메뉴 건너뛰기




Volumn 2, Issue 5, 2007, Pages

Retraction: The Role for HNF-1β-Targeted Collectrin in Maintenance of Primary Cilia and Cell Polarity in Collecting Duct Cells (PLoS ONE (2007) 2:5 (e414) DOI: 10.1371/journal.pone.0000414);The role for HNF-1β-targeted collectrin in maintenance of primary cilia and cell polarity in collecting duct cells

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ANGIOTENSIN CONVERTING ENZYME 2; COLLECTRIN; GAMMA ACTIN; HEPATOCYTE NUCLEAR FACTOR 1BETA; MESSENGER RNA; MYOSIN II; MYOSIN IIA; POLYCYSTIN 2; POLYCYSTIN 2 POLARIS COMPLEX; SNARE PROTEIN; UNCLASSIFIED DRUG; MEMBRANE PROTEIN; PRIMER DNA; SMALL INTERFERING RNA; TMEM27 PROTEIN, MOUSE;

EID: 34547859121     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0286174     Document Type: Erratum
Times cited : (47)

References (52)
  • 1
    • 0032782374 scopus 로고    scopus 로고
    • Screening for genes up-regulated in 5/6 nephrectomized mouse kidney
    • Zhang H, Wada J, Kanwar YS, Tsuchiyama Y, Hiragushi K, et al. (1999) Screening for genes up-regulated in 5/6 nephrectomized mouse kidney. Kidney Int 56: 549-558.
    • (1999) Kidney Int , vol.56 , pp. 549-558
    • Zhang, H.1    Wada, J.2    Kanwar, Y.S.3    Tsuchiyama, Y.4    Hiragushi, K.5
  • 2
    • 0035907347 scopus 로고    scopus 로고
    • Collectrin, a collecting duct-specific transmembrane glycoprotein, is a novel homolog of ACE2 and is developmentally regulated in embryonic kidneys
    • Zhang H, Wada J, Hida K, Tsuchiyama Y, Hiragushi K, et al. (2001) Collectrin, a collecting duct-specific transmembrane glycoprotein, is a novel homolog of ACE2 and is developmentally regulated in embryonic kidneys. J Biol Chem 276: 17132-17139.
    • (2001) J Biol Chem , vol.276 , pp. 17132-17139
    • Zhang, H.1    Wada, J.2    Hida, K.3    Tsuchiyama, Y.4    Hiragushi, K.5
  • 3
    • 33845864984 scopus 로고    scopus 로고
    • Essential role for collectrin in renal amino acid transport
    • Danilczyk U, Sarao R, Remy C, Benabbas C, Stange G, et al. (2006) Essential role for collectrin in renal amino acid transport. Nature 444: 1088-1091.
    • (2006) Nature , vol.444 , pp. 1088-1091
    • Danilczyk, U.1    Sarao, R.2    Remy, C.3    Benabbas, C.4    Stange, G.5
  • 5
    • 33644875891 scopus 로고    scopus 로고
    • Tmem27: A cleaved and shed plasma membrane protein that stimulates pancreatic beta cell proliferation
    • Akpinar P, Kuwajima S, Krutzfeldt J, Stoffel M (2005) Tmem27: a cleaved and shed plasma membrane protein that stimulates pancreatic beta cell proliferation. Cell Metab 2: 385-397.
    • (2005) Cell Metab , vol.2 , pp. 385-397
    • Akpinar, P.1    Kuwajima, S.2    Krutzfeldt, J.3    Stoffel, M.4
  • 6
    • 33644878503 scopus 로고    scopus 로고
    • The HNF-1 target collectrin controls insulin excytosis by SNARE complex formation
    • Fukui K, Yang Q, Cao Y, Takahashi N, Hatakeyama H, et al. (2005) The HNF-1 target collectrin controls insulin excytosis by SNARE complex formation. Cell Metab 2: 373-384.
    • (2005) Cell Metab , vol.2 , pp. 373-384
    • Fukui, K.1    Yang, Q.2    Cao, Y.3    Takahashi, N.4    Hatakeyama, H.5
  • 7
    • 0030031453 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor 1 inactivation results in hepatic dysfunction, phenylketonuria, and renal Fanconi syndrome
    • Pontoglio M, Barra J, Hadchouel M, Doyen A, Kress C, et al. (1996) Hepatocyte nuclear factor 1 inactivation results in hepatic dysfunction, phenylketonuria, and renal Fanconi syndrome. Cell 84: 575-585.
