메뉴 건너뛰기




Volumn 212, Issue 11, 2009, Pages 1638-1646

NHE3 regulatory complexes

Author keywords

Na H exchange; Protein complexes; Signal transduction

Indexed keywords

SODIUM CHLORIDE; SODIUM PROTON EXCHANGE PROTEIN; SODIUM PROTON EXCHANGE PROTEIN 3; SODIUM-HYDROGEN EXCHANGER 3;

EID: 66449132859     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: 10.1242/jeb.028605     Document Type: Review
Times cited : (101)

References (80)
  • 2
    • 33745743608 scopus 로고    scopus 로고
    • Crystal structure of CHP2 complexed with NHE1-cytosolic region and an implication for pH regulation
    • Ammar, Y. B., Takeda, S., Hisamitsu, T., Mori, H. and Wakabayashi, S. (2006). Crystal structure of CHP2 complexed with NHE1-cytosolic region and an implication for pH regulation. EMBO J. 25, 2315-2325.
    • (2006) EMBO J , vol.25 , pp. 2315-2325
    • Ammar, Y.B.1    Takeda, S.2    Hisamitsu, T.3    Mori, H.4    Wakabayashi, S.5
  • 3
    • 21644467295 scopus 로고    scopus 로고
    • +- coupled amino acid transporter hPATI (SLC36A1)
    • +- coupled amino acid transporter hPATI (SLC36A1). J. Cell Physiol. 204, 604-613.
    • (2005) J. Cell Physiol , vol.204 , pp. 604-613
    • Anderson, C.M.1    Thwaites, D.T.2
  • 6
    • 33744489358 scopus 로고    scopus 로고
    • + exchanger NHE1. Acta Crystallogr. Sect F Struct Biol. Cryst. Commun. 61, 956-958.
    • + exchanger NHE1. Acta Crystallogr. Sect F Struct Biol. Cryst. Commun. 61, 956-958.
  • 8
    • 33750375599 scopus 로고    scopus 로고
    • Na+/H+ exchangers in renal regulation of acid-base balance
    • Bobulescu, I. A. and Moe, O. W. (2006). Na+/H+ exchangers in renal regulation of acid-base balance. Semin. Nephrol. 26, 334-344.
    • (2006) Semin. Nephrol , vol.26 , pp. 334-344
    • Bobulescu, I.A.1    Moe, O.W.2
  • 9
    • 0036083415 scopus 로고    scopus 로고
    • Human Na+/H+ exchanger isoform 6 is found in the recycling endosomes of cells, not mitochondria
    • Brett, C. L., Wei, Y., Donowitz, M. and Rao, R. (2002). Human Na+/H+ exchanger isoform 6 is found in the recycling endosomes of cells, not mitochondria. Am. J. Physiol. 282, 1031-1041.
    • (2002) Am. J. Physiol , vol.282 , pp. 1031-1041
    • Brett, C.L.1    Wei, Y.2    Donowitz, M.3    Rao, R.4
  • 10
    • 12144271044 scopus 로고    scopus 로고
    • The evolutionary origins of eukaryotic sodium/proton exchangers
    • Brett, C. L., Donowitz, M. and Rao, R. (2005a). The evolutionary origins of eukaryotic sodium/proton exchangers. Am. J. Physiol. Cell 288, C223-C229.
    • (2005) Am. J. Physiol. Cell , vol.288
    • Brett, C.L.1    Donowitz, M.2    Rao, R.3
  • 13
    • 4344578072 scopus 로고    scopus 로고
    • The lateral mobility of NHE3 on the apical membrane of renal epithelial OK cells is limited by the PDZ domain proteins NHERF1/2, but is dependent on an intact actin cytoskeleton as determined by FRAP
    • Cha, B., Kenworthy, A., Murtazina, R. and Donowitz, M. (2004). The lateral mobility of NHE3 on the apical membrane of renal epithelial OK cells is limited by the PDZ domain proteins NHERF1/2, but is dependent on an intact actin cytoskeleton as determined by FRAP. J. Cell Sci. 117, 3353-3365.
