메뉴 건너뛰기




Volumn 19, Issue 6, 2004, Pages 362-369

Regulation of ion transport by the NHERF family of PDZ proteins

Author keywords

[No Author keywords available]

Indexed keywords

BRIDGED COMPOUND; MEMBRANE PROTEIN; PDZ PROTEIN; SODIUM PROTON EXCHANGE PROTEIN; SODIUM PROTON EXCHANGE PROTEIN 1;

EID: 10444286035     PISSN: 15489213     EISSN: None     Source Type: Journal    
DOI: 10.1152/physiol.00020.2004     Document Type: Review
Times cited : (137)

References (68)
  • 2
    • 0032711693 scopus 로고    scopus 로고
    • Basolateral Na(+)/HCO(3)(-) cotransport activity is regulated by the dissociable Na(+)/H(+) exchanger regulatory factor
    • Bernardo AA, Kear FT, Santos AV, Ma J, Steplock D, Robey RB, and Weinman EJ. Basolateral Na(+)/HCO(3)(-) cotransport activity is regulated by the dissociable Na(+)/H(+) exchanger regulatory factor. J Clin Invest 104: 195-201, 1999.
    • (1999) J Clin Invest , vol.104 , pp. 195-201
    • Bernardo, A.A.1    Kear, F.T.2    Santos, A.V.3    Ma, J.4    Steplock, D.5    Robey, R.B.6    Weinman, E.J.7
  • 3
    • 0034674677 scopus 로고    scopus 로고
    • The B1 subunit of the H+ATPase is a PDZ domain-binding protein. Colocalization with NHE-RF in renal B-intercalated cells
    • Breton S, Wiederhold T, Marshansky V, Nsumu NN, Ramesh V, and Brown D. The B1 subunit of the H+ATPase is a PDZ domain-binding protein. Colocalization with NHE-RF in renal B-intercalated cells. J Biol Chem 275: 18219-18224, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 18219-18224
    • Breton, S.1    Wiederhold, T.2    Marshansky, V.3    Nsumu, N.N.4    Ramesh, V.5    Brown, D.6
  • 4
    • 0033575916 scopus 로고    scopus 로고
    • A kinase-regulated PDZ-domain interaction controls endocytic sorting of the β2-adrenergic receptor
    • Cao TT, Deacon HW, Reczek D, Bretscher A, and von Zastrow M. A kinase-regulated PDZ-domain interaction controls endocytic sorting of the β2-adrenergic receptor. Nature 401: 286-290, 1999.
    • (1999) Nature , vol.401 , pp. 286-290
    • Cao, T.T.1    Deacon, H.W.2    Reczek, D.3    Bretscher, A.4    Von Zastrow, M.5
  • 7
    • 0037155343 scopus 로고    scopus 로고
    • + exchanger regulatory factor 2 in apical plasma membranes
    • + exchanger regulatory factor 2 in apical plasma membranes. J Biol Chem 277: 10506-10511, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 10506-10511
    • DeMarco, S.J.1    Chicka, M.C.2    Strehler, E.E.3
  • 8
    • 0033180348 scopus 로고    scopus 로고
    • Protein modules as organizers of membrane structure
    • Fanning AS and Anderson JM. Protein modules as organizers of membrane structure. Curr Opin Cell Biol 11: 432-439, 1999.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 432-439
    • Fanning, A.S.1    Anderson, J.M.2
  • 9
    • 0034637561 scopus 로고    scopus 로고
    • Evidence for ezrin-radixin-moesin-binding phosphoprotein 50 (EBP50) self-association through PDZ-PDZ interactions
    • Fouassier L, Yun CC, Fitz JG, and Doctor RB. Evidence for ezrin-radixin-moesin-binding phosphoprotein 50 (EBP50) self-association through PDZ-PDZ interactions. J Biol Chem 275: 25039-25045, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 25039-25045
    • Fouassier, L.1    Yun, C.C.2    Fitz, J.G.3    Doctor, R.B.4
  • 12
    • 0037031937 scopus 로고    scopus 로고
    • Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output
    • Glynne PA, Darling KE, Picot J, and Evans TJ. Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output. J Biol Chem 277: 33132-33138, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 33132-33138
    • Glynne, P.A.1    Darling, K.E.2    Picot, J.3    Evans, T.J.4
  • 15
    • 0033588029 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase 6A phosphorylates the Na(+)/H(+) exchanger regulatory factor via a PDZ domain-mediated interaction
