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Volumn 291, Issue 4, 2006, Pages

Erratum: Polarized biosynthetic traffic in renal epithelial cells: Sorting, sorting everywhere (American Journal of Physiology - Renal Physiology (2006) 291, (F707-F713) DOI:10.1152/ajprenal.00161.2006);Polarized biosynthetic traffic in renal epithelial cells: Sorting, sorting, everywhere

Author keywords

Apical; Basolateral; Madin Darby canine kidney; Membrane traffic; trans Golgi network

Indexed keywords

APICAL MEMBRANE; BASOLATERAL MEMBRANE; BIOSYNTHESIS; CELL MEMBRANE; CELL SURFACE; ENDOSOME; HUMAN; KIDNEY EPITHELIUM; LIPID COMPOSITION; NONHUMAN; POLARIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN TARGETING; REVIEW; SIGNAL TRANSDUCTION; TRANS GOLGI NETWORK;

EID: 33749422547     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.zh2-4978-corr.2007     Document Type: Erratum
Times cited : (40)

References (57)
  • 1
    • 30044440555 scopus 로고    scopus 로고
    • A novel type of detergent-resistant membranes may contribute to an early protein sorting event in epithelial cells
    • Alfalah M, Wetzel G, Fischer I, Busche R, Sterchi EE, Zimmer KP, Sallmann HP, and Naim HY. A novel type of detergent-resistant membranes may contribute to an early protein sorting event in epithelial cells. J Biol Chem 280: 42636-42643, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 42636-42643
    • Alfalah, M.1    Wetzel, G.2    Fischer, I.3    Busche, R.4    Sterchi, E.E.5    Zimmer, K.P.6    Sallmann, H.P.7    Naim, H.Y.8
  • 2
    • 0242298589 scopus 로고    scopus 로고
    • The Rab8 GTPase selectively regulates AP-1B-dependent basolateral transport in polarized Madin-Darby canine kidney cells
    • Ang AL, Folsch H, Koivisto UM, Pypaert M, and Mellman I. The Rab8 GTPase selectively regulates AP-1B-dependent basolateral transport in polarized Madin-Darby canine kidney cells. J Cell Biol 163: 339-350, 2003.
    • (2003) J Cell Biol , vol.163 , pp. 339-350
    • Ang, A.L.1    Folsch, H.2    Koivisto, U.M.3    Pypaert, M.4    Mellman, I.5
  • 3
    • 8444221583 scopus 로고    scopus 로고
    • Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells
    • Ang AL, Taguchi T, Francis S, Folsch H, Murrells LJ, Pypaert M, Warren G, and Mellman I. Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells. J Cell Biol 167: 531-543, 2004.
    • (2004) J Cell Biol , vol.167 , pp. 531-543
    • Ang, A.L.1    Taguchi, T.2    Francis, S.3    Folsch, H.4    Murrells, L.J.5    Pypaert, M.6    Warren, G.7    Mellman, I.8
  • 5
    • 0034139848 scopus 로고    scopus 로고
    • Definition of distinct compartments in polarized Madin-Darby canine kidney (MDCK) cells for membrane-volume sorting, polarized sorting and apical recycling
    • Brown PS, Wang E, Aroeti B, Chapin SJ, Mostov KE, and Dunn KW. Definition of distinct compartments in polarized Madin-Darby canine kidney (MDCK) cells for membrane-volume sorting, polarized sorting and apical recycling. Traffic 1: 124-140, 2000.
    • (2000) Traffic , vol.1 , pp. 124-140
    • Brown, P.S.1    Wang, E.2    Aroeti, B.3    Chapin, S.J.4    Mostov, K.E.5    Dunn, K.W.6
  • 7
    • 0032494121 scopus 로고    scopus 로고
    • The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells
    • Chuang JZ and Sung CH. The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells. J Cell Biol 142: 1245-1256, 1998.
    • (1998) J Cell Biol , vol.142 , pp. 1245-1256
    • Chuang, J.Z.1    Sung, C.H.2
  • 9
    • 0142011463 scopus 로고    scopus 로고
    • Taking the A-train: Actin-based force generators and organelle targeting
    • Fehrenbacher KL, Boldogh IR, and Pon LA. Taking the A-train: actin-based force generators and organelle targeting. Trends Cell Biol 13: 472-477, 2003.