    • (2004) J. Cell Sci , vol.117 , pp. 3353-3365
    • Cha, B.1    Kenworthy, A.2    Murtazina, R.3    Donowitz, M.4
  • 14
    • 33744779069 scopus 로고    scopus 로고
    • The NHE3 juxtamembrane cytoplasmic domain directly binds ezrin: Dual role in NHE3 trafficking and mobility in the brush border
    • Cha, B., Tse, M., Yun, C., Kovbasnjuk, O., Mohan, S., Hubbard, A., Arpin, M. and Donowitz, M. (2006a). The NHE3 juxtamembrane cytoplasmic domain directly binds ezrin: dual role in NHE3 trafficking and mobility in the brush border. Mol. Biol. Cell 17, 2661-2673.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2661-2673
    • Cha, B.1    Tse, M.2    Yun, C.3    Kovbasnjuk, O.4    Mohan, S.5    Hubbard, A.6    Arpin, M.7    Donowitz, M.8
  • 15
    • 66449112361 scopus 로고    scopus 로고
    • NHE3 has restricted brush border (BB) mobility due to cytoskeletal association which is dynamic as part of acute stimulation and inhibition
    • Cha, B., Kenworthy, A., Tse, M. and Donowitz, M. (2006b). NHE3 has restricted brush border (BB) mobility due to cytoskeletal association which is dynamic as part of acute stimulation and inhibition. Gastroenterology 132, A100.
    • (2006) Gastroenterology , vol.132
    • Cha, B.1    Kenworthy, A.2    Tse, M.3    Donowitz, M.4
  • 16
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P. Y. and Fasman, G. D. (1974). Prediction of protein conformation. Biochemistry 13, 222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 18
    • 34447629085 scopus 로고    scopus 로고
    • Regulatory binding partners and complexes of NHE3
    • Donowitz, M. and Li, X. (2007). Regulatory binding partners and complexes of NHE3. Physiol. Rev. 87, 825-887.
    • (2007) Physiol. Rev , vol.87 , pp. 825-887
    • Donowitz, M.1    Li, X.2
  • 20
    • 48749106109 scopus 로고    scopus 로고
    • The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport
    • Faham, S., Watanabe, A., Besserer, G. M., Cascio, D., Specht, A., Hirayama, B. A., Wright, E. M. and Abramson, J. (2008). The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport. Science 321 , 810-814.
    • (2008) Science , vol.321 , pp. 810-814
    • Faham, S.1    Watanabe, A.2    Besserer, G.M.3    Cascio, D.4    Specht, A.5    Hirayama, B.A.6    Wright, E.M.7    Abramson, J.8
  • 22
    • 53549110255 scopus 로고    scopus 로고
    • Steady-state function of the ubiquitous mammalian Na/H exchanger (NHE1) in relation to dimmer coupling models with 2Na/2H stoichiometry
    • Fuster, D., Moe, O. W. and Hilgemann, D. W. (2008). Steady-state function of the ubiquitous mammalian Na/H exchanger (NHE1) in relation to dimmer coupling models with 2Na/2H stoichiometry. J. Gen. Physiol. 132, 465-480.
    • (2008) J. Gen. Physiol , vol.132 , pp. 465-480
    • Fuster, D.1    Moe, O.W.2    Hilgemann, D.W.3
  • 23
    • 0033231441 scopus 로고    scopus 로고
    • Inhibition of Na+/H+ exchange impairs receptor-mediated albumin endocytosis in renal proximal tubule-derived epithelial cells from opossum
    • Gekle, M., Drumm, K., Mildenberger, S., Freudinger, R., Gassner, B. and Silbernagll, S. (1999). Inhibition of Na+/H+ exchange impairs receptor-mediated albumin endocytosis in renal proximal tubule-derived epithelial cells from opossum. J. Physiol. 520, 709-721.
    • (1999) J. Physiol , vol.520 , pp. 709-721
    • Gekle, M.1    Drumm, K.2    Mildenberger, S.3    Freudinger, R.4    Gassner, B.5    Silbernagll, S.6
  • 24
    • 0035868903 scopus 로고    scopus 로고
    • Inhibition of Na+/H+ exchanger 3 interferes with apical receptor-mediated endocytosis via vesicle fusion
    • Gekle, M., Freudinger, R. and Mildenberger, S. (2001). Inhibition of Na+/H+ exchanger 3 interferes with apical receptor-mediated endocytosis via vesicle fusion. J. Physiol. 531, 619-629.