    • Hall RA, Spurney RF, Premont RT, Rahman N, Blitzer JT, Pitcher JA, and Lefkowitz RJ. G protein-coupled receptor kinase 6A phosphorylates the Na(+)/H(+) exchanger regulatory factor via a PDZ domain-mediated interaction. J Biol Chem 274: 24328-24334, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 24328-24334
    • Hall, R.A.1    Spurney, R.F.2    Premont, R.T.3    Rahman, N.4    Blitzer, J.T.5    Pitcher, J.A.6    Lefkowitz, R.J.7
  • 20
    • 0035827518 scopus 로고    scopus 로고
    • + exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator
    • + exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 276: 19683-19686, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 19683-19686
    • Karthikeyan, S.1    Leung, T.2    Ladias, J.A.3
  • 21
    • 0037166247 scopus 로고    scopus 로고
    • + exchanger regulatory factor interaction with the β2 adrenergic and platelet-derived growth factor receptors
    • + exchanger regulatory factor interaction with the β2 adrenergic and platelet-derived growth factor receptors. J Biol Chem 277: 18973-18978, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 18973-18978
    • Karthikeyan, S.1    Leung, T.2    Ladias, J.A.3
  • 22
    • 0037189512 scopus 로고    scopus 로고
    • + exchanger 3 (NHE3) requires an NHE3-E3KARP-α-actinin-4 complex for oligomerization and endocytosis
    • + exchanger 3 (NHE3) requires an NHE3-E3KARP-α-actinin-4 complex for oligomerization and endocytosis. J Biol Chem 277: 23714-23724, 2002.
    • (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
  • 23
    • 0034823954 scopus 로고    scopus 로고
    • Identification of two distinct structural motifs that, when added to the C-terminal tail of the rat Ih receptor, redirect the internalized hormone-receptor complex from a degradation to a recycling pathway
    • Kishi M, Liu X, Hirakawa T, Reczek D, Bretscher A, and Ascoli M. Identification of two distinct structural motifs that, when added to the C-terminal tail of the rat Ih receptor, redirect the internalized hormone-receptor complex from a degradation to a recycling pathway. Mol Endocrinol 15: 1624-1635, 2001.
    • (2001) Mol Endocrinol , vol.15 , pp. 1624-1635
    • Kishi, M.1    Liu, X.2    Hirakawa, T.3    Reczek, D.4    Bretscher, A.5    Ascoli, M.6
  • 24
    • 0037315288 scopus 로고    scopus 로고
    • Targeted disruption of the PDZK1 gene by homologous recombination
    • Kocher O, Pal R, Roberts M, Cirovic C, and Gilchrist A. Targeted disruption of the PDZK1 gene by homologous recombination. Mol Cell Biol 23: 1175-1180, 2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 1175-1180
    • Kocher, O.1    Pal, R.2    Roberts, M.3    Cirovic, C.4    Gilchrist, A.5
  • 26
    • 0032491428 scopus 로고    scopus 로고
    • The role of NHERF and E3KARP in the cAMP-mediated inhibition of NHE3
    • Lamprecht G, Weinman EJ, and Yun CH. The role of NHERF and E3KARP in the cAMP-mediated inhibition of NHE3. J Biol Chem 273: 29972-29978, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 29972-29978
    • Lamprecht, G.1    Weinman, E.J.2    Yun, C.H.3
  • 27
    • 0035943075 scopus 로고    scopus 로고
    • Oligomerization of NHERF-1 and NHERF-2 PDZ domains: Differential regulation by association with receptor carboxyl-termini and by phosphorylation
    • Lau AG and Hall RA. Oligomerization of NHERF-1 and NHERF-2 PDZ domains: differential regulation by association with receptor carboxyl-termini and by phosphorylation. Biochemistry 40: 8572-8580, 2001.
    • (2001) Biochemistry , vol.40 , pp. 8572-8580
    • Lau, A.G.1    Hall, R.A.2
  • 28
    • 0037868290 scopus 로고    scopus 로고
    • Role of NHERF-1 in regulation of the activity of Na-K ATPase and sodium-phosphate co-transport in epithelial cells
    • Lederer ED, Khundmiri SJ, and Weinman EJ. Role of NHERF-1 in regulation of the activity of Na-K ATPase and sodium-phosphate co-transport in epithelial cells. J Am Soc Nephrol 14: 1711-1719, 2003.