    • (1996) Cell , vol.84 , pp. 575-585
    • Pontoglio, M.1    Barra, J.2    Hadchouel, M.3    Doyen, A.4    Kress, C.5
  • 8
    • 2342508500 scopus 로고    scopus 로고
    • A transcriptional network in polycystic kidney disease
    • Gresh L, Fischer E, Reimann A, Tanguy M, Garbay S, et al. (2004) A transcriptional network in polycystic kidney disease. Embo J 23: 1657-1668.
    • (2004) Embo J , vol.23 , pp. 1657-1668
    • Gresh, L.1    Fischer, E.2    Reimann, A.3    Tanguy, M.4    Garbay, S.5
  • 9
    • 0031453186 scopus 로고    scopus 로고
    • Mutation in hepatocyte nuclear factor-1 beta gene (TCF2) associated with MODY
    • Horikawa Y, Iwasaki N, Hara M, Furuta H, Hinokio Y, et al. (1997) Mutation in hepatocyte nuclear factor-1 beta gene (TCF2) associated with MODY. Nat Genet 17: 384-385.
    • (1997) Nat Genet , vol.17 , pp. 384-385
    • Horikawa, Y.1    Iwasaki, N.2    Hara, M.3    Furuta, H.4    Hinokio, Y.5
  • 10
    • 33644878503 scopus 로고    scopus 로고
    • The HNF-1 target collectrin controls insulin exocytosis by SNARE complex formation
    • Fukui K, Yang Q, Cao Y, Takahashi N, Hatakeyama H, et al. (2005) The HNF-1 target collectrin controls insulin exocytosis by SNARE complex formation. Cell Metab 2: 373-384.
    • (2005) Cell Metab , vol.2 , pp. 373-384
    • Fukui, K.1    Yang, Q.2    Cao, Y.3    Takahashi, N.4    Hatakeyama, H.5
  • 11
    • 2142659368 scopus 로고    scopus 로고
    • Mutation of hepatocyte nuclear factor-1beta inhibits Pkhd1 gene expression and produces renal cysts in mice
    • Hiesberger T, Bai Y, Shao X, McNally BT, Sinclair AM, et al. (2004) Mutation of hepatocyte nuclear factor-1beta inhibits Pkhd1 gene expression and produces renal cysts in mice. J Clin Invest 113: 814-825.
    • (2004) J Clin Invest , vol.113 , pp. 814-825
    • Hiesberger, T.1    Bai, Y.2    Shao, X.3    McNally, B.T.4    Sinclair, A.M.5
  • 12
    • 15444375084 scopus 로고    scopus 로고
    • Role of the hepatocyte nuclear factor-1beta (HNF-1beta) C-terminal domain in Pkhd1 (ARPKD) gene transcription and renal cystogenesis
    • Hiesberger T, Shao X, Gourley E, Reimann A, Pontoglio M, et al. (2005) Role of the hepatocyte nuclear factor-1beta (HNF-1beta) C-terminal domain in Pkhd1 (ARPKD) gene transcription and renal cystogenesis. J Biol Chem 280: 10578-10586.
    • (2005) J Biol Chem , vol.280 , pp. 10578-10586
    • Hiesberger, T.1    Shao, X.2    Gourley, E.3    Reimann, A.4    Pontoglio, M.5
  • 14
    • 0029813157 scopus 로고    scopus 로고
    • Syntaxin-4 is localized to the apical plasma membrane of rat renal collecting duct cells: Possible role in aquaporin-2 trafficking
    • Mandon B, Chou CL, Nielsen S, Knepper MA (1996) Syntaxin-4 is localized to the apical plasma membrane of rat renal collecting duct cells: possible role in aquaporin-2 trafficking. J Clin Invest 98: 906-913.
    • (1996) J Clin Invest , vol.98 , pp. 906-913
    • Mandon, B.1    Chou, C.L.2    Nielsen, S.3    Knepper, M.A.4
  • 15
    • 20244369880 scopus 로고    scopus 로고
    • Identification of adipocyte adhesion molecule (ACAM), a novel CTX gene family, implicated in adipocyte maturation and development of obesity
    • Eguchi J, Wada J, Hida K, Zhang H, Matsuoka T, et al. (2005) Identification of adipocyte adhesion molecule (ACAM), a novel CTX gene family, implicated in adipocyte maturation and development of obesity. Biochem J 387: 343-353.