    • (2001) J. Physiol , vol.531 , pp. 619-629
    • Gekle, M.1    Freudinger, R.2    Mildenberger, S.3
  • 25
    • 0035824614 scopus 로고    scopus 로고
    • Association of Na(+)-H(+) exchanger isoform NHE3 and dipeptidyl peptidase IV in the renal proximal tubule
    • Girardi, A. C Degray, B. C., Nagy, T., Biemesderfer, D. and Aronson, P. S. (2001). Association of Na(+)-H(+) exchanger isoform NHE3 and dipeptidyl peptidase IV in the renal proximal tubule. J. Biol. Chem. 276, 46671-46677.
    • (2001) J. Biol. Chem , vol.276 , pp. 46671-46677
    • Girardi, A.C.1    Degray, B.C.2    Nagy, T.3    Biemesderfer, D.4    Aronson, P.S.5
  • 26
    • 6044261454 scopus 로고    scopus 로고
    • Role of dipeptidyl peptidase IV in regulating activity of Na+/H+ exchanger isoform NHE3 in proximal tubule cells
    • Girardi, A. C., Knauf, F., Demuth, H. U. and Aronson, P. S. (2004). Role of dipeptidyl peptidase IV in regulating activity of Na+/H+ exchanger isoform NHE3 in proximal tubule cells. Am. J. Physiol. Cell Physiol. 287, C1238-C1245.
    • (2004) Am. J. Physiol. Cell Physiol , vol.287
    • Girardi, A.C.1    Knauf, F.2    Demuth, H.U.3    Aronson, P.S.4
  • 27
    • 38849093208 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition downregulates Na+-H+ exchanger NHE3 in rat renal proximal tubule
    • Girardi, A. C Fukuda, L. E., Rossoni, L. V., Malnic, G. and Rebougas, N. A. (2008). Dipeptidyl peptidase IV inhibition downregulates Na+-H+ exchanger NHE3 in rat renal proximal tubule. Am. J. Physiol. Renal Physiol. 294, F414-F422.
    • (2008) Am. J. Physiol. Renal Physiol , vol.294
    • Girardi, A.C.1    Fukuda, L.E.2    Rossoni, L.V.3    Malnic, G.4    Rebougas, N.A.5
  • 30
    • 57749112095 scopus 로고    scopus 로고
    • 3) Receptor-binding protein released with IP3, binds Na+/H+ exchanger NHE3 and activates NHE3 activity in response to calcium
    • 3) Receptor-binding protein released with IP3, binds Na+/H+ exchanger NHE3 and activates NHE3 activity in response to calcium. J. Biol. Chem. 283, 33544-33553.
    • (2008) J. Biol. Chem , vol.283 , pp. 33544-33553
    • He, P.1    Zhang, H.2    Yun, C.C.3
  • 36
    • 0030830711 scopus 로고    scopus 로고
    • Ileal microvillar protein villin is tyrosine-phosphorylated and associates with PLC-gamma1: Role of cytoskeletal rearrangement in the carbachol-induced inhibition of ileal NaCl absorption
    • Khurana, S., Arpin, M., Patterson, R. and Donowitz, M. (1997). Ileal microvillar protein villin is tyrosine-phosphorylated and associates with PLC-gamma1: role of cytoskeletal rearrangement in the carbachol-induced inhibition of ileal NaCl absorption. J. Biol. Chem. 272, 30115-30121.
    • (1997) J. Biol. Chem , vol.272 , pp. 30115-30121
    • Khurana, S.1    Arpin, M.2    Patterson, R.3    Donowitz, M.4
  • 37
    • 0037189512 scopus 로고    scopus 로고
    • + exchanger 3 (NHE3) requires an NHE3- E3KARP-alpha-actinin-4 complex for oligomerization and endocytosis
    • + exchanger 3 (NHE3) requires an NHE3- E3KARP-alpha-actinin-4 complex for oligomerization and endocytosis. J. Biol. Chem. 277, 23714-23724.
    • (2002) J. Biol. Chem , vol.277 , pp. 23714-23724
    • Kim, J.H.1    Lee-Kwon, W.2    Park, J.B.3    Ryu, S.H.4    Yun, C.H.5    Donowitz, M.6
  • 38
    • 33847650845 scopus 로고    scopus 로고
    • + antiporter of Escherichia coli, at physiological pH
    • + antiporter of Escherichia coli, at physiological pH. Biochemistry46, 2419-2430.