    • (2003) J Am Soc Nephrol , vol.14 , pp. 1711-1719
    • Lederer, E.D.1    Khundmiri, S.J.2    Weinman, E.J.3
  • 29
    • 0038269099 scopus 로고    scopus 로고
    • + exchanger 3 (NHE3) activity by increasing its exocytosis by an NHE3 kinase a regulatory protein-dependent mechanism
    • + exchanger 3 (NHE3) activity by increasing its exocytosis by an NHE3 kinase A regulatory protein-dependent mechanism. J Biol Chem 278: 16494-16501, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 16494-16501
    • Lee-Kwon, W.1    Kawano, K.2    Choi, J.W.3    Kim, J.H.4    Donowitz, M.5
  • 30
    • 0037178820 scopus 로고    scopus 로고
    • + exchanger regulatory factor (EBP50/NHERF) blocks U50,488H-induced down-regulation of the human kappa opioid receptor by enhancing its recycling rate
    • + exchanger regulatory factor (EBP50/NHERF) blocks U50,488H-induced down-regulation of the human kappa opioid receptor by enhancing its recycling rate. J Biol Chem 277: 27545-27552, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 27545-27552
    • Li, J.G.1    Chen, C.2    Liu-Chen, L.Y.3
  • 33
    • 0242330281 scopus 로고    scopus 로고
    • + exchanger-regulatory factor 1 mediates inhibition of phosphate transport by parathyroid hormone and second messengers by acting at multiple sites in opossum kidney cells
    • + exchanger-regulatory factor 1 mediates inhibition of phosphate transport by parathyroid hormone and second messengers by acting at multiple sites in opossum kidney cells. Mol Endocrinol 17: 2355-2364, 2003.
    • (2003) Mol Endocrinol , vol.17 , pp. 2355-2364
    • Mahon, M.J.1    Cole, J.A.2    Lederer, E.D.3    Segre, G.V.4
  • 34
    • 0037142080 scopus 로고    scopus 로고
    • + exchanger regulatory factor 2 directs parathyroid hormone 1 receptor signalling
    • + exchanger regulatory factor 2 directs parathyroid hormone 1 receptor signalling. Nature 417: 858-861, 2002.
    • (2002) Nature , vol.417 , pp. 858-861
    • Mahon, M.J.1    Donowitz, M.2    Yun, C.C.3    Segre, G.V.4
  • 36
    • 0033571594 scopus 로고    scopus 로고
    • Yes-associated protein 65 localizes p62(c-Yes) to the apical compartment of airway epithelia by association with EBP50
    • Mohler PJ, Kreda SM, Boucher RC, Sudol M, Stutts MJ, and Milgram SL. Yes-associated protein 65 localizes p62(c-Yes) to the apical compartment of airway epithelia by association with EBP50. J Cell Biol 147: 879-890, 1999.
    • (1999) J Cell Biol , vol.147 , pp. 879-890
    • Mohler, P.J.1    Kreda, S.M.2    Boucher, R.C.3    Sudol, M.4    Stutts, M.J.5    Milgram, S.L.6
  • 38
    • 0942298158 scopus 로고    scopus 로고
    • Cellular retinaldehyde-binding protein interacts with ERM-binding phosphoprotein 50 in retinal pigment epithelium
    • Nawrot M, West K, Huang J, Possin DE, Bretscher A, Crabb JW, and Saari JC. Cellular retinaldehyde-binding protein interacts with ERM-binding phosphoprotein 50 in retinal pigment epithelium. Invest Ophthalmol Vis Sci 45: 393-401, 2004.
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 393-401
    • Nawrot, M.1    West, K.2    Huang, J.3    Possin, D.E.4    Bretscher, A.5    Crabb, J.W.6    Saari, J.C.7
  • 39
    • 0012927828 scopus 로고    scopus 로고
    • PDZ domain proteins: Plug and play!
    • Nourry C, Grant SG, and Borg JP. PDZ domain proteins: plug and play! Sci STKE 2003: RE7, 2003.
    • (2003) Sci STKE , vol.2003
    • Nourry, C.1    Grant, S.G.2    Borg, J.P.3
  • 40
    • 0036617756 scopus 로고    scopus 로고
    • CIC-3B, a novel CIC-3 splicing variant that interacts with EBP50 and facilitates expression of CFTR-regulated ORCC
    • Ogura T, Furukawa T, Toyozaki T, Yamada K, Zheng YJ, Katayama Y, Nakaya H, and Inagaki N. CIC-3B, a novel CIC-3 splicing variant that interacts with EBP50 and facilitates expression of CFTR-regulated ORCC. FASEB J 16: 863-865, 2002.
