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Volumn 13, Issue 1, 2012, Pages 116-128

The parathyroid hormone receptorsome and the potential for therapeutic intervention

Author keywords

Arrestins; Calmodulin; Calpain; Ezrin; G proteins; NHERF 1 and 2; Osteoporosis; Parathyroid hormone; Parathyroid hormone 1 receptor

Indexed keywords

ARGININE; CALMODULIN; CALPAIN; EZRIN; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; LYSINE; PARATHYROID HORMONE; PARATHYROID HORMONE RECEPTOR; PARATHYROID HORMONE RECEPTOR 1; PARATHYROID HORMONE RELATED PROTEIN; PDZ PROTEIN; PHOSPHATE; PROTEIN NHERF 1; UNCLASSIFIED DRUG;

EID: 84855846095     PISSN: 13894501     EISSN: 18735592     Source Type: Journal    
DOI: 10.2174/138945012798868416     Document Type: Article
Times cited : (16)

References (112)
  • 1
    • 0032735547 scopus 로고    scopus 로고
    • Receptors for PTH and PTHrP: Their biological importance and functional properties
    • Mannstadt M, Jüppner H, Gardella T. Receptors for PTH and PTHrP: their biological importance and functional properties. Am J Physiol 1999; 277: F665-75.
    • (1999) Am J Physiol , vol.277
    • Mannstadt, M.1    Jüppner, H.2    Gardella, T.3
  • 2
    • 0037373225 scopus 로고    scopus 로고
    • Midgestational lethality in mice lacking the parathyroid hormone (PTH)/PTH-related peptide receptor is associated with abrupt cardiomyocyte death
    • Qian J, Colbert MC, Witte D, et al. Midgestational lethality in mice lacking the parathyroid hormone (PTH)/PTH-related peptide receptor is associated with abrupt cardiomyocyte death. Endocrinology 2003; 144(3): 1053-61.
    • (2003) Endocrinology , vol.144 , Issue.3 , pp. 1053-1061
    • Qian, J.1    Colbert, M.C.2    Witte, D.3
  • 3
    • 0031808508 scopus 로고    scopus 로고
    • Coupling of the PTH/PTHrP receptor to multiple G-proteins. Direct demonstration of receptor activation of Gs, Gq/11, and Gi(1) by [alpha-32P]GTPgamma-azidoanilide photoaffinity labeling
    • Schwindinger WF, Fredericks J, Watkins L, et al. Coupling of the PTH/PTHrP receptor to multiple G-proteins. Direct demonstration of receptor activation of Gs, Gq/11, and Gi(1) by [alpha-32P]GTPgamma-azidoanilide photoaffinity labeling. Endocrine 1998; 8(2): 201-9.
    • (1998) Endocrine , vol.8 , Issue.2 , pp. 201-209
    • Schwindinger, W.F.1    Fredericks, J.2    Watkins, L.3
  • 4
    • 0027292853 scopus 로고
    • Cloned, stably expressed parathyroid hormone (PTH)/PTH-related peptide receptors activate multiple messenger signals and biological responses in LLC-PK1 kidney cells
    • Bringhurst FR, Jüppner H, Guo J, et al. Cloned, stably expressed parathyroid hormone (PTH)/PTH-related peptide receptors activate multiple messenger signals and biological responses in LLC-PK1 kidney cells. Endocrinology 1993; 132(5): 2090-2098.
    • (1993) Endocrinology , vol.132 , Issue.5 , pp. 2090-2098
    • Bringhurst, F.R.1    Jüppner, H.2    Guo, J.3
  • 5
    • 0025035439 scopus 로고
    • Stimulation of transient elevations in cytosolic Ca2+ is related to inhibition of Pi transport in OK cells
    • Miyauchi A, Dobre V, Rickmeyer M, Cole J, Forte L, Hruska KA. Stimulation of transient elevations in cytosolic Ca2+ is related to inhibition of Pi transport in OK cells. Am J Physiol 1990; 259(3 Pt 2): F485-93.
    • (1990) Am J Physiol , vol.259 , Issue.3 PART 2
    • Miyauchi, A.1    Dobre, V.2    Rickmeyer, M.3    Cole, J.4    Forte, L.5    Hruska, K.A.6
  • 6
    • 0027291932 scopus 로고
    • Parathyroid hormone increases cytosolic calcium concentration in adult rat cardiac myocytes
    • Smogorzewski M, Zayed M, Zhang YB, Roe J, Massry SG. Parathyroid hormone increases cytosolic calcium concentration in adult rat cardiac myocytes. Am J Physiol 1993; 264(6 Pt 2): H1998-2006.
    • (1993) Am J Physiol , vol.264 , Issue.6 PART 2
    • Smogorzewski, M.1    Zayed, M.2    Zhang, Y.B.3    Roe, J.4    Massry, S.G.5
  • 7
    • 0027416439 scopus 로고
    • Parathyroid hormone raises cytosolic calcium in pancreatic islets: Study on mechanisms
    • Fadda GZ, Thanakitcharu P, Smogorzewski M, Massry SG. Parathyroid hormone raises cytosolic calcium in pancreatic islets: study on mechanisms. Kidney Int 1993; 43(3): 554-60.
    • (1993) Kidney Int , vol.43 , Issue.3 , pp. 554-560
    • Fadda, G.Z.1    Thanakitcharu, P.2    Smogorzewski, M.3    Massry, S.G.4
  • 8
    • 0028961707 scopus 로고
    • Pathways involved in PTH-induced rise in cytosolic Ca2+ concentration of rat renal proximal tubule
    • Tanaka H, Smogorzewski M, Koss M, Massry SG. Pathways involved in PTH-induced rise in cytosolic Ca2+ concentration of rat renal proximal tubule. Am J Physiol 1995; 268(2 Pt 2): F330-7.
    • (1995) Am J Physiol , vol.268 , Issue.2 PART 2
    • Tanaka, H.1    Smogorzewski, M.2    Koss, M.3    Massry, S.G.4
  • 9
    • 2542420098 scopus 로고    scopus 로고
    • Stimulation by parathyroid hormone of a NHERF-1-assembled complex consisting of the parathyroid hormone I receptor, phospholipase Cbeta, and actin increases intracellular calcium in opossum kidney cells
    • Mahon M, Segre G. Stimulation by parathyroid hormone of a NHERF-1-assembled complex consisting of the parathyroid hormone I receptor, phospholipase Cbeta, and actin increases intracellular calcium in opossum kidney cells. J Biol Chem 2004; 279: 23550-8.
    • (2004) J Biol Chem , vol.279 , pp. 23550-23558
    • Mahon, M.1    Segre, G.2
  • 10
    • 0033305424 scopus 로고    scopus 로고
    • Parathyroid hormone activates mitogen-activated protein kinase in opossum kidney cells
    • Cole JA. Parathyroid hormone activates mitogen-activated protein kinase in opossum kidney cells. Endocrinology 1999; 140(12): 5771-9.
    • (1999) Endocrinology , vol.140 , Issue.12 , pp. 5771-5779
    • Cole, J.A.1
  • 11
    • 17744388606 scopus 로고    scopus 로고
    • G alpha12/G alpha13 subunits of heterotrimeric G proteins mediate parathyroid hormone activation of phospholipase D in UMR-106 osteoblastic cells
    • Singh AT, Gilchrist A, Voyno-Yasenetskaya T, Radeff-Huang JM, Stern PH. G alpha12/G alpha13 subunits of heterotrimeric G proteins mediate parathyroid hormone activation of phospholipase D in UMR-106 osteoblastic cells. Endocrinology 2005; 146(5): 2171-5.
