KH, Brackmann M, Schaupp M, Spilker C, Anand R, et al. 2001. Intracellular neuronal calcium sensor (NCS) protein VILIP-1 modulates cGMP signalling pathways in transfected neural cells and cerebellar granule neurones. J. Neurochem. 78:1277-86
    • (2001) J. Neurochem. , vol.78 , pp. 1277-1286
    • Braunewell, K.H.1    Brackmann, M.2    Schaupp, M.3    Spilker, C.4    Anand, R.5
  • 66
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M, Sala C. 2001. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24:1-29
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 67
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: Structural modules for protein complex assembly
    • Hung AY, Sheng M. 2002. PDZ domains: structural modules for protein complex assembly. J. Biol. Chem. 277:5699-702
    • (2002) J. Biol. Chem. , vol.277 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 68
    • 0034859579 scopus 로고    scopus 로고
    • Molecular determinants for apical expression of the renal type IIa Na/Pi-cotransporter
    • Karim-Jimenez Z, Hernando N, Biber J, Murer H. 2001. Molecular determinants for apical expression of the renal type IIa Na/Pi-cotransporter. Plügers Arch. 442:782-90
    • (2001) Plügers Arch. , vol.442 , pp. 782-790
    • Karim-Jimenez, Z.1    Hernando, N.2    Biber, J.3    Murer, H.4
  • 69
    • 0035853041 scopus 로고    scopus 로고
    • Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein
    • Wang L, Sunahara RK, Krumins A, Perkins G, Crochiere ML, et al. 2000. Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein. Proc. Natl. Acad. Sci. USA 98: 3220-25
    • (2000) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3220-3225
    • Wang, L.1    Sunahara, R.K.2    Krumins, A.3    Perkins, G.4    Crochiere, M.L.5
  • 70
    • 0028946268 scopus 로고
    • Characterization of a protein cofactor that mediates protein kinase A regulation of the renal brush border membrane Na-H exchanger
    • Weinman EJ, Steplock D, Wang Y, Shenolikar S. 1995. Characterization of a protein cofactor that mediates protein kinase A regulation of the renal brush border membrane Na-H exchanger. J. Clin. Invest. 95:2143-49
    • (1995) J. Clin. Invest. , vol.95 , pp. 2143-2149
    • Weinman, E.J.1    Steplock, D.2    Wang, Y.3    Shenolikar, S.4
  • 72
    • 0033834085 scopus 로고    scopus 로고
    • Signal complex regulation of renal transport: NHERF and regulation of NHE3 by PKA
    • Weinman E, Minkoff C, Shenolikar S. 2000. Signal complex regulation of renal transport: NHERF and regulation of NHE3 by PKA. Am. J. Physiol. Renal Physiol. 279:F393-F99
    • (2000) Am. J. Physiol. Renal Physiol. , vol.279
    • Weinman, E.1    Minkoff, C.2    Shenolikar, S.3


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