    • (2002) FASEB J , vol.16 , pp. 863-865
    • Ogura, T.1    Furukawa, T.2    Toyozaki, T.3    Yamada, K.4    Zheng, Y.J.5    Katayama, Y.6    Nakaya, H.7    Inagaki, N.8
  • 43
    • 0041421190 scopus 로고    scopus 로고
    • A kinase-regulated mechanism controls CFTR channel gating by disrupting bivalent PDZ domain interactions
    • Raghuram V, Hormuth H, and Foskett JK. A kinase-regulated mechanism controls CFTR channel gating by disrupting bivalent PDZ domain interactions. Proc Natl Acad Sci USA 100: 9620-9625, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9620-9625
    • Raghuram, V.1    Hormuth, H.2    Foskett, J.K.3
  • 44
    • 0035970113 scopus 로고    scopus 로고
    • Regulation of cystic fibrosis transmembrane conductance regulator single-channel gating by bivalent PDZ-domain-mediated interaction
    • Raghuram V, Mak DD, and Foskett JK. Regulation of cystic fibrosis transmembrane conductance regulator single-channel gating by bivalent PDZ-domain-mediated interaction. Proc Natl Acad Sci USA 98: 1300-1305, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1300-1305
    • Raghuram, V.1    Mak, D.D.2    Foskett, J.K.3
  • 45
    • 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, and Bretscher A. Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J Cell Biol 139: 169-179, 1997.
    • (1997) J Cell Biol , vol.139 , pp. 169-179
    • Reczek, D.1    Berryman, M.2    Bretscher, A.3
  • 46
    • 0035795417 scopus 로고    scopus 로고
    • Identification of EPI64, a TBC/rabGAP domain-containing microvillar protein that binds to the first PDZ domain of EBP50 and E3KARP
    • Reczek D and Bretscher A. Identification of EPI64, a TBC/rabGAP domain-containing microvillar protein that binds to the first PDZ domain of EBP50 and E3KARP. J Cell Biol 153: 191-206, 2001.
    • (2001) J Cell Biol , vol.153 , pp. 191-206
    • Reczek, D.1    Bretscher, A.2
  • 47
    • 0037175055 scopus 로고    scopus 로고
    • Regulation of GTP-binding protein αq (Gαq) signaling by the ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50)
    • Rochdi MD, Watier V, La Madeleine C, Nakata H, Kozasa T, and Parent JL. Regulation of GTP-binding protein αq (Gαq) signaling by the ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50). J Biol Chem 277: 40751-40759, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 40751-40759
    • Rochdi, M.D.1    Watier, V.2    La Madeleine, C.3    Nakata, H.4    Kozasa, T.5    Parent, J.L.6
  • 49
    • 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, and 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 USA 99: 11470-11475, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11470-11475
    • Shenolikar, S.1    Voltz, J.W.2    Minkoff, C.M.3    Wade, J.B.4    Weinman, E.J.5
  • 50
    • 0038121958 scopus 로고    scopus 로고
    • EBP50, a β-catenin-associating protein, enhances Wnt signaling and is overexpressed in hepatocellular carcinoma
    • Shibata T, Chuma M, Kokubu A, Sakamoto M, and Hirohashi S. EBP50, a β-catenin-associating protein, enhances Wnt signaling and is overexpressed in hepatocellular carcinoma. Hepatology 38: 178-186, 2003.
    • (2003) Hepatology , vol.38 , pp. 178-186
    • Shibata, T.1    Chuma, M.2    Kokubu, A.3    Sakamoto, M.4    Hirohashi, S.5
  • 52
    • 0037031938 scopus 로고    scopus 로고
    • The adenosine 2b receptor is recruited to the plasma membrane and associates with E3KARP and Ezrin upon agonist stimulation
    • Sitaraman SV, Wang L, Wong M, Bruewer M, Hobert M, Yun CH, Merlin D, and Madara JL. The adenosine 2b receptor is recruited to the plasma membrane and associates with E3KARP and Ezrin upon agonist stimulation. J Biol Chem 277: 33188-33195, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 33188-33195
    • Sitaraman, S.V.1    Wang, L.2    Wong, M.3    Bruewer, M.4    Hobert, M.5    Yun, C.H.6    Merlin, D.7    Madara, J.L.8
  • 54
    • 0033940009 scopus 로고    scopus 로고
    • Functional analysis of the neurofibromatosis type 2 protein by means of disease-causing point mutations
    • Stokowski RP and Cox DR. Functional analysis of the neurofibromatosis type 2 protein by means of disease-causing point mutations. Am J Hum Genet 66: 873-891, 2000.