    • (2003) Trends Cell Biol , vol.13 , pp. 472-477
    • Fehrenbacher, K.L.1    Boldogh, I.R.2    Pon, L.A.3
  • 10
    • 0032692619 scopus 로고    scopus 로고
    • A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells
    • Folsch H, Ohno H, Bonifacino JS, and Mellman I. A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. Cell 99: 189-198, 1999.
    • (1999) Cell , vol.99 , pp. 189-198
    • Folsch, H.1    Ohno, H.2    Bonifacino, J.S.3    Mellman, I.4
  • 11
    • 0242266915 scopus 로고    scopus 로고
    • The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains
    • Folsch H, Pypaert M, Maday S, Pelletier L, and Mellman I. The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains. J Cell Biol 163: 351-362, 2003.
    • (2003) J Cell Biol , vol.163 , pp. 351-362
    • Folsch, H.1    Pypaert, M.2    Maday, S.3    Pelletier, L.4    Mellman, I.5
  • 12
    • 0035809211 scopus 로고    scopus 로고
    • Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells
    • Folsch H, Pypaert M, Schu P, and Mellman I. Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells. J Cell Biol 152: 595-606, 2001.
    • (2001) J Cell Biol , vol.152 , pp. 595-606
    • Folsch, H.1    Pypaert, M.2    Schu, P.3    Mellman, I.4
  • 13
    • 0028969528 scopus 로고
    • Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface
    • Futter CE, Connolly CN, Cutler DF, and Hopkins CR. Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface. J Biol Chem 270: 10999-11003, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 10999-11003
    • Futter, C.E.1    Connolly, C.N.2    Cutler, D.F.3    Hopkins, C.R.4
  • 14
    • 0036045770 scopus 로고    scopus 로고
    • The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane
    • Gan Y, McGraw TE, and Rodriguez-Boulan E. The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane. Nat Cell Biol 4: 605-609, 2002.
    • (2002) Nat Cell Biol , vol.4 , pp. 605-609
    • Gan, Y.1    McGraw, T.E.2    Rodriguez-Boulan, E.3
  • 15
    • 33744956177 scopus 로고    scopus 로고
    • Phosphatidylinositol 5-kinase stimulates apical biosynthetic delivery via an Arp2/3-dependent mechanism
    • Guerriero CJ, Weixel KM, Bruns JR, and Weisz OA. Phosphatidylinositol 5-kinase stimulates apical biosynthetic delivery via an Arp2/3-dependent mechanism. J Biol Chem 281: 15376-15384, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 15376-15384
    • Guerriero, C.J.1    Weixel, K.M.2    Bruns, J.R.3    Weisz, O.A.4
  • 17
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells
    • Hirschberg K, Miller CM, Ellenberg J, Presley JF, Siggia ED, Phair RD, and Lippincott-Schwartz J. Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells. J Cell Biol 143: 1485-1503, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 1485-1503
    • Hirschberg, K.1    Miller, C.M.2    Ellenberg, J.3    Presley, J.F.4    Siggia, E.D.5    Phair, R.D.6    Lippincott-Schwartz, J.7
  • 18
    • 33644855363 scopus 로고    scopus 로고
    • Polarized apical sorting of guanylyl cyclase C is specified by a cytosolic signal
    • Hodson CA, Ambrogi IG, Scott RO, Mohler PJ, and Milgram SL. Polarized apical sorting of guanylyl cyclase C is specified by a cytosolic signal. Traffic 7: 456-464, 2006.
    • (2006) Traffic , vol.7 , pp. 456-464
    • Hodson, C.A.1    Ambrogi, I.G.2    Scott, R.O.3    Mohler, P.J.4    Milgram, S.L.5
  • 19
    • 33645316484 scopus 로고    scopus 로고
    • Vectorial insertion of apical and basolateral membrane proteins in polarized epithelial cells revealed by quantitative 3D live cell imaging
    • Hua W, Sheff D, Toomre D, and Mellman I. Vectorial insertion of apical and basolateral membrane proteins in polarized epithelial cells revealed by quantitative 3D live cell imaging. J Cell Biol 172: 1035-1044, 2006.
    • (2006) J Cell Biol , vol.172 , pp. 1035-1044
    • Hua, W.1    Sheff, D.2    Toomre, D.3    Mellman, I.4
  • 20
    • 0037380088 scopus 로고    scopus 로고
    • Distinct cytoskeletal tracks direct individual vesicle populations to the apical membrane of epithelial cells
    • Jacob R, Heine M, Alfalah M, and Naim HY. Distinct cytoskeletal tracks direct individual vesicle populations to the apical membrane of epithelial cells. Curr Biol 13: 607-612, 2003.