    • (2005) Biochem J , vol.387 , pp. 343-353
    • Eguchi, J.1    Wada, J.2    Hida, K.3    Zhang, H.4    Matsuoka, T.5
  • 16
    • 0031940158 scopus 로고    scopus 로고
    • Characterization of mammalian translocase of inner mitochondrial membrane (Tim44) isolated from diabetic newborn mouse kidney
    • Wada J, Kanwar YS (1998) Characterization of mammalian translocase of inner mitochondrial membrane (Tim44) isolated from diabetic newborn mouse kidney. Proc Natl Acad Sci U S A 95: 144-149.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 144-149
    • Wada, J.1    Kanwar, Y.S.2
  • 17
    • 0029865283 scopus 로고    scopus 로고
    • Cloning of mouse integrin alphaV cDNA and role of the alphaV-related matrix receptors in metanephric development
    • Wada J, Kumar A, Liu Z, Ruoslahti E, Reichardt L, et al. (1996) Cloning of mouse integrin alphaV cDNA and role of the alphaV-related matrix receptors in metanephric development. J Cell Biol 132: 1161-1176.
    • (1996) J Cell Biol , vol.132 , pp. 1161-1176
    • Wada, J.1    Kumar, A.2    Liu, Z.3    Ruoslahti, E.4    Reichardt, L.5
  • 18
    • 0347357836 scopus 로고    scopus 로고
    • Polycystic kidney disease
    • Wilson PD (2004) Polycystic kidney disease. N Engl J Med 350: 151-164.
    • (2004) N Engl J Med , vol.350 , pp. 151-164
    • Wilson, P.D.1
  • 19
    • 14044266355 scopus 로고    scopus 로고
    • Abnormal EGF-dependent regulation of sodium absorption in ARPKD collecting duct cells
    • Veizis IE, Cotton CU (2005) Abnormal EGF-dependent regulation of sodium absorption in ARPKD collecting duct cells. Am J Physiol Renal Physiol 288: F474-482.
    • (2005) Am J Physiol Renal Physiol , vol.288
    • Veizis, I.E.1    Cotton, C.U.2
  • 20
    • 0037334326 scopus 로고    scopus 로고
    • Polycystic kidney disease-the ciliary connection
    • Ong AC, Wheatley DN (2003) Polycystic kidney disease-the ciliary connection. Lancet 361: 774-776.
    • (2003) Lancet , vol.361 , pp. 774-776
    • Ong, A.C.1    Wheatley, D.N.2
  • 21
    • 4544287005 scopus 로고    scopus 로고
    • Cystic kidney diseases: All roads lead to the cilium
    • Zhang Q, Taulman PD, Yoder BK (2004) Cystic kidney diseases: all roads lead to the cilium. Physiology (Bethesda) 19: 225-230.
    • (2004) Physiology (Bethesda) , vol.19 , pp. 225-230
    • Zhang, Q.1    Taulman, P.D.2    Yoder, B.K.3
  • 22
    • 0029586470 scopus 로고
    • Primary cilia in normal and pathological tissues
    • Wheatley DN (1995) Primary cilia in normal and pathological tissues. Pathobiology 63: 222-238.
    • (1995) Pathobiology , vol.63 , pp. 222-238
    • Wheatley, D.N.1
  • 23
    • 0028322016 scopus 로고
    • Candidate gene associated with a mutation causing recessive polycystic kidney disease in mice
    • Moyer JH, Lee-Tischler MJ, Kwon HY, Schrick JJ, Avner ED, et al. (1994) Candidate gene associated with a mutation causing recessive polycystic kidney disease in mice. Science 264: 1329-1333.
    • (1994) Science , vol.264 , pp. 1329-1333
    • Moyer, J.H.1    Lee-Tischler, M.J.2    Kwon, H.Y.3    Schrick, J.J.4    Avner, E.D.5
  • 24
    • 0035159015 scopus 로고    scopus 로고
    • Polaris, a protein involved in left-right axis patterning, localizes to basal bodies and cilia
    • Taulman PD, Haycraft CJ, Balkovetz DF, Yoder BK (2001) Polaris, a protein involved in left-right axis patterning, localizes to basal bodies and cilia. Mol Biol Cell 12: 589-599.