    • (2005) Endocrinology , vol.146 , Issue.5 , pp. 2171-2175
    • Singh, A.T.1    Gilchrist, A.2    Voyno-Yasenetskaya, T.3    Radeff-Huang, J.M.4    Stern, P.H.5
  • 12
    • 0034893961 scopus 로고    scopus 로고
    • Nitric oxide as a second messenger in parathyroid hormone-related protein signaling
    • Kalinowski L, Dobrucki LW, Malinski T. Nitric oxide as a second messenger in parathyroid hormone-related protein signaling. J Endocrinol 2001; 170(2): 433-40.
    • (2001) J Endocrinol , vol.170 , Issue.2 , pp. 433-440
    • Kalinowski, L.1    Dobrucki, L.W.2    Malinski, T.3
  • 13
    • 0033324980 scopus 로고    scopus 로고
    • Vasorelaxant properties of parathyroid hormone-related protein in the mouse: Evidence for endothelium involvement independent of nitric oxide formation
    • Sutliff RL, Weber CS, Qian J, Miller ML, Clemens TL, Paul RJ. Vasorelaxant properties of parathyroid hormone-related protein in the mouse: evidence for endothelium involvement independent of nitric oxide formation. Endocrinology 1999; 140(5): 2077-83.
    • (1999) Endocrinology , vol.140 , Issue.5 , pp. 2077-2083
    • Sutliff, R.L.1    Weber, C.S.2    Qian, J.3    Miller, M.L.4    Clemens, T.L.5    Paul, R.J.6
  • 14
    • 0030460776 scopus 로고    scopus 로고
    • The N-terminal region of the third intracellular loop of the parathyroid hormone (PTH)/PTH-related peptide receptor is critical for coupling to cAMP and inositol phosphate/Ca2++ signal transduction pathways
    • Huang Z, Chen Y, Pratt S, et al. The N-terminal region of the third intracellular loop of the parathyroid hormone (PTH)/PTH-related peptide receptor is critical for coupling to cAMP and inositol phosphate/Ca2++ signal transduction pathways. J Biol Chem 1996; 271: 33382-9.
    • (1996) J Biol Chem , vol.271 , pp. 33382-33389
    • Huang, Z.1    Chen, Y.2    Pratt, S.3
  • 15
    • 0030895863 scopus 로고    scopus 로고
    • Mutations in the second cytoplasmic loop of the rat parathyroid hormone (PTH)/PTHrelated protein receptor result in selective loss of PTH-stimulated phospholipase C activity
    • Iida-Klein A, Guo J, Takamura M, et al. Mutations in the second cytoplasmic loop of the rat parathyroid hormone (PTH)/PTHrelated protein receptor result in selective loss of PTH-stimulated phospholipase C activity. J Biol Chem 1997; 272: 6882-9.
    • (1997) J Biol Chem , vol.272 , pp. 6882-6889
    • Iida-Klein, A.1    Guo, J.2    Takamura, M.3
  • 17
    • 0030613761 scopus 로고    scopus 로고
    • Switching of the coupling of the beta2-adrenergic receptor to different G proteins by protein kinase A
    • Daaka Y, Luttrell LM, Lefkowitz RJ. Switching of the coupling of the beta2-adrenergic receptor to different G proteins by protein kinase A. Nature 1997; 390(6655): 88-91.
    • (1997) Nature , vol.390 , Issue.6655 , pp. 88-91
    • Daaka, Y.1    Luttrell, L.M.2    Lefkowitz, R.J.3
  • 18
    • 0028904960 scopus 로고
    • Truncation of the carboxylterminal region of the parathyroid hormone (PTH)/PTH-related peptide receptor enhances PTH stimulation of adenylate cyclase but not phospholipase C
    • Iida-Klein A, Guo J, Xie LY, et al. Truncation of the carboxylterminal region of the parathyroid hormone (PTH)/PTH-related peptide receptor enhances PTH stimulation of adenylate cyclase but not phospholipase C. J Biol Chem 1995; 270: 8458-65.
    • (1995) J Biol Chem , vol.270 , pp. 8458-8465
    • Iida-Klein, A.1    Guo, J.2    Xie, L.Y.3
  • 19
    • 12744281523 scopus 로고    scopus 로고
    • Calmodulin interacts with the cytoplasmic tails of the parathyroid hormone 1 receptor and a sub-set of class b G-protein coupled receptors
    • Mahon MJ, Shimada M. Calmodulin interacts with the cytoplasmic tails of the parathyroid hormone 1 receptor and a sub-set of class b G-protein coupled receptors. FEBS Lett 2005; 579(3): 803-7.
    • (2005) FEBS Lett , vol.579 , Issue.3 , pp. 803-807
    • Mahon, M.J.1    Shimada, M.2
  • 20
    • 29444434762 scopus 로고    scopus 로고
    • A docking site for G protein betagamma subunits on the parathyroid hormone 1 receptor supports signaling through multiple pathways
    • Mahon MJ, Bonacci TM, Divieti P, Smrcka AV. A docking site for G protein betagamma subunits on the parathyroid hormone 1 receptor supports signaling through multiple pathways. Mol Endocrinol 2006; 20(1): 136-46.
    • (2006) Mol Endocrinol , vol.20 , Issue.1 , pp. 136-146
    • Mahon, M.J.1    Bonacci, T.M.2    Divieti, P.3    Smrcka, A.V.4
  • 21
    • 17744370970 scopus 로고    scopus 로고
    • The receptor for parathyroid hormone and parathyroid hormone-related peptide is hydrolyzed and its signaling properties are altered by directly binding the calpain small subunit
    • Shimada M, Mahon MJ, Greer PA, Segre GV. The receptor for parathyroid hormone and parathyroid hormone-related peptide is hydrolyzed and its signaling properties are altered by directly binding the calpain small subunit. Endocrinology 2005; 146(5): 2336-44.
    • (2005) Endocrinology , vol.146 , Issue.5 , pp. 2336-2344
    • Shimada, M.1    Mahon, M.J.2    Greer, P.A.3    Segre, G.V.4
  • 22
    • 0035903123 scopus 로고    scopus 로고
    • Mapping of calmodulin and Gbetagamma binding domains within the Cterminal region of the metabotropic glutamate receptor 7A
    • El Far O, Bofill-Cardona E, Airas JM, et al. Mapping of calmodulin and Gbetagamma binding domains within the Cterminal region of the metabotropic glutamate receptor 7A. J Biol Chem 2001; 276(33): 30662-9.
    • (2001) J Biol Chem , vol.276 , Issue.33 , pp. 30662-30669
    • El Far, O.1    Bofill-Cardona, E.2    Airas, J.M.3
  • 23
    • 0032568664 scopus 로고    scopus 로고
    • Sites for Galpha binding on the G protein beta subunit overlap with sites for regulation of phospholipase Cbeta and adenylyl cyclase
    • Li Y, Sternweis PM, Charnecki S, et al. Sites for Galpha binding on the G protein beta subunit overlap with sites for regulation of phospholipase Cbeta and adenylyl cyclase. J Biol Chem 1998; 273(26): 16265-72.
    • (1998) J Biol Chem , vol.273 , Issue.26 , pp. 16265-16272
    • Li, Y.1    Sternweis, P.M.2    Charnecki, S.3
  • 24
    • 46049115862 scopus 로고    scopus 로고
    • Structure of the parathyroid hormone receptor C terminus bound to the Gprotein dimer Gbeta1gamma2
    • Johnston CA, Kimple AJ, Giguere PM, Siderovski DP. Structure of the parathyroid hormone receptor C terminus bound to the Gprotein dimer Gbeta1gamma2. Structure 2008; 16(7): 1086-94.