    • (2007) Biochemistry , vol.46 , pp. 2419-2430
    • Kozachkov, L.1    Herz, K.2    Padan, E.3
  • 39
    • 0037108068 scopus 로고    scopus 로고
    • The down regulated in adenoma (dra) gene product binds to the second PDZ domain of the NHE3 kinase A regulatory protein (E3KARP), potentially linking intestinal Cl-HCO3-exchange to Na+/H+ exchange
    • Lamprecht, G., Heil, A., Baisch, S., Lin-Wu, E., Yun, C. C., Kalbacher, H., Gregor, M. and Seidler, U. (2002). The down regulated in adenoma (dra) gene product binds to the second PDZ domain of the NHE3 kinase A regulatory protein (E3KARP), potentially linking intestinal Cl-HCO3-exchange to Na+/H+ exchange. Biochemistry 41, 12336-12342.
    • (2002) Biochemistry , vol.41 , pp. 12336-12342
    • Lamprecht, G.1    Heil, A.2    Baisch, S.3    Lin-Wu, E.4    Yun, C.C.5    Kalbacher, H.6    Gregor, M.7    Seidler, U.8
  • 46
    • 0032521112 scopus 로고    scopus 로고
    • Relationships between Na+/glucose cotransporter (SGLT1) currents and fluxes
    • Mackenzie, B., Loo, D. D. and Wright, E. M. (1998). Relationships between Na+/glucose cotransporter (SGLT1) currents and fluxes. J. Membr. Biol. 162, 101-106.
    • (1998) J. Membr. Biol , vol.162 , pp. 101-106
    • Mackenzie, B.1    Loo, D.D.2    Wright, E.M.3
  • 47
    • 0023510866 scopus 로고
    • Structural basis for physiological regulation of paracellular pathways in intestinal epithelia
    • Madara, J. L. and Pappenheimer, J. R. (1987). Structural basis for physiological regulation of paracellular pathways in intestinal epithelia. J. Membr. Biol. 100, 149-164.
    • (1987) J. Membr. Biol , vol.100 , pp. 149-164
    • Madara, J.L.1    Pappenheimer, J.R.2
  • 48
    • 33747169125 scopus 로고    scopus 로고
    • Mutational analysis of the intramembranous H10 loop of yeast Nhx1 reveals a critical role in ion homeostasis and vesicle trafficking
    • Mukherjee, S., Kallay, L., Brett, C. L. and Rao, R. (2006). Mutational analysis of the intramembranous H10 loop of yeast Nhx1 reveals a critical role in ion homeostasis and vesicle trafficking. Biochem. J. 398, 97-105.
    • (2006) Biochem. J , vol.398 , pp. 97-105
    • Mukherjee, S.1    Kallay, L.2    Brett, C.L.3    Rao, R.4
  • 49
    • 59449095460 scopus 로고    scopus 로고
    • Functional coupling of the down regulated in adenoma Cl-/base exchanger DRA and the apical sodium/hydrogen exchangers NHE2 and NHE3
    • Musch, M. W., Arvans, D. L., Wu, G. D. and Chang, E. B. (2008). Functional coupling of the down regulated in adenoma Cl-/base exchanger DRA and the apical sodium/hydrogen exchangers NHE2 and NHE3. Am. J. Physiol. Gastrointest. Liver Physiol. 296, G202-G210.
    • (2008) Am. J. Physiol. Gastrointest. Liver Physiol , vol.296
    • Musch, M.W.1    Arvans, D.L.2    Wu, G.D.3    Chang, E.B.4
  • 50
    • 12544258841 scopus 로고    scopus 로고
    • + xchange isoforms are distributed to Golgi and post-Golgi compartments and are involved in organelle pH regulation
    • + xchange isoforms are distributed to Golgi and post-Golgi compartments and are involved in organelle pH regulation. J. Biol. Chem. 280, 1561-1572.
    • (2005) J. Biol. Chem , vol.280 , pp. 1561-1572
    • Nakamura, N.1    Tanaka, S.2    Teko, Y.3    Mitsui, K.4    Kanazawa, H.5
  • 52
    • 66449100221 scopus 로고    scopus 로고
    • + exchanger localized to the trans-Golgi network
    • + exchanger localized to the trans-Golgi network. J. Biol. Chem. 280, 1561-1572.