    • (2001) Mol Biol Cell , vol.12 , pp. 589-599
    • Taulman, P.D.1    Haycraft, C.J.2    Balkovetz, D.F.3    Yoder, B.K.4
  • 25
    • 0034735526 scopus 로고    scopus 로고
    • Chlamydomonas IFT88 and its mouse homologue, polycystic kidney disease gene tg737, are required for assembly of cilia and flagella
    • Pazour GJ, Dickert BL, Vucica Y, Seeley ES, Rosenbaum JL, et al. (2000) Chlamydomonas IFT88 and its mouse homologue, polycystic kidney disease gene tg737, are required for assembly of cilia and flagella. J Cell Biol 151: 709-718.
    • (2000) J Cell Biol , vol.151 , pp. 709-718
    • Pazour, G.J.1    Dickert, B.L.2    Vucica, Y.3    Seeley, E.S.4    Rosenbaum, J.L.5
  • 26
    • 0032504963 scopus 로고    scopus 로고
    • Cloning of inv, a gene that controls left/right asymmetry and kidney development
    • Mochizuki T, Saijoh Y, Tsuchiya K, Shirayoshi Y, Takai S, et al. (1998) Cloning of inv, a gene that controls left/right asymmetry and kidney development. Nature 395: 177-181.
    • (1998) Nature , vol.395 , pp. 177-181
    • Mochizuki, T.1    Saijoh, Y.2    Tsuchiya, K.3    Shirayoshi, Y.4    Takai, S.5
  • 27
    • 0036177603 scopus 로고    scopus 로고
    • Cystin, a novel cilia-associated protein, is disrupted in the cpk mouse model of polycystic kidney disease
    • Hou X, Mrug M, Yoder BK, Lefkowitz EJ, Kremmidiotis G, et al. (2002) Cystin, a novel cilia-associated protein, is disrupted in the cpk mouse model of polycystic kidney disease. J Clin Invest 109: 533-540.
    • (2002) J Clin Invest , vol.109 , pp. 533-540
    • Hou, X.1    Mrug, M.2    Yoder, B.K.3    Lefkowitz, E.J.4    Kremmidiotis, G.5
  • 28
    • 0036785149 scopus 로고    scopus 로고
    • The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia
    • Yoder BK, Hou X, Guay-Woodford LM (2002) The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia. J Am Soc Nephrol 13: 2508-2516.
    • (2002) J Am Soc Nephrol , vol.13 , pp. 2508-2516
    • Yoder, B.K.1    Hou, X.2    Guay-Woodford, L.M.3
  • 29
    • 2942625562 scopus 로고    scopus 로고
    • Bardet-Biedl syndrome type 4 (BBS4)-null mice implicate Bbs4 in flagella formation but not global cilia assembly
    • Mykytyn K, Mullins RF, Andrews M, Chiang AP, Swiderski RE, et al. (2004) Bardet-Biedl syndrome type 4 (BBS4)-null mice implicate Bbs4 in flagella formation but not global cilia assembly. Proc Natl Acad Sci U S A 101: 8664-8669.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8664-8669
    • Mykytyn, K.1    Mullins, R.F.2    Andrews, M.3    Chiang, A.P.4    Swiderski, R.E.5
  • 30
    • 0142104970 scopus 로고    scopus 로고
    • Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl syndrome
    • Ansley SJ, Badano JL, Blacque OE, Hill J, Hoskins BE, et al. (2003) Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl syndrome. Nature 425: 628-633.
    • (2003) Nature , vol.425 , pp. 628-633
    • Ansley, S.J.1    Badano, J.L.2    Blacque, O.E.3    Hill, J.4    Hoskins, B.E.5
  • 31
    • 0037317302 scopus 로고    scopus 로고
    • Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells
    • Nauli SM, Alenghat FJ, Luo Y, Williams E, Vassilev P, et al. (2003) Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells. Nat Genet 33: 129-137.
    • (2003) Nat Genet , vol.33 , pp. 129-137
    • Nauli, S.M.1    Alenghat, F.J.2    Luo, Y.3    Williams, E.4    Vassilev, P.5
  • 32
    • 0014104888 scopus 로고
    • Flagellar regeneration in protozoan flagellates
    • Rosenbaum JL, Child FM (1967) Flagellar regeneration in protozoan flagellates. J Cell Biol 34: 345-364.