    • (2008) Structure , vol.16 , Issue.7 , pp. 1086-1094
    • Johnston, C.A.1    Kimple, A.J.2    Giguere, P.M.3    Siderovski, D.P.4
  • 26
    • 33746155723 scopus 로고    scopus 로고
    • Calpain involvement in the remodeling of cytoskeletal anchorage complexes
    • Lebart MC, Benyamin Y. Calpain involvement in the remodeling of cytoskeletal anchorage complexes. FEBS J 2006; 273(15): 3415-26.
    • (2006) FEBS J , vol.273 , Issue.15 , pp. 3415-3426
    • Lebart, M.C.1    Benyamin, Y.2
  • 27
    • 0027162182 scopus 로고
    • Ezrin-calpain I interactions in gastric parietal cells
    • Yao X, Thibodeau A, Forte JG. Ezrin-calpain I interactions in gastric parietal cells. Am J Physiol 1993; 265(1 Pt 1): C36-46.
    • (1993) Am J Physiol , vol.265 , Issue.1 PART 1
    • Yao, X.1    Thibodeau, A.2    Forte, J.G.3
  • 28
    • 0031570762 scopus 로고    scopus 로고
    • The calpain-calpastatin system and cellular proliferation and differentiation in rodent osteoblastic cells
    • Murray SS, Grisanti MS, Bentley GV, Kahn AJ, Urist MR, Murray EJ. The calpain-calpastatin system and cellular proliferation and differentiation in rodent osteoblastic cells. Exp Cell Res 1997; 233(2): 297-309.
    • (1997) Exp Cell Res , vol.233 , Issue.2 , pp. 297-309
    • Murray, S.S.1    Grisanti, M.S.2    Bentley, G.V.3    Kahn, A.J.4    Urist, M.R.5    Murray, E.J.6
  • 29
    • 0028926482 scopus 로고
    • Parathyroid hormoneinduced retraction of MC3T3-E1 osteoblastic cells is attenuated by the calpain inhibitor N-Ac-Leu-Leu-norleucinal
    • Murray EJ, Tram KK, Murray SS, Lee DB. Parathyroid hormoneinduced retraction of MC3T3-E1 osteoblastic cells is attenuated by the calpain inhibitor N-Ac-Leu-Leu-norleucinal. Metabolism 1995; 44(2): 141-4.
    • (1995) Metabolism , vol.44 , Issue.2 , pp. 141-144
    • Murray, E.J.1    Tram, K.K.2    Murray, S.S.3    Lee, D.B.4
  • 31
    • 51049114509 scopus 로고    scopus 로고
    • In vivo targeted deletion of calpain small subunit, Capn4, in cells of the osteoblast lineage impairs cell proliferation, differentiation, and bone formation
    • Shimada M, Greer PA, McMahon AP, Bouxsein ML, Schipani E. In vivo targeted deletion of calpain small subunit, Capn4, in cells of the osteoblast lineage impairs cell proliferation, differentiation, and bone formation. J Biol Chem 2008; 283(30): 21002-10.
    • (2008) J Biol Chem , vol.283 , Issue.30 , pp. 21002-21010
    • Shimada, M.1    Greer, P.A.2    McMahon, A.P.3    Bouxsein, M.L.4    Schipani, E.5
  • 32
    • 77952612543 scopus 로고    scopus 로고
    • Targeted deletion of Capn4 in cells of the chondrocyte lineage impairs chondrocyte proliferation and differentiation
    • Kashiwagi A, Schipani E, Fein MJ, Greer PA, Shimada M. Targeted deletion of Capn4 in cells of the chondrocyte lineage impairs chondrocyte proliferation and differentiation. Mol Cell Biol 2010; 30(11): 2799-810.
    • (2010) Mol Cell Biol , vol.30 , Issue.11 , pp. 2799-2810
    • Kashiwagi, A.1    Schipani, E.2    Fein, M.J.3    Greer, P.A.4    Shimada, M.5
  • 33
    • 56749152348 scopus 로고    scopus 로고
    • The Year in Basic Science: Calmodulin kinase cascades
    • Means AR. The Year in Basic Science: calmodulin kinase cascades. Mol Endocrinol 2008; 22(12): 2759-65.
    • (2008) Mol Endocrinol , vol.22 , Issue.12 , pp. 2759-2765
    • Means, A.R.1
  • 34
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads AR, Friedberg F. Sequence motifs for calmodulin recognition. Faseb J 1997; 11(5): 331-40.
    • (1997) Faseb J , vol.11 , Issue.5 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 35
    • 0022503880 scopus 로고
    • Possible role of calcium in parathyroid hormone actions in rabbit renal proximal tubules
    • Yanagawa N, Jo OD. Possible role of calcium in parathyroid hormone actions in rabbit renal proximal tubules. Am J Physiol 1986; 250(5 Pt 2): F942-8.
    • (1986) Am J Physiol , vol.250 , Issue.5 PART 2
    • Yanagawa, N.1    Jo, O.D.2
  • 36
    • 0022506052 scopus 로고
    • Parathyroid hormoneinduced changes of the brush border membrane topography and cytosketelon in cultured renal proximal tubular cells
    • Goligorsky MS, Menton DN, Hruska KA. Parathyroid hormoneinduced changes of the brush border membrane topography and cytosketelon in cultured renal proximal tubular cells. J Membr Biol 1986; 92: 151-62.
    • (1986) J Membr Biol , vol.92 , pp. 151-162
    • Goligorsky, M.S.1    Menton, D.N.2    Hruska, K.A.3
  • 38
    • 0033868210 scopus 로고    scopus 로고
    • Parathyroid hormone induces rat interstitial collagenase mRNA through Ets-1 facilitated by cyclic AMP response element-binding protein and Ca(2+)/calmodulin-dependent protein kinase II in osteoblastic cells
    • Quinn CO, Rajakumar RA, Agapova OA. Parathyroid hormone induces rat interstitial collagenase mRNA through Ets-1 facilitated by cyclic AMP response element-binding protein and Ca(2+)/calmodulin-dependent protein kinase II in osteoblastic cells. J Mol Endocrinol 2000; 25(1): 73-84.
    • (2000) J Mol Endocrinol , vol.25 , Issue.1 , pp. 73-84
    • Quinn, C.O.1    Rajakumar, R.A.2    Agapova, O.A.3
  • 39
    • 0033570107 scopus 로고    scopus 로고
    • Endocytosis of Ligand-Human Parathyroid Hormone Receptor 1 Complexes Is Protein Kinase C-dependent and Involves-Arrestin2
    • Ferrari S, Behar V, Chorev M, Rosenblatt M, Bisello A. Endocytosis of Ligand-Human Parathyroid Hormone Receptor 1 Complexes Is Protein Kinase C-dependent and Involves-Arrestin2. J Biol Chem 1999; 274: 29968-75.
    • (1999) J Biol Chem , vol.274 , pp. 29968-29975
    • Ferrari, S.1    Behar, V.2    Chorev, M.3    Rosenblatt, M.4    Bisello, A.5
  • 40
    • 0036139163 scopus 로고    scopus 로고
    • Phosphorylation of the receptor for PTH and PTHrP is required for internalization and regulates receptor signaling
    • Tawfeek HA, Qian F, Abou-Samra AB. Phosphorylation of the receptor for PTH and PTHrP is required for internalization and regulates receptor signaling. Mol Endocrinol 2002; 16(1): 1-13.