    • (2003) Curr Biol , vol.13 , pp. 607-612
    • Jacob, R.1    Heine, M.2    Alfalah, M.3    Naim, H.Y.4
  • 21
    • 0035908953 scopus 로고    scopus 로고
    • Apical membrane proteins are transported in distinct vesicular carriers
    • Jacob R and Naim H. Apical membrane proteins are transported in distinct vesicular carriers. Curr Biol 11: 1444-1450, 2001.
    • (2001) Curr Biol , vol.11 , pp. 1444-1450
    • Jacob, R.1    Naim, H.2
  • 22
    • 0035147424 scopus 로고    scopus 로고
    • Multicolour imaging of post-Golgi sorting and trafficking in live cells
    • Keller P, Toomre D, Diaz E, White J, and Simons K. Multicolour imaging of post-Golgi sorting and trafficking in live cells. Nature Cell Biol 3: 140-149, 2001.
    • (2001) Nature Cell Biol , vol.3 , pp. 140-149
    • Keller, P.1    Toomre, D.2    Diaz, E.3    White, J.4    Simons, K.5
  • 24
    • 0034329456 scopus 로고    scopus 로고
    • A novel assay to demonstrate an intersection of the exocytic and endocytic pathways at early endosomes
    • Laird V and Spiess M. A novel assay to demonstrate an intersection of the exocytic and endocytic pathways at early endosomes. Exp Cell Res 260: 340-345, 2000.
    • (2000) Exp Cell Res , vol.260 , pp. 340-345
    • Laird, V.1    Spiess, M.2
  • 25
    • 0028871658 scopus 로고
    • Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes
    • Leitinger B, Hille-Rehfeld A, and Spiess M. Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes. Proc Natl Acad Sci USA 92: 10109-10113, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10109-10113
    • Leitinger, B.1    Hille-Rehfeld, A.2    Spiess, M.3
  • 26
    • 0025133358 scopus 로고
    • Vectorial apical delivery and slow endocytosis of a glycolipid-anchored fusion protein in transfected MDCK cells
    • Lisanti MP, Caras IW, Gilbert T, Hanzel D, and Rodriguez-Boulan E. Vectorial apical delivery and slow endocytosis of a glycolipid-anchored fusion protein in transfected MDCK cells. Proc Natl Acad Sci USA 87: 7419-7423, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7419-7423
    • Lisanti, M.P.1    Caras, I.W.2    Gilbert, T.3    Hanzel, D.4    Rodriguez-Boulan, E.5
  • 27
    • 16344363943 scopus 로고    scopus 로고
    • Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin
    • Lock JG and Stow JL. Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin. Mol Biol Cell 16: 1744-1755, 2005.
    • (2005) Mol Biol Cell , vol.16 , pp. 1744-1755
    • Lock, J.G.1    Stow, J.L.2
  • 28
    • 24944564503 scopus 로고
    • The in vitro cultivation of tissues of domestic and laboratory animals
    • Madin SH, Andriese PC, and Darby NB. The in vitro cultivation of tissues of domestic and laboratory animals. Am J Vet Res 18: 932-941, 1957.
    • (1957) Am J Vet Res , vol.18 , pp. 932-941
    • Madin, S.H.1    Andriese, P.C.2    Darby, N.B.3
  • 29
    • 0020804564 scopus 로고
    • Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation
    • Matlin KS and Simons K. Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation. Cell 34: 233-243, 1983.
    • (1983) Cell , vol.34 , pp. 233-243
    • Matlin, K.S.1    Simons, K.2
  • 30
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muniz M, Morsomme P, and Riezman H. Protein sorting upon exit from the endoplasmic reticulum. Cell 104: 313-320, 2001.
    • (2001) Cell , vol.104 , pp. 313-320
    • Muniz, M.1    Morsomme, P.2    Riezman, H.3
  • 31
    • 0029943503 scopus 로고    scopus 로고
    • Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells
    • Müsch A, Xu H, Shields D, and Rodriguez-Boulan E. Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells. J Cell Biol 133: 543-558, 1996.