    • (1967) J Cell Biol , vol.34 , pp. 345-364
    • Rosenbaum, J.L.1    Child, F.M.2
  • 33
    • 0027098030 scopus 로고
    • Polarity of flagellar assembly in Chlamydomonas
    • Johnson KA, Rosenbaum JL (1992) Polarity of flagellar assembly in Chlamydomonas. J Cell Biol 119: 1605-1611.
    • (1992) J Cell Biol , vol.119 , pp. 1605-1611
    • Johnson, K.A.1    Rosenbaum, J.L.2
  • 35
    • 21344443110 scopus 로고    scopus 로고
    • Polycystin-2-an intracellular or plasma membrane channel?
    • Witzgall R (2005) Polycystin-2-an intracellular or plasma membrane channel? Naunyn Schmiedebergs Arch Pharmacol 371: 342-347.
    • (2005) Naunyn Schmiedebergs Arch Pharmacol , vol.371 , pp. 342-347
    • Witzgall, R.1
  • 37
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: A SNARE-associated protein implicated in synaptic transmission
    • Ilardi JM, Mochida S, Sheng ZH (1999) Snapin: a SNARE-associated protein implicated in synaptic transmission. Nat Neurosci 2: 119-124.
    • (1999) Nat Neurosci , vol.2 , pp. 119-124
    • Ilardi, J.M.1    Mochida, S.2    Sheng, Z.H.3
  • 38
    • 0142138839 scopus 로고    scopus 로고
    • Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells
    • Buxton P, Zhang XM, Walsh B, Sriratana A, Schenberg I, et al. (2003) Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells. Biochem J 375: 433-440.
    • (2003) Biochem J , vol.375 , pp. 433-440
    • Buxton, P.1    Zhang, X.M.2    Walsh, B.3    Sriratana, A.4    Schenberg, I.5
  • 39
    • 0037106579 scopus 로고    scopus 로고
    • Functional involvement of VAMP/synaptobrevin-2 in cAMP-stimulated aquaporin 2 translocation in renal collecting duct cells
    • Gouraud S, Laera A, Calamita G, Carmosino M, Procino G, et al. (2002) Functional involvement of VAMP/synaptobrevin-2 in cAMP-stimulated aquaporin 2 translocation in renal collecting duct cells. J Cell Sci 115: 3667-3674.
    • (2002) J Cell Sci , vol.115 , pp. 3667-3674
    • Gouraud, S.1    Laera, A.2    Calamita, G.3    Carmosino, M.4    Procino, G.5
  • 40
    • 27844523175 scopus 로고    scopus 로고
    • Actin and non-muscle myosin II facilitate apical exocytosis of tear proteins in rabbit lacrimal acinar epithelial cells
    • Jerdeva GV, Wu K, Yarber FA, Rhodes CJ, Kalman D, et al. (2005) Actin and non-muscle myosin II facilitate apical exocytosis of tear proteins in rabbit lacrimal acinar epithelial cells. J Cell Sci 118: 4797-4812.
    • (2005) J Cell Sci , vol.118 , pp. 4797-4812
    • Jerdeva, G.V.1    Wu, K.2    Yarber, F.A.3    Rhodes, C.J.4    Kalman, D.5
  • 41
    • 0040971539 scopus 로고    scopus 로고
    • Myosin II is involved in the production of constitutive transport vesicles from the TGN
    • Musch A, Cohen D, Rodriguez-Boulan E (1997) Myosin II is involved in the production of constitutive transport vesicles from the TGN. J Cell Biol 138: 291-306.
    • (1997) J Cell Biol , vol.138 , pp. 291-306
    • Musch, A.1    Cohen, D.2    Rodriguez-Boulan, E.3
  • 42
    • 0036904982 scopus 로고    scopus 로고
    • The role of myosin in vesicle transport during bovine chromaffin cell secretion
    • Neco P, Gil A, Del Mar Frances M, Viniegra S, Gutierrez LM (2002) The role of myosin in vesicle transport during bovine chromaffin cell secretion. Biochem J 368: 405-413.
    • (2002) Biochem J , vol.368 , pp. 405-413
    • Neco, P.1    Gil, A.2    Del Mar Frances, M.3    Viniegra, S.4    Gutierrez, L.M.5
  • 43
    • 0037403173 scopus 로고    scopus 로고
    • Myosin II in retinal pigmented epithelial cells: Evidence for an association with membranous vesicles
    • Linz-McGillem LA, Alliegro MC (2003) Myosin II in retinal pigmented epithelial cells: evidence for an association with membranous vesicles. Exp Eye Res 76: 543-552.