    • (2002) Mol Endocrinol , vol.16 , Issue.1 , pp. 1-13
    • Tawfeek, H.A.1    Qian, F.2    Abou-Samra, A.B.3
  • 41
    • 0037041007 scopus 로고    scopus 로고
    • Internalization determinants of the parathyroid hormone receptor differentially regulate beta-arrestin/receptor association
    • Vilardaga JP, Krasel C, Chauvin S, Bambino T, Lohse MJ, Nissenson RA. Internalization determinants of the parathyroid hormone receptor differentially regulate beta-arrestin/receptor association. J Biol Chem 2002; 277(10): 8121-9.
    • (2002) J Biol Chem , vol.277 , Issue.10 , pp. 8121-8129
    • Vilardaga, J.P.1    Krasel, C.2    Chauvin, S.3    Bambino, T.4    Lohse, M.J.5    Nissenson, R.A.6
  • 42
    • 0034823739 scopus 로고    scopus 로고
    • Parathyroid hormone receptor internalization is independent of protein kinase A and phospholipase C activation
    • Tawfeek HA, Che J, Qian F, Abou-Samra AB. Parathyroid hormone receptor internalization is independent of protein kinase A and phospholipase C activation. Am J Physiol Endocrinol Metab 2001; 281(3): E545-57.
    • (2001) Am J Physiol Endocrinol Metab , vol.281 , Issue.3
    • Tawfeek, H.A.1    Che, J.2    Qian, F.3    Abou-Samra, A.B.4
  • 43
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz RJ, Shenoy SK. Transduction of receptor signals by beta-arrestins. Science 2005; 308(5721): 512-7.
    • (2005) Science , vol.308 , Issue.5721 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 44
    • 33744957160 scopus 로고    scopus 로고
    • Distinct beta-arrestinand G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation
    • Gesty-Palmer D, Chen M, Reiter E, et al. Distinct beta-arrestinand G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation. J Biol Chem 2006; 281(16): 10856-64.
    • (2006) J Biol Chem , vol.281 , Issue.16 , pp. 10856-10864
    • Gesty-Palmer, D.1    Chen, M.2    Reiter, E.3
  • 45
    • 33845967852 scopus 로고    scopus 로고
    • Proline-rich motifs in the parathyroid hormone (PTH)/PTH-related protein receptor C terminus mediate scaffolding of c-Src with betaarrestin2 for ERK1/2 activation
    • Rey A, Manen D, Rizzoli R, Caverzasio J, Ferrari SL. Proline-rich motifs in the parathyroid hormone (PTH)/PTH-related protein receptor C terminus mediate scaffolding of c-Src with betaarrestin2 for ERK1/2 activation. J Biol Chem 2006; 281(50): 38181-8.
    • (2006) J Biol Chem , vol.281 , Issue.50 , pp. 38181-38188
    • Rey, A.1    Manen, D.2    Rizzoli, R.3    Caverzasio, J.4    Ferrari, S.L.5
  • 46
    • 0037142080 scopus 로고    scopus 로고
    • Na(+)/H(+) exchanger regulatory factor 2 directs parathyroid hormone 1 receptor signalling
    • Mahon M, Donowitz M, Yun C, Segre G. Na(+)/H(+) exchanger regulatory factor 2 directs parathyroid hormone 1 receptor signalling. Nature 2002; 417: 858-61.
    • (2002) Nature , vol.417 , pp. 858-861
    • Mahon, M.1    Donowitz, M.2    Yun, C.3    Segre, G.4
  • 47
    • 0034740693 scopus 로고    scopus 로고
    • Mechanism and role of PDZ domains in signaling complex assembly
    • Harris BZ, Lim WA. Mechanism and role of PDZ domains in signaling complex assembly. J Cell Sci 2001; 114(Pt 18): 3219-31.
    • (2001) J Cell Sci , vol.114 , Issue.PART 18 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 48
    • 0035861856 scopus 로고    scopus 로고
    • Classification of PDZ domains
    • Bezprozvanny I, Maximov A. Classification of PDZ domains. FEBS Lett 2001; 509(3): 457-62.
    • (2001) FEBS Lett , vol.509 , Issue.3 , pp. 457-462
    • Bezprozvanny, I.1    Maximov, A.2
  • 50
    • 0032541057 scopus 로고    scopus 로고
    • The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule
    • Reczek D, Bretscher A. The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule. J Biol Chem 1998; 273(29): 18452-8.
    • (1998) J Biol Chem , vol.273 , Issue.29 , pp. 18452-18458
    • Reczek, D.1    Bretscher, A.2
  • 51
    • 0030608877 scopus 로고    scopus 로고
    • Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family
    • Reczek D, Berryman M, Bretscher A. Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J Cell Biol 1997; 139(1): 169-79.
    • (1997) J Cell Biol , vol.139 , Issue.1 , pp. 169-179
    • Reczek, D.1    Berryman, M.2    Bretscher, A.3
  • 52
    • 0032080043 scopus 로고    scopus 로고
    • Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR)
    • Wang S, Raab RW, Schatz PJ, Guggino WB, Li M. Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR). FEBS Lett 1998; 427(1): 103-8.
    • (1998) FEBS Lett , vol.427 , Issue.1 , pp. 103-108
    • Wang, S.1    Raab, R.W.2    Schatz, P.J.3    Guggino, W.B.4    Li, M.5
  • 53
    • 0034535348 scopus 로고    scopus 로고
    • Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF
    • Tang Y, Tang J, Chen Z, et al. Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF. J Biol Chem 2000; 275(48): 37559-64.
    • (2000) J Biol Chem , vol.275 , Issue.48 , pp. 37559-37564
    • Tang, Y.1    Tang, J.2    Chen, Z.3
  • 54
    • 77956247356 scopus 로고    scopus 로고
    • Na/H exchanger regulatory factors control PTH receptor signaling by facilitating differential activation of G{alpha} protein subunits
    • Wang B, Ardura JA, Romero G, Yang YS, Hall RA, Friedman PA. Na/H exchanger regulatory factors control PTH receptor signaling by facilitating differential activation of G{alpha} protein subunits. J Biol Chem 2010; 285: 26976-86.
    • (2010) J Biol Chem , vol.285 , pp. 26976-26986
    • Wang, B.1    Ardura, J.A.2    Romero, G.3    Yang, Y.S.4    Hall, R.A.5    Friedman, P.A.6
  • 55
    • 0029042451 scopus 로고
    • Further evidence for a novel receptor for amino-terminal parathyroid hormone-related protein on keratinocytes and squamous carcinoma cell lines
    • Orloff JJ, Kats Y, Urena P, et al. Further evidence for a novel receptor for amino-terminal parathyroid hormone-related protein on keratinocytes and squamous carcinoma cell lines. Endocrinology 1995; 136: 3016-23.
    • (1995) Endocrinology , vol.136 , pp. 3016-3023
    • Orloff, J.J.1    Kats, Y.2    Urena, P.3
  • 56
    • 0027502285 scopus 로고
    • Amino-terminal parathyroid hormone-related portein: Specific binding and cytosolic calcium responses in rat insulinoma cells
    • Gaich G, Orloff JJ, Atillasoy EJ, Burtis WJ, Ganz MB, Stewart AF. Amino-terminal parathyroid hormone-related portein: specific binding and cytosolic calcium responses in rat insulinoma cells. Endocrinology 1993; 132: 1402-9.