    • (1996) J Cell Biol , vol.133 , pp. 543-558
    • Müsch, A.1    Xu, H.2    Shields, D.3    Rodriguez-Boulan, E.4
  • 32
    • 0037076273 scopus 로고    scopus 로고
    • The δ subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface
    • Nishimura N, Plutner H, Hahn K, and Balch WE. The δ subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface. Proc Natl Acad Sci USA 99: 6755-6760, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6755-6760
    • Nishimura, N.1    Plutner, H.2    Hahn, K.3    Balch, W.E.4
  • 34
    • 0034685896 scopus 로고    scopus 로고
    • Interactions between the exocytic and endocytic pathways in polarized Madin-Darby canine kidney cells
    • Orzech E, Cohen S, Weiss A, and Aroeti B. Interactions between the exocytic and endocytic pathways in polarized Madin-Darby canine kidney cells. J Biol Chem 275: 15207-15219, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 15207-15219
    • Orzech, E.1    Cohen, S.2    Weiss, A.3    Aroeti, B.4
  • 35
    • 0033593332 scopus 로고    scopus 로고
    • Interactions of the AP-1 Golgi adaptor with the polymeric immunoglobulin receptor and their possible role in mediating brefeldin A-sensitive basolateral targeting from the trans-Golgi network
    • Orzech E, Schlessinger K, Weiss A, Okamoto CT, and Aroeti B. Interactions of the AP-1 Golgi adaptor with the polymeric immunoglobulin receptor and their possible role in mediating brefeldin A-sensitive basolateral targeting from the trans-Golgi network. J Biol Chem 274: 2201-2215, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 2201-2215
    • Orzech, E.1    Schlessinger, K.2    Weiss, A.3    Okamoto, C.T.4    Aroeti, B.5
  • 36
    • 33645277808 scopus 로고    scopus 로고
    • GPI-anchored proteins are directly targeted to the apical surface in fully polarized MDCK cells
    • Paladino S, Pocard T, Catino MA, and Zurzolo C. GPI-anchored proteins are directly targeted to the apical surface in fully polarized MDCK cells. J Cell Biol 172: 1023-1034, 2006.
    • (2006) J Cell Biol , vol.172 , pp. 1023-1034
    • Paladino, S.1    Pocard, T.2    Catino, M.A.3    Zurzolo, C.4
  • 37
    • 9444267662 scopus 로고    scopus 로고
    • Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins
    • Paladino S, Sarnataro D, Pillich R, Tivodar S, Nitsch L, and Zurzolo C. Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J Cell Biol 167: 699-709, 2004.
    • (2004) J Cell Biol , vol.167 , pp. 699-709
    • Paladino, S.1    Sarnataro, D.2    Pillich, R.3    Tivodar, S.4    Nitsch, L.5    Zurzolo, C.6
  • 38
    • 0036195484 scopus 로고    scopus 로고
    • Detergent-resistant membrane microdomains and apical sorting of GPI-anchored proteins in polarized epithelial cells
    • Paladino S, Sarnataro D, and Zurzolo C. Detergent-resistant membrane microdomains and apical sorting of GPI-anchored proteins in polarized epithelial cells. Int J Med Microbiol 291: 439-445, 2002.
    • (2002) Int J Med Microbiol , vol.291 , pp. 439-445
    • Paladino, S.1    Sarnataro, D.2    Zurzolo, C.3
  • 39
    • 2342599664 scopus 로고    scopus 로고
    • Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway
    • Polishchuk R, Di Pentima A, and Lippincott-Schwartz J. Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway. Nat Cell Biol 6: 297-307, 2004.
    • (2004) Nat Cell Biol , vol.6 , pp. 297-307
    • Polishchuk, R.1    Di Pentima, A.2    Lippincott-Schwartz, J.3
  • 41
    • 0038586509 scopus 로고    scopus 로고
    • Basolateral cycling mediated by a lumenal domain targeting determinant
    • Puthenveedu MA, Bruns JR, Weisz OA, and Linstedt AD. Basolateral cycling mediated by a lumenal domain targeting determinant. Mol Biol Cell 14: 1801-1807, 2003.
    • (2003) Mol Biol Cell , vol.14 , pp. 1801-1807
    • Puthenveedu, M.A.1    Bruns, J.R.2    Weisz, O.A.3    Linstedt, A.D.4
  • 42
    • 0033179221 scopus 로고    scopus 로고
    • Glycans in post-Golgi apical targeting: Sorting signals or structural props?
    • Rodriguez-Boulan E and Gonzalez A. Glycans in post-Golgi apical targeting: sorting signals or structural props? Trends Cell Biol 9: 291-294, 1999.