    • (2000) Am J Hum Genet , vol.66 , pp. 873-891
    • Stokowski, R.P.1    Cox, D.R.2
  • 55
    • 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, Trost C, Flockerzi V, Li M, Ramesh V, and Zhu MX. Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF. J Biol Chem 275: 37559-37564, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 37559-37564
    • Tang, Y.1    Tang, J.2    Chen, Z.3    Trost, C.4    Flockerzi, V.5    Li, M.6    Ramesh, V.7    Zhu, M.X.8
  • 56
    • 0035834678 scopus 로고    scopus 로고
    • Distinct binding specificity of the multiple PDZ domains of INADL, a human protein with homology to INAD from Drosophila melanogaster
    • Vaccaro P, Brannetti B, Montecchi-Palazzi L, Philipp S, Citterich MH, Cesareni G, and Dente L. Distinct binding specificity of the multiple PDZ domains of INADL, a human protein with homology to INAD from Drosophila melanogaster. J Biol Chem 276: 42122-42130, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 42122-42130
    • Vaccaro, P.1    Brannetti, B.2    Montecchi-Palazzi, L.3    Philipp, S.4    Citterich, M.H.5    Cesareni, G.6    Dente, L.7
  • 57
    • 0037503653 scopus 로고    scopus 로고
    • PDZ domains-glue and guide
    • Van Ham M and Hendriks W. PDZ domains-glue and guide. Mol Biol Rep 30: 69-82, 2003.
    • (2003) Mol Biol Rep , vol.30 , pp. 69-82
    • Van Ham, M.1    Hendriks, W.2
  • 59
    • 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, and 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 427: 103-108, 1998.
    • (1998) FEBS Lett , vol.427 , pp. 103-108
    • Wang, S.1    Raab, R.W.2    Schatz, P.J.3    Guggino, W.B.4    Li, M.5
  • 60
    • 0033834085 scopus 로고    scopus 로고
    • Signal complex regulation of renal transport proteins: NHERF and regulation of NHE3 by PKA
    • Weinman EJ, Minkoff C, and Shenolikar S. Signal complex regulation of renal transport proteins: NHERF and regulation of NHE3 by PKA. Am J Physiol Renal Physiol 279: F393-F399, 2000.
    • (2000) Am J Physiol Renal Physiol , vol.279
    • Weinman, E.J.1    Minkoff, C.2    Shenolikar, S.3
  • 62
    • 0037432134 scopus 로고    scopus 로고
    • NHERF-1 uniquely transduces the cAMP signals that inhibit sodium-hydrogen exchange in mouse renal apical membranes
    • Weinman EJ, Steplock D, and Shenolikar S. NHERF-1 uniquely transduces the cAMP signals that inhibit sodium-hydrogen exchange in mouse renal apical membranes. FEBS Lett 536: 141-144, 2003.
    • (2003) FEBS Lett , vol.536 , pp. 141-144
    • Weinman, E.J.1    Steplock, D.2    Shenolikar, S.3
  • 64
    • 0242349774 scopus 로고    scopus 로고
    • A C-terminal PDZ motif in NHE3 binds NHERF-1 and enhances cAMP inhibition of sodium-hydrogen exchange
    • Weinman EJ, Wang Y, Wang F, Greer C, Steplock D, and Shenolikar S. A C-terminal PDZ motif in NHE3 binds NHERF-1 and enhances cAMP inhibition of sodium-hydrogen exchange. Biochemistry 42: 12662-12668, 2003.
    • (2003) Biochemistry , vol.42 , pp. 12662-12668
    • Weinman, E.J.1    Wang, Y.2    Wang, F.3    Greer, C.4    Steplock, D.5    Shenolikar, S.6
  • 65
    • 1342282968 scopus 로고    scopus 로고
    • Assembly and trafficking of a multiprotein ROMK (Kir1.1) channel complex by PDZ interactions
    • Yoo D, Flagg TP, Olsen O, Raghuram V, Foskett JK, and Welling PA. Assembly and trafficking of a multiprotein ROMK (Kir1.1) channel complex by PDZ interactions. J Biol Chem 279: 6863-6873, 2003.
    • (2003) J Biol Chem , vol.279 , pp. 6863-6873
    • Yoo, D.1    Flagg, T.P.2    Olsen, O.3    Raghuram, V.4    Foskett, J.K.5    Welling, P.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.