    • (1993) Endocrinology , vol.132 , pp. 1402-1409
    • Gaich, G.1    Orloff, J.J.2    Atillasoy, E.J.3    Burtis, W.J.4    Ganz, M.B.5    Stewart, A.F.6
  • 57
    • 0029029862 scopus 로고
    • Parathyroid hormone induces protein kinase C but not adenylate cyclase in adult cardiomyocytes and regulates cyclic AMP levels via protein kinase C-dependent phosphodiesterase activity
    • Schluter KD, Weber M, Piper HM. Parathyroid hormone induces protein kinase C but not adenylate cyclase in adult cardiomyocytes and regulates cyclic AMP levels via protein kinase C-dependent phosphodiesterase activity. Biochem J 1995; 310 (Pt 2): 439-44.
    • (1995) Biochem J , vol.310 , Issue.PART 2 , pp. 439-444
    • Schluter, K.D.1    Weber, M.2    Piper, H.M.3
  • 58
    • 0026509647 scopus 로고
    • Parathyroid hormone-related protein binding to human T-cell lymphotropic virus type I-infected lymphocytes
    • McCauley LK, Rosol TJ, Merryman JI, Capen CC. Parathyroid hormone-related protein binding to human T-cell lymphotropic virus type I-infected lymphocytes. Endocrinology 1992; 130(1): 300-6.
    • (1992) Endocrinology , vol.130 , Issue.1 , pp. 300-306
    • McCauley, L.K.1    Rosol, T.J.2    Merryman, J.I.3    Capen, C.C.4
  • 59
    • 0242384770 scopus 로고    scopus 로고
    • Activation-independent parathyroid hormone receptor internalization is regulated by NHERF1 (EBP50)
    • Sneddon WB, Syme CA, Bisello A, et al. Activation-independent parathyroid hormone receptor internalization is regulated by NHERF1 (EBP50). J Biol Chem 2003; 278(44): 43787-96.
    • (2003) J Biol Chem , vol.278 , Issue.44 , pp. 43787-43796
    • Sneddon, W.B.1    Syme, C.A.2    Bisello, A.3
  • 61
    • 37549002128 scopus 로고    scopus 로고
    • NHERF1 regulates parathyroid hormone receptor membrane retention without affecting recycling
    • Wang B, Bisello A, Yang Y, Romero GG, Friedman PA. NHERF1 regulates parathyroid hormone receptor membrane retention without affecting recycling. J Biol Chem 2007; 282(50): 36214-22.
    • (2007) J Biol Chem , vol.282 , Issue.50 , pp. 36214-36222
    • Wang, B.1    Bisello, A.2    Yang, Y.3    Romero, G.G.4    Friedman, P.A.5
  • 62
    • 43049089392 scopus 로고    scopus 로고
    • Regulation of parathyroid hormone type 1 receptor dynamics, traffic, and signaling by the Na+/H+ exchanger regulatory factor-1 in rat osteosarcoma ROS 17/2.8 cells
    • Wheeler D, Garrido JL, Bisello A, Kim YK, Friedman PA, Romero G. Regulation of parathyroid hormone type 1 receptor dynamics, traffic, and signaling by the Na+/H+ exchanger regulatory factor-1 in rat osteosarcoma ROS 17/2.8 cells. Mol Endocrinol 2008; 22(5): 1163-70.
    • (2008) Mol Endocrinol , vol.22 , Issue.5 , pp. 1163-1170
    • Wheeler, D.1    Garrido, J.L.2    Bisello, A.3    Kim, Y.K.4    Friedman, P.A.5    Romero, G.6
  • 63
    • 34548364156 scopus 로고    scopus 로고
    • NHERF-1 and the cytoskeleton regulate the traffic and membrane dynamics of G protein-coupled receptors
    • Wheeler D, Sneddon WB, Wang B, Friedman PA, Romero G. NHERF-1 and the cytoskeleton regulate the traffic and membrane dynamics of G protein-coupled receptors. J Biol Chem 2007; 282(34): 25076-87.
    • (2007) J Biol Chem , vol.282 , Issue.34 , pp. 25076-25087
    • Wheeler, D.1    Sneddon, W.B.2    Wang, B.3    Friedman, P.A.4    Romero, G.5
  • 64
    • 66149096210 scopus 로고    scopus 로고
    • NHERF1 regulates parathyroid hormone receptor desensitization: Interference with beta-arrestin binding
    • Wang B, Yang Y, Abou-Samra AB, Friedman PA. NHERF1 regulates parathyroid hormone receptor desensitization: interference with beta-arrestin binding. Mol Pharmacol 2009; 75(5): 1189-97.
    • (2009) Mol Pharmacol , vol.75 , Issue.5 , pp. 1189-1197
    • Wang, B.1    Yang, Y.2    Abou-Samra, A.B.3    Friedman, P.A.4
  • 65
    • 77956897685 scopus 로고    scopus 로고
    • Formation of a ternary complex between NHERF1, {beta}-arrestin, and parathyroid hormone receptor
    • Klenk C, Vetter T, Zurn A, et al. Formation of a ternary complex between NHERF1, {beta}-arrestin, and parathyroid hormone receptor. J Biol Chem 2010; 285: 30355-62.
    • (2010) J Biol Chem , vol.285 , pp. 30355-30362
    • Klenk, C.1    Vetter, T.2    Zurn, A.3
  • 66
    • 0034995853 scopus 로고    scopus 로고
    • Differential renal distribution of NHERF isoforms and their colocalization with NHE3, ezrin, and ROMK
    • Wade JB, Welling PA, Donowitz M, Shenolikar S, Weinman EJ. Differential renal distribution of NHERF isoforms and their colocalization with NHE3, ezrin, and ROMK. Am J Physiol Cell Physiol 2001; 280(1): C192-8.
    • (2001) Am J Physiol Cell Physiol , vol.280 , Issue.1
    • Wade, J.B.1    Welling, P.A.2    Donowitz, M.3    Shenolikar, S.4    Weinman, E.J.5
  • 67
    • 0032498963 scopus 로고    scopus 로고
    • The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange
    • Hall RA, Premont RT, Chow CW, et al. The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange. Nature 1998; 392(6676): 626-30.
    • (1998) Nature , vol.392 , Issue.6676 , pp. 626-630
    • Hall, R.A.1    Premont, R.T.2    Chow, C.W.3
  • 68
    • 0031026535 scopus 로고    scopus 로고
    • Cell-specific expression of the parathyroid hormone (PTH)PTH-related peptide receptor gene in kidney from kidney-specific and ubiquitous promotors
    • Amizuka N, Lee HS, Khan MY, et al. Cell-specific expression of the parathyroid hormone (PTH)PTH-related peptide receptor gene in kidney from kidney-specific and ubiquitous promotors. Endocrinology 1997; 138: 469-81.
    • (1997) Endocrinology , vol.138 , pp. 469-481
    • Amizuka, N.1    Lee, H.S.2    Khan, M.Y.3
  • 69
    • 0242665678 scopus 로고    scopus 로고
    • Calcium-sensing receptor regulation of PTH-inhibitable proximal tubule phosphate transport
    • Ba J, Brown D, Friedman PA. Calcium-sensing receptor regulation of PTH-inhibitable proximal tubule phosphate transport. Am J Physiol Renal Physiol 2003; 285(6): F1233-43.
    • (2003) Am J Physiol Renal Physiol , vol.285 , Issue.6
    • Ba, J.1    Brown, D.2    Friedman, P.A.3
  • 70
    • 33847043099 scopus 로고    scopus 로고
    • Defective coupling of apical PTH receptors to phospholipase C prevents internalization of the Na+-phosphate cotransporter NaPi-IIa in Nherf1-deficient mice
    • Capuano P, Bacic D, Roos M, et al. Defective coupling of apical PTH receptors to phospholipase C prevents internalization of the Na+-phosphate cotransporter NaPi-IIa in Nherf1-deficient mice. Am J Physiol Cell Physiol 2007; 292(2): C927-34.