    • (1999) Trends Cell Biol , vol.9 , pp. 291-294
    • Rodriguez-Boulan, E.1    Gonzalez, A.2
  • 44
    • 20544431747 scopus 로고    scopus 로고
    • Protein sorting in the Golgi complex: Shifting paradigms
    • Rodriguez-Boulan E and Musch A. Protein sorting in the Golgi complex: shifting paradigms. Biochim Biophys Acta 1744: 455-464, 2005.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 455-464
    • Rodriguez-Boulan, E.1    Musch, A.2
  • 48
    • 0036167130 scopus 로고    scopus 로고
    • AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells
    • Simmen T, Honing S, Icking A, Tikkanen R, and Hunziker W. AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells. Nat Cell Biol 4: 154-159, 2002.
    • (2002) Nat Cell Biol , vol.4 , pp. 154-159
    • Simmen, T.1    Honing, S.2    Icking, A.3    Tikkanen, R.4    Hunziker, W.5
  • 49
    • 0037404459 scopus 로고    scopus 로고
    • Identification of an apical sorting determinant in the cytoplasmic tail of megalin
    • Takeda T, Yamazaki H, and Farquhar MG. Identification of an apical sorting determinant in the cytoplasmic tail of megalin. Am J Physiol Cell Physiol 284: C1105-C1113, 2003.
    • (2003) Am J Physiol Cell Physiol , vol.284
    • Takeda, T.1    Yamazaki, H.2    Farquhar, M.G.3
  • 50
    • 0346752326 scopus 로고    scopus 로고
    • Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL
    • Tall RD, Alonso MA, and Roth MG. Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL. Traffic 4: 838-849, 2003.
    • (2003) Traffic , vol.4 , pp. 838-849
    • Tall, R.D.1    Alonso, M.A.2    Roth, M.G.3
  • 51
    • 0032897432 scopus 로고    scopus 로고
    • Dual-color visualization of trans-Golgi network to plasma membrane traffic along microtubules in living cells
    • Toomre D, Keller P, White J, Olivo JC, and Simons K. Dual-color visualization of trans-Golgi network to plasma membrane traffic along microtubules in living cells. J Cell Sci 112: 21-33, 1999.
    • (1999) J Cell Sci , vol.112 , pp. 21-33
    • Toomre, D.1    Keller, P.2    White, J.3    Olivo, J.C.4    Simons, K.5
  • 52
    • 20544465126 scopus 로고    scopus 로고
    • Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane
    • Traub LM. Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane. Biochim Biophys Acta 1744: 415-437, 2005.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 415-437
    • Traub, L.M.1
  • 53
    • 0345099309 scopus 로고    scopus 로고
    • AP-1B: Polarized sorting at the endosome
    • Traub LM and Apodaca G. AP-1B: polarized sorting at the endosome. Nat Cell Biol 5: 1045-1047, 2003.
    • (2003) Nat Cell Biol , vol.5 , pp. 1045-1047
    • Traub, L.M.1    Apodaca, G.2
  • 54
    • 23844520920 scopus 로고    scopus 로고
    • A proteoglycan undergoes different modifications en route to the apical and basolateral surfaces of Madin-Darby canine kidney cells
    • Tveit H, Dick G, Skibeli V, and Prydz K. A proteoglycan undergoes different modifications en route to the apical and basolateral surfaces of Madin-Darby canine kidney cells. J Biol Chem 280: 29596-29603, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 29596-29603
    • Tveit, H.1    Dick, G.2    Skibeli, V.3    Prydz, K.4
  • 55
    • 33645100455 scopus 로고    scopus 로고
    • Differences in the apical and basolateral pathways for glycosaminoglycan biosynthesis in Madin-Darby canine kidney cells
    • Vuong TT, Prydz K, and Tveit H. Differences in the apical and basolateral pathways for glycosaminoglycan biosynthesis in Madin-Darby canine kidney cells. Glycobiology 16: 326-332, 2006.
    • (2006) Glycobiology , vol.16 , pp. 326-332
    • Vuong, T.T.1    Prydz, K.2    Tveit, H.3
  • 57
    • 0029879919 scopus 로고    scopus 로고
    • Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells
    • Yoshimori T, Keller P, Roth MG, and Simons K. Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. J Cell Biol 133: 247-256, 1996.
    • (1996) J Cell Biol , vol.133 , pp. 247-256
    • Yoshimori, T.1    Keller, P.2    Roth, M.G.3    Simons, K.4


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