    • (2001) J. Biol. Chem , vol.280 , pp. 1561-1572
    • Numata, M.1    Orlowski, J.2
  • 53
    • 1242272754 scopus 로고    scopus 로고
    • Diversity of the mammalian sodium/proton exchanger SLC9 gene family
    • Orlowski, J. and Grinstein, S. (2004). Diversity of the mammalian sodium/proton exchanger SLC9 gene family. Pflugers Arch. 447, 549-565.
    • (2004) Pflugers Arch , vol.447 , pp. 549-565
    • Orlowski, J.1    Grinstein, S.2
  • 54
    • 34547963769 scopus 로고    scopus 로고
    • Emerging roles of alkali cation/proton exchangers in organellar homeostasis
    • Orlowski, J. and Grinstein, S. (2007). Emerging roles of alkali cation/proton exchangers in organellar homeostasis. Curr. Opin. Cell Biol. 1, 483-492.
    • (2007) Curr. Opin. Cell Biol , vol.1 , pp. 483-492
    • Orlowski, J.1    Grinstein, S.2
  • 56
    • 0035907278 scopus 로고    scopus 로고
    • Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers
    • 17367
    • Pang, T., Su, X., Wakabayashi, S. and Shigekawa, M. (2001). Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers. J. Biol. Chem. 276, 17367, 17372.
    • (2001) J. Biol. Chem , vol.276 , pp. 17372
    • Pang, T.1    Su, X.2    Wakabayashi, S.3    Shigekawa, M.4
  • 61
    • 12544256432 scopus 로고    scopus 로고
    • Akt2 phosphorylates ezrin to trigger NHE3 translocation and activation
    • Shiue, H., Musch, M. W., Wang, Y., Chang, E. B. and Turner, J. R. (2005). Akt2 phosphorylates ezrin to trigger NHE3 translocation and activation. J. Biol. Chem. 280, 1688-1695.
    • (2005) J. Biol. Chem , vol.280 , pp. 1688-1695
    • Shiue, H.1    Musch, M.W.2    Wang, Y.3    Chang, E.B.4    Turner, J.R.5
  • 62
    • 66449131072 scopus 로고    scopus 로고
    • Sullivan, S., Alex, P., Dassopoulos, T., Zachos, N. C lacobuzio-Donahue, C Donowitz, M., Brant, S. R., Cuffari, C., Harris, M. L., Datta, L. W. et al. (2008). Downregulation of sodium transporters and NHERF proteins in IBD patients and mouse colitis models: potential contributors to IBD-associated diarrhea. Inflamm. Bowel Dis. 15, 261-274.
    • Sullivan, S., Alex, P., Dassopoulos, T., Zachos, N. C lacobuzio-Donahue, C Donowitz, M., Brant, S. R., Cuffari, C., Harris, M. L., Datta, L. W. et al. (2008). Downregulation of sodium transporters and NHERF proteins in IBD patients and mouse colitis models: potential contributors to IBD-associated diarrhea. Inflamm. Bowel Dis. 15, 261-274.
  • 64
    • 34347379290 scopus 로고    scopus 로고
    • H+-coupled nutrient, micronutrient and drug transporters in the mammalian small intestine
    • Thwaites, D. T. and Anderson, C. M. (2007). H+-coupled nutrient, micronutrient and drug transporters in the mammalian small intestine. Exp. Physiol. 92, 603-619.
    • (2007) Exp. Physiol , vol.92 , pp. 603-619
    • Thwaites, D.T.1    Anderson, C.M.2
  • 67
    • 36148953899 scopus 로고    scopus 로고
    • Phosphorylation of PDZ1 domain attenuates NHERF-1 binding to cellular targets
    • Voltz, J. W., Brush, M., Sikes, S., Steplock, D., Weinman, E. J. and Shenolikar, S. (2007). Phosphorylation of PDZ1 domain attenuates NHERF-1 binding to cellular targets. J. Biol. Chem. 282, 33879-33887.
    • (2007) J. Biol. Chem , vol.282 , pp. 33879-33887
    • Voltz, J.W.1    Brush, M.2    Sikes, S.3    Steplock, D.4    Weinman, E.J.5    Shenolikar, S.6
  • 68
    • 0034677758 scopus 로고    scopus 로고
    • A novel topology model of the human Na+/H+ exchanger isoforms 1
    • Wakabayashi, S., Pang, T., Su, X. and Shigekawa, M. (2000). A novel topology model of the human Na+/H+ exchanger isoforms 1. J. Biol. Chem. 275, 7942-7949.