    • (2007) Am J Physiol Cell Physiol , vol.292 , Issue.2
    • Capuano, P.1    Bacic, D.2    Roos, M.3
  • 71
    • 0034524664 scopus 로고    scopus 로고
    • ERM-Merlin and EBP50 protein families in plasma membrane organization and function
    • Bretscher A, Chambers D, Nguyen R, Reczek D. ERM-Merlin and EBP50 protein families in plasma membrane organization and function. Annu Rev Cell Dev Biol 2000; 16: 113-43.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 113-143
    • Bretscher, A.1    Chambers, D.2    Nguyen, R.3    Reczek, D.4
  • 72
    • 0032559637 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2
    • Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S. Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. J Cell Biol 1998; 140(4): 885-95.
    • (1998) J Cell Biol , vol.140 , Issue.4 , pp. 885-895
    • Yonemura, S.1    Hirao, M.2    Doi, Y.3    Takahashi, N.4    Kondo, T.5    Tsukita, S.6
  • 73
    • 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, et al. The NHE3 juxtamembrane cytoplasmic domain directly binds ezrin: dual role in NHE3 trafficking and mobility in the brush border. Mol Biol Cell 2006; 17(6): 2661-73.
    • (2006) Mol Biol Cell , vol.17 , Issue.6 , pp. 2661-2673
    • Cha, B.1    Tse, M.2    Yun, C.3
  • 74
    • 70349779413 scopus 로고    scopus 로고
    • The parathyroid hormone 1 receptor directly binds to the FERM domain of ezrin, an interaction that supports apical receptor localization and signaling in LLC-PK1 cells
    • Mahon MJ. The parathyroid hormone 1 receptor directly binds to the FERM domain of ezrin, an interaction that supports apical receptor localization and signaling in LLC-PK1 cells. Mol Endocrinol 2009; 23(10): 1691-701.
    • (2009) Mol Endocrinol , vol.23 , Issue.10 , pp. 1691-1701
    • Mahon, M.J.1
  • 75
    • 23944521772 scopus 로고    scopus 로고
    • Regulation of phosphorus homeostasis by the type IIa Na/phosphate cotransporter
    • Tenenhouse H. Regulation of phosphorus homeostasis by the type IIa Na/phosphate cotransporter. Annu Rev Nutr 2005; 25: 197-214.
    • (2005) Annu Rev Nutr , vol.25 , pp. 197-214
    • Tenenhouse, H.1
  • 77
    • 0037015060 scopus 로고    scopus 로고
    • PDZ-domain interactions and apical expression of type IIa Na/P(i) cotransporters
    • Hernando N, Deliot N, Gisler SM, et al. PDZ-domain interactions and apical expression of type IIa Na/P(i) cotransporters. Proc Natl Acad Sci U S A 2002; 99(18): 11957-62.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.18 , pp. 11957-11962
    • Hernando, N.1    Deliot, N.2    Gisler, S.M.3
  • 78
    • 0037143761 scopus 로고    scopus 로고
    • Targeted disruption of the mouse NHERF-1 gene promotes internalization of proximal tubule sodium-phosphate cotransporter type IIa and renal phosphate wasting
    • Shenolikar S, Voltz JW, Minkoff CM, Wade JB, Weinman EJ. Targeted disruption of the mouse NHERF-1 gene promotes internalization of proximal tubule sodium-phosphate cotransporter type IIa and renal phosphate wasting. Proc Natl Acad Sci U S A 2002; 99(17): 11470-5.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.17 , pp. 11470-11475
    • Shenolikar, S.1    Voltz, J.W.2    Minkoff, C.M.3    Wade, J.B.4    Weinman, E.J.5
  • 79
    • 41149086133 scopus 로고    scopus 로고
    • Ezrin promotes functional expression and parathyroid hormone-mediated regulation of the sodium-phosphate cotransporter 2a in LLC-PK1 cells
    • Mahon MJ. Ezrin promotes functional expression and parathyroid hormone-mediated regulation of the sodium-phosphate cotransporter 2a in LLC-PK1 cells. Am J Physiol Renal Physiol 2008; 294(3): F667-75.
    • (2008) Am J Physiol Renal Physiol , vol.294 , Issue.3
    • Mahon, M.J.1
  • 80
    • 0024563170 scopus 로고
    • Clonal sublines that are morphologically and functionally distinct from parental OK cells
    • Cole JA, Forte LR, Krause WJ, Thorne PK. Clonal sublines that are morphologically and functionally distinct from parental OK cells. Am J Physiol 1989; 256(4 Pt 2): F672-9.
    • (1989) Am J Physiol , vol.256 , Issue.4 PART 2
    • Cole, J.A.1    Forte, L.R.2    Krause, W.J.3    Thorne, P.K.4
  • 81
    • 0242330281 scopus 로고    scopus 로고
    • Na+/H+ exchangerregulatory factor 1 mediates inhibition of phosphate transport by parathyroid hormone and second messengers by acting at multiple sites in opossum kidney cells
    • Mahon MJ, Cole JA, Lederer ED, Segre GV. Na+/H+ exchangerregulatory factor 1 mediates inhibition of phosphate transport by parathyroid hormone and second messengers by acting at multiple sites in opossum kidney cells. Mol Endocrinol 2003; 17(11): 2355-64.
    • (2003) Mol Endocrinol , vol.17 , Issue.11 , pp. 2355-2364
    • Mahon, M.J.1    Cole, J.A.2    Lederer, E.D.3    Segre, G.V.4
  • 82
    • 33749449769 scopus 로고    scopus 로고
    • Adenoviral expression of NHERF-1 in NHERF-1 null mouse renal proximal tubule cells restores Npt2a regulation by low phosphate media and parathyroid hormone
    • Cunningham R, Steplock D, E X, et al. Adenoviral expression of NHERF-1 in NHERF-1 null mouse renal proximal tubule cells restores Npt2a regulation by low phosphate media and parathyroid hormone. Am J Physiol Renal Physiol 2006; 291(4): F896-901.
    • (2006) Am J Physiol Renal Physiol , vol.291 , Issue.4
    • Cunningham, R.1    Steplock, D.E.X.2
  • 83
    • 36048958880 scopus 로고    scopus 로고
    • Parathyroid hormone inhibits renal phosphate transport by phosphorylation of serine 77 of sodium-hydrogen exchanger regulatory factor-1
    • Weinman EJ, Biswas RS, Peng Q, et al. Parathyroid hormone inhibits renal phosphate transport by phosphorylation of serine 77 of sodium-hydrogen exchanger regulatory factor-1. J Clin Invest 2007; 117(11): 3412-20.
    • (2007) J Clin Invest , vol.117 , Issue.11 , pp. 3412-3420
    • Weinman, E.J.1    Biswas, R.S.2    Peng, Q.3
  • 84
    • 73449096477 scopus 로고    scopus 로고
    • PTH-induced internalization of apical membrane NaPi2a: Role of actin and myosin VI
    • Blaine J, Okamura K, Giral H, et al. PTH-induced internalization of apical membrane NaPi2a: role of actin and myosin VI. Am J Physiol Cell Physiol 2009; 297(6): C1339-46.