    • (2003) Exp Eye Res , vol.76 , pp. 543-552
    • Linz-McGillem, L.A.1    Alliegro, M.C.2
  • 44
    • 0026557199 scopus 로고
    • Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization
    • Miller M, Bower E, Levitt P, Li D, Chantler PD (1992) Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization. Neuron 8: 25-44.
    • (1992) Neuron , vol.8 , pp. 25-44
    • Miller, M.1    Bower, E.2    Levitt, P.3    Li, D.4    Chantler, P.D.5
  • 45
    • 0742288022 scopus 로고    scopus 로고
    • Nonmuscle myosin IIA and IIB have distinct functions in the exocytosis-dependent process of cell membrane repair
    • Togo T, Steinhardt RA (2004) Nonmuscle myosin IIA and IIB have distinct functions in the exocytosis-dependent process of cell membrane repair. Mol Biol Cell 15: 688-695.
    • (2004) Mol Biol Cell , vol.15 , pp. 688-695
    • Togo, T.1    Steinhardt, R.A.2
  • 46
    • 3042646322 scopus 로고    scopus 로고
    • New roles of myosin II during vesicle transport and fusion in chromaffin cells
    • Neco P, Giner D, Viniegra S, Borges R, Villarroel A, et al. (2004) New roles of myosin II during vesicle transport and fusion in chromaffin cells. J Biol Chem 279: 27450-27457.
    • (2004) J Biol Chem , vol.279 , pp. 27450-27457
    • Neco, P.1    Giner, D.2    Viniegra, S.3    Borges, R.4    Villarroel, A.5
  • 47
    • 22344445826 scopus 로고    scopus 로고
    • Cilia and the cell cycle?
    • Quarmby LM, Parker JD (2005) Cilia and the cell cycle? J Cell Biol 169: 707-710.
    • (2005) J Cell Biol , vol.169 , pp. 707-710
    • Quarmby, L.M.1    Parker, J.D.2
  • 48
    • 0036151534 scopus 로고    scopus 로고
    • Distinct subcellular expression of endogenous polycystin-2 in the plasma membrane and Golgi apparatus of MDCK cells
    • Scheffers MS, Le H, van der Bent P, Leonhard W, Prins F, et al. (2002) Distinct subcellular expression of endogenous polycystin-2 in the plasma membrane and Golgi apparatus of MDCK cells. Hum Mol Genet 11: 59-67.
    • (2002) Hum Mol Genet , vol.11 , pp. 59-67
    • Scheffers1    MS, L.H.2    van der3    Bent, P.4    Leonhard, W.5    Prins, F.6
  • 50
    • 20144383835 scopus 로고    scopus 로고
    • Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation
    • Kottgen M, Benzing T, Simmen T, Tauber R, Buchholz B, et al. (2005) Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation. Embo J 24: 705-716.
    • (2005) Embo J , vol.24 , pp. 705-716
    • Kottgen, M.1    Benzing, T.2    Simmen, T.3    Tauber, R.4    Buchholz, B.5
  • 51
    • 4544321242 scopus 로고    scopus 로고
    • PIGEA-14, a novel coiled-coil protein affecting the intracellular distribution of polycystin-2
    • Hidaka S, Konecke V, Osten L, Witzgall R (2004) PIGEA-14, a novel coiled-coil protein affecting the intracellular distribution of polycystin-2. J Biol Chem 279: 35009-35016.
    • (2004) J Biol Chem , vol.279 , pp. 35009-35016
    • Hidaka, S.1    Konecke, V.2    Osten, L.3    Witzgall, R.4
  • 52
    • 0037019017 scopus 로고    scopus 로고
    • Polycystin-2 localizes to kidney cilia and the ciliary level is elevated in orpk mice with polycystic kidney disease
    • Pazour GJ, San Agustin JT, Follit JA, Rosenbaum JL, Witman GB (2002) Polycystin-2 localizes to kidney cilia and the ciliary level is elevated in orpk mice with polycystic kidney disease. Curr Biol 12: R378-380.
    • (2002) Curr Biol , vol.12
    • Pazour, G.J.1    San Agustin, J.T.2    Follit, J.A.3    Rosenbaum, J.L.4    Witman, G.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.