    • (2000) J. Biol. Chem , vol.275 , pp. 7942-7949
    • Wakabayashi, S.1    Pang, T.2    Su, X.3    Shigekawa, M.4
  • 70
    • 36048958880 scopus 로고    scopus 로고
    • Parathyroid hormone inhibits renal phosphate transport by phosphorylation of serine 77 of sodium-hydrogen exchanger regulatory factor-1
    • Weinman, E. J., Biswas, R. S., Peng, G., Shen, L., Turner, C. L., E, X., Steplock, D., Shenolikar, S. and Cunningham, R. (2007). Parathyroid hormone inhibits renal phosphate transport by phosphorylation of serine 77 of sodium-hydrogen exchanger regulatory factor-1. J. Clin. Invest. 117, 3412-3420.
    • (2007) J. Clin. Invest , vol.117 , pp. 3412-3420
    • Weinman, E.J.1    Biswas, R.S.2    Peng, G.3    Shen, L.4    Turner, C.L.E.X.5    Steplock, D.6    Shenolikar, S.7    Cunningham, R.8
  • 71
    • 0035793559 scopus 로고    scopus 로고
    • + exchanger Nhx1 is an N-linked glycoprotein. Topological implications
    • + exchanger Nhx1 is an N-linked glycoprotein. Topological implications. J. Biol. Chem. 276, 3401-3407.
    • (2001) J. Biol. Chem , vol.276 , pp. 3401-3407
    • Wells, K.M.1    Rao, R.2
  • 72
    • 21744432667 scopus 로고    scopus 로고
    • Subcloning, localization, and expression of the rat intestinal sodium-hydrogen exchanger isoforms 8
    • Xu, H., Chen, R. and Ghishan, F. K. (2005). Subcloning, localization, and expression of the rat intestinal sodium-hydrogen exchanger isoforms 8. Am. J. Physiol. Gastrointest. Liver Physiol. 289, G36-G41.
    • (2005) Am. J. Physiol. Gastrointest. Liver Physiol , vol.289
    • Xu, H.1    Chen, R.2    Ghishan, F.K.3
  • 73
    • 38349143138 scopus 로고    scopus 로고
    • Gastrointestinal distribution and kinetic characterization of the sodium-hydrogen exchanger isoforms 9 (NHE8)
    • Xu, H., Chen, H., Dong, J., Lynch, R. and Ghishan, F. K. (2008). Gastrointestinal distribution and kinetic characterization of the sodium-hydrogen exchanger isoforms 9 (NHE8). Cell Physiol. Biochem. 21, 109-116.
    • (2008) Cell Physiol. Biochem , vol.21 , pp. 109-116
    • Xu, H.1    Chen, H.2    Dong, J.3    Lynch, R.4    Ghishan, F.K.5
  • 76
    • 15744368985 scopus 로고    scopus 로고
    • + exchange. Annu. Rev. Physiol. 67, 411-443.
    • + exchange. Annu. Rev. Physiol. 67, 411-443.
  • 77
    • 66449096718 scopus 로고    scopus 로고
    • Phospholipase Cy (PLCy) directly binds to the Na+/H+ exchanger 3 (NHE3) C-terminus which is necessary for basal and calcium-mediated inhibition of NHE3 activity
    • Zachos, N. C., van Rossum, D. B., Patterson, R., Snyder, S. and Donowitz, M. (2008). Phospholipase Cy (PLCy) directly binds to the Na+/H+ exchanger 3 (NHE3) C-terminus which is necessary for basal and calcium-mediated inhibition of NHE3 activity. Gastroenterology 134, A107.
    • (2008) Gastroenterology , vol.134
    • Zachos, N.C.1    van Rossum, D.B.2    Patterson, R.3    Snyder, S.4    Donowitz, M.5
  • 79
    • 0034636804 scopus 로고    scopus 로고
    • + exchanger NHE3 has 11 membrane spanning domains and a cleaved signal peptide: Topology analysis using in vitro transcription/translation
    • + exchanger NHE3 has 11 membrane spanning domains and a cleaved signal peptide: topology analysis using in vitro transcription/translation. Biochemistry39, 8102-8112.
    • (2000) Biochemistry , vol.39 , pp. 8102-8112
    • Zizak, M.1    Cavet, M.E.2    Bayle, D.3    Tse, C.M.4    Hallen, S.5    Sachs, G.6    Donowitz, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.