    • (2009) Am J Physiol Cell Physiol , vol.297 , Issue.6
    • Blaine, J.1    Okamura, K.2    Giral, H.3
  • 85
    • 0026069186 scopus 로고
    • Parathyroid hormone promotes the disassembly of cytoskeletal actin and myosin in cultured osteoblastic cells: Mediation by cyclic AMP
    • Egan JJ, Gronowicz G, Rodan GA. Parathyroid hormone promotes the disassembly of cytoskeletal actin and myosin in cultured osteoblastic cells: mediation by cyclic AMP. J Cell Biochem 1991; 45(1): 101-11.
    • (1991) J Cell Biochem , vol.45 , Issue.1 , pp. 101-111
    • Egan, J.J.1    Gronowicz, G.2    Rodan, G.A.3
  • 86
    • 0031033178 scopus 로고    scopus 로고
    • Ezrin is a cyclic AMPdependent protein kinase anchoring protein
    • Dransfield DT, Bradford AJ, Smith J, et al. Ezrin is a cyclic AMPdependent protein kinase anchoring protein. Embo J 1997; 16(1): 35-43.
    • (1997) Embo J , vol.16 , Issue.1 , pp. 35-43
    • Dransfield, D.T.1    Bradford, A.J.2    Smith, J.3
  • 87
    • 0142122528 scopus 로고    scopus 로고
    • PTH/PTH-related protein receptor interacts directly with Tctex-1 through its COOH terminus
    • Sugai M, Saito M, Sukegawa I, et al. PTH/PTH-related protein receptor interacts directly with Tctex-1 through its COOH terminus. Biochem Biophys Res Commun 2003; 311(1): 24-31.
    • (2003) Biochem Biophys Res Commun , vol.311 , Issue.1 , pp. 24-31
    • Sugai, M.1    Saito, M.2    Sukegawa, I.3
  • 88
    • 0036171544 scopus 로고    scopus 로고
    • Motor-cargo interactions: The key to transport specificity
    • Karcher RL, Deacon SW, Gelfand VI. Motor-cargo interactions: the key to transport specificity. Trends Cell Biol 2002; 12(1): 21-7.
    • (2002) Trends Cell Biol , vol.12 , Issue.1 , pp. 21-27
    • Karcher, R.L.1    Deacon, S.W.2    Gelfand, V.I.3
  • 89
    • 0033603239 scopus 로고    scopus 로고
    • Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1
    • Tai AW, Chuang JZ, Bode C, Wolfrum U, Sung CH. Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1. Cell 1999; 97(7): 877-87.
    • (1999) Cell , vol.97 , Issue.7 , pp. 877-887
    • Tai, A.W.1    Chuang, J.Z.2    Bode, C.3    Wolfrum, U.4    Sung, C.H.5
  • 90
    • 0026344220 scopus 로고
    • Heterogeneous localization of G protein alpha-subunits in rat kidney
    • Stow JL, Sabolic I, Brown D. Heterogeneous localization of G protein alpha-subunits in rat kidney. Am J Physiol 1991; 261(5 Pt 2): F831-40.
    • (1991) Am J Physiol , vol.261 , Issue.5 PART 2
    • Stow, J.L.1    Sabolic, I.2    Brown, D.3
  • 91
    • 0037332392 scopus 로고    scopus 로고
    • Galpha12-and Galpha13-protein subunit linkage of D5 dopamine receptors in the nephron
    • Zheng S, Yu P, Zeng C, et al. Galpha12-and Galpha13-protein subunit linkage of D5 dopamine receptors in the nephron. Hypertension 2003; 41(3): 604-10.
    • (2003) Hypertension , vol.41 , Issue.3 , pp. 604-610
    • Zheng, S.1    Yu, P.2    Zeng, C.3
  • 92
    • 0031759430 scopus 로고    scopus 로고
    • Immunolocalization of phospholipase C isoforms in rat kidney
    • Lea JP, Ertoy D, Hollis JL, Marrero MB, Sands JM. Immunolocalization of phospholipase C isoforms in rat kidney. Kidney Int 1998; 54(5): 1484-90.
    • (1998) Kidney Int , vol.54 , Issue.5 , pp. 1484-1490
    • Lea, J.P.1    Ertoy, D.2    Hollis, J.L.3    Marrero, M.B.4    Sands, J.M.5
  • 93
    • 0016024619 scopus 로고
    • Ultrastructural cytochemical localization of adenylate cyclase in the rat nephron
    • Sato T, Garcia-Bunuel R, Brandes D. Ultrastructural cytochemical localization of adenylate cyclase in the rat nephron. Lab Invest 1974; 30(2): 222-9.
    • (1974) Lab Invest , vol.30 , Issue.2 , pp. 222-229
    • Sato, T.1    Garcia-Bunuel, R.2    Brandes, D.3
  • 94
    • 0000683821 scopus 로고
    • Studies of calcium and phosphorus metabolism: V. A study of the bone trabeculae as a readily available reserve supply of calcium
    • Bauer W, Aub JC, Albright F. Studies of calcium and phosphorus metabolism: V. A study of the bone trabeculae as a readily available reserve supply of calcium. J Exp Med 1929; 49(1): 145-62.
    • (1929) J Exp Med , vol.49 , Issue.1 , pp. 145-162
    • Bauer, W.1    Aub, J.C.2    Albright, F.3
  • 95
    • 0019815677 scopus 로고
    • Short-term effects of synthetic human parathyroid hormone-(1--34) administration on bone mineral metabolism in osteoporotic patients
    • Slovik DM, Neer RM, Potts JT, Jr. Short-term effects of synthetic human parathyroid hormone-(1--34) administration on bone mineral metabolism in osteoporotic patients. J Clin Invest 1981; 68(5): 1261-71.
    • (1981) J Clin Invest , vol.68 , Issue.5 , pp. 1261-1271
    • Slovik, D.M.1    Neer, R.M.2    Potts Jr., J.T.3
  • 96
    • 0035837553 scopus 로고    scopus 로고
    • Effect of parathyroid hormone (1-34) on fractures and bone mineral density in postmenopausal women with osteoporosis
    • Neer RM, Arnaud CD, Zanchetta JR, et al. Effect of parathyroid hormone (1-34) on fractures and bone mineral density in postmenopausal women with osteoporosis. N Engl J Med 2001; 344(19): 1434-41.
    • (2001) N Engl J Med , vol.344 , Issue.19 , pp. 1434-1441
    • Neer, R.M.1    Arnaud, C.D.2    Zanchetta, J.R.3
  • 97
    • 57749189593 scopus 로고    scopus 로고
    • Teriparatide: A review of its use in osteoporosis
    • Blick SK, Dhillon S, Keam SJ. Teriparatide: a review of its use in osteoporosis. Drugs 2008; 68(18): 2709-37.
    • (2008) Drugs , vol.68 , Issue.18 , pp. 2709-2737
    • Blick, S.K.1    Dhillon, S.2    Keam, S.J.3
  • 98
    • 0242268524 scopus 로고    scopus 로고
    • Osteoblastic cells regulate the haematopoietic stem cell niche
    • Calvi LM, Adams GB, Weibrecht KW, et al. Osteoblastic cells regulate the haematopoietic stem cell niche. Nature 2003; 425(6960): 841-6.
    • (2003) Nature , vol.425 , Issue.6960 , pp. 841-846
    • Calvi, L.M.1    Adams, G.B.2    Weibrecht, K.W.3
  • 99
    • 33846869023 scopus 로고    scopus 로고
    • Therapeutic targeting of a stem cell niche
    • Adams GB, Martin RP, Alley IR, et al. Therapeutic targeting of a stem cell niche. Nat Biotechnol 2007; 25(2): 238-43.
    • (2007) Nat Biotechnol , vol.25 , Issue.2 , pp. 238-243
    • Adams, G.B.1    Martin, R.P.2    Alley, I.R.3
  • 100
    • 34250203595 scopus 로고    scopus 로고
    • Phase I trial of parathyroid hormone to facilitate stem cell mobilization
    • Ballen KK, Shpall EJ, Avigan D, et al. Phase I trial of parathyroid hormone to facilitate stem cell mobilization. Biol Blood Marrow Transplant 2007; 13(7): 838-43.
    • (2007) Biol Blood Marrow Transplant , vol.13 , Issue.7 , pp. 838-843
    • Ballen, K.K.1    Shpall, E.J.2    Avigan, D.3
  • 101
    • 34249280604 scopus 로고    scopus 로고
    • Targeting the stem cell niche: Squeezing blood from bones
    • Ballen K. Targeting the stem cell niche: squeezing blood from bones. Bone Marrow Transplant 2007; 39(11): 655-60.
    • (2007) Bone Marrow Transplant , vol.39 , Issue.11 , pp. 655-660
    • Ballen, K.1
  • 102
    • 38049086228 scopus 로고    scopus 로고
    • Altered selectivity of parathyroid hormone (PTH) and PTH-related protein (PTHrP) for distinct conformations of the PTH/PTHrP receptor
    • Dean T, Vilardaga JP, Potts JT, Jr., Gardella TJ. Altered selectivity of parathyroid hormone (PTH) and PTH-related protein (PTHrP) for distinct conformations of the PTH/PTHrP receptor. Mol Endocrinol 2008; 22(1): 156-66.
    • (2008) Mol Endocrinol , vol.22 , Issue.1 , pp. 156-166
    • Dean, T.1    Vilardaga, J.P.2    Potts Jr., J.T.3    Gardella, T.J.4
  • 103
    • 36549086789 scopus 로고    scopus 로고
    • Progress, paradox, and potential: Parathyroid hormone research over five decades
    • Potts JT, Gardella TJ. Progress, paradox, and potential: parathyroid hormone research over five decades. Ann N Y Acad Sci 2007; 1117: 196-208.
    • (2007) Ann N Y Acad Sci , vol.1117 , pp. 196-208
    • Potts, J.T.1    Gardella, T.J.2
  • 104
    • 55949089800 scopus 로고    scopus 로고
    • Prolonged signaling at the parathyroid hormone receptor by peptide ligands targeted to a specific receptor conformation
    • Okazaki M, Ferrandon S, Vilardaga JP, Bouxsein ML, Potts JT Jr., Gardella TJ. Prolonged signaling at the parathyroid hormone receptor by peptide ligands targeted to a specific receptor conformation. Proc Natl Acad Sci U S A 2008; 105(43): 16525-30.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.43 , pp. 16525-16530
    • Okazaki, M.1    Ferrandon, S.2    Vilardaga, J.P.3    Bouxsein, M.L.4    Potts Jr., J.T.5    Gardella, T.J.6
  • 105
    • 0033550046 scopus 로고    scopus 로고
    • Amino-terminal modifications of human parathyroid hormone (PTH) selectively alter phospholipase C signaling via the type 1 PTH receptor: Implications for design of signal-specific PTH ligands
    • Takasu H, Gardella TJ, Luck MD, Potts JT, Jr., Bringhurst FR. Amino-terminal modifications of human parathyroid hormone (PTH) selectively alter phospholipase C signaling via the type 1 PTH receptor: implications for design of signal-specific PTH ligands. Biochemistry 1999; 38(41): 13453-60.
    • (1999) Biochemistry , vol.38 , Issue.41 , pp. 13453-13460
    • Takasu, H.1    Gardella, T.J.2    Luck, M.D.3    Potts Jr., J.T.4    Bringhurst, F.R.5
  • 106
    • 0037064132 scopus 로고    scopus 로고
    • Selective ligand-induced stabilization of active and desensitized parathyroid hormone type 1 receptor conformations
    • Bisello A, Chorev M, Rosenblatt M, Monticelli L, Mierke DF, Ferrari SL. Selective ligand-induced stabilization of active and desensitized parathyroid hormone type 1 receptor conformations. J Biol Chem 2002; 277(41): 38524-30.
    • (2002) J Biol Chem , vol.277 , Issue.41 , pp. 38524-38530
    • Bisello, A.1    Chorev, M.2    Rosenblatt, M.3    Monticelli, L.4    Mierke, D.F.5    Ferrari, S.L.6
  • 107
    • 73949084919 scopus 로고    scopus 로고
    • A beta-arrestin-biased agonist of the parathyroid hormone receptor (PTH1R) promotes bone formation independent of G protein activation
    • Gesty-Palmer D, Flannery P, Yuan L, et al. A beta-arrestin-biased agonist of the parathyroid hormone receptor (PTH1R) promotes bone formation independent of G protein activation. Sci Transl Med 2009; 1(1): 1ra1.
    • (2009) Sci Transl Med , vol.1 , Issue.1
    • Gesty-Palmer, D.1    Flannery, P.2    Yuan, L.3
  • 108
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin MR, Wells JA. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov 2004; 3(4): 301-17.
    • (2004) Nat Rev Drug Discov , vol.3 , Issue.4 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 109
    • 33846061735 scopus 로고    scopus 로고
    • Rational design of a nonpeptide general chemical scaffold for reversible inhibition of PDZ domain interactions
    • Fujii N, Haresco JJ, Novak KA, et al. Rational design of a nonpeptide general chemical scaffold for reversible inhibition of PDZ domain interactions. Bioorg Med Chem Lett 2007; 17(2): 549-52.
    • (2007) Bioorg Med Chem Lett , vol.17 , Issue.2 , pp. 549-552
    • Fujii, N.1    Haresco, J.J.2    Novak, K.A.3
  • 110
    • 0141958040 scopus 로고    scopus 로고
    • A selective irreversible inhibitor targeting a PDZ protein interaction domain
    • Fujii N, Haresco JJ, Novak KA, Stokoe D, Kuntz ID, Guy RK. A selective irreversible inhibitor targeting a PDZ protein interaction domain. J Am Chem Soc 2003; 125(40): 12074-5.
    • (2003) J Am Chem Soc , vol.125 , Issue.40 , pp. 12074-12075
    • Fujii, N.1    Haresco, J.J.2    Novak, K.A.3    Stokoe, D.4    Kuntz, I.D.5    Guy, R.K.6
  • 111
    • 76249119763 scopus 로고    scopus 로고
    • Identification of a smallmolecule inhibitor of the PICK1 PDZ domain that inhibits hippocampal LTP and LTD
    • Thorsen TS, Madsen KL, Rebola N, et al. Identification of a smallmolecule inhibitor of the PICK1 PDZ domain that inhibits hippocampal LTP and LTD. Proc Natl Acad Sci USA 2010; 107(1): 413-8.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.1 , pp. 413-418
    • Thorsen, T.S.1    Madsen, K.L.2    Rebola, N.3
  • 112
    • 79953164965 scopus 로고    scopus 로고
    • Functional regulation of CFTR-containing macromolecular complexes: A small-molecule inhibitor approach
    • Zhang W, Penmatsa H, Ren A, et al. Functional regulation of CFTR-containing macromolecular complexes: a small-molecule inhibitor approach. Biochem J 2011; 435(2): 451-62.
    • (2011) Biochem J , vol.435 , Issue.2 , pp. 451-462
    • Zhang, W.1    Penmatsa, H.2    Ren, A.3


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