메뉴 건너뛰기




Volumn 63, Issue 12, 2006, Pages 778-791

Actin filaments are involved in the maintenance of Golgi cisternae morphology and intra-Golgi pH

Author keywords

Actin; Cytoskeleton; Electron tomography; Golgi apparatus; pH

Indexed keywords

ACTIN; BAFILOMYCIN A1; BOTULINUM TOXIN; BOTULINUM TOXIN C 2; CONCANAMYCIN A; CYTOCHALASIN D; F ACTIN; HYDROLASE INHIBITOR; LATRUNCULIN B; MYCALOLIDE B; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; TOXIN; UNCLASSIFIED DRUG;

EID: 33751163972     PISSN: 08861544     EISSN: 10970169     Source Type: Journal    
DOI: 10.1002/cm.20161     Document Type: Article
Times cited : (55)

References (67)
  • 1
    • 0029165047 scopus 로고
    • Chloride channels of intracellular organelles
    • Al Awqati Q. 1995. Chloride channels of intracellular organelles. Curr Opin Cell Biol 7:504-508.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 504-508
    • Al Awqati, Q.1
  • 3
    • 0034843704 scopus 로고    scopus 로고
    • Neutralization of pH in the Golgi apparatus causes redistribution of glycosyltransferases and changes in the o-glycosylation of mucins
    • Axelsson MA, Karlsson NG, Steel DM, Ouwendijk J, Nilsson T, Hansson GC. 2001. Neutralization of pH in the Golgi apparatus causes redistribution of glycosyltransferases and changes in the o-glycosylation of mucins. Glycobiology 11:633-644.
    • (2001) Glycobiology , vol.11 , pp. 633-644
    • Axelsson, M.A.1    Karlsson, N.G.2    Steel, D.M.3    Ouwendijk, J.4    Nilsson, T.5    Hansson, G.C.6
  • 5
    • 20544465130 scopus 로고    scopus 로고
    • Spectrins and the Golgi
    • Beck KA. 2005. Spectrins and the Golgi. Biochim Biophys Acta 1744:374-382.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 374-382
    • Beck, K.A.1
  • 6
    • 0027993053 scopus 로고
    • Golgi spectrin: Identification of an erythroid β-spectrin homolog associated with the Golgi complex
    • Beck KA, Buchanan JA, Malhotra V, Nelson WJ. 1994. Golgi spectrin: Identification of an erythroid β-spectrin homolog associated with the Golgi complex. J Cell Biol 127:707-723.
    • (1994) J Cell Biol , vol.127 , pp. 707-723
    • Beck, K.A.1    Buchanan, J.A.2    Malhotra, V.3    Nelson, W.J.4
  • 7
    • 0030918480 scopus 로고    scopus 로고
    • Golgi membrane skeleton: Identification localization and oligomerization of a 195 kDa ankyrin isoform associated with the Golgi complex
    • Beck KA, Buchanan JA, Nelson WJ. 1997. Golgi membrane skeleton: Identification localization and oligomerization of a 195 kDa ankyrin isoform associated with the Golgi complex. J Cell Sci 110:1239-1249.
    • (1997) J Cell Sci , vol.110 , pp. 1239-1249
    • Beck, K.A.1    Buchanan, J.A.2    Nelson, W.J.3
  • 8
    • 18344381438 scopus 로고    scopus 로고
    • Actin and Arf1-dependent recruitment of a cortactin-dynamin complex to the Golgi regulates post-Golgi transport
    • Cao H, Weller S, Orth JD, Chen J, Huang B, Chen JL, Stamnes M, McNiven MA. 2005. Actin and Arf1-dependent recruitment of a cortactin-dynamin complex to the Golgi regulates post-Golgi transport. Nat Cell Biol 7:483-492.
    • (2005) Nat Cell Biol , vol.7 , pp. 483-492
    • Cao, H.1    Weller, S.2    Orth, J.D.3    Chen, J.4    Huang, B.5    Chen, J.L.6    Stamnes, M.7    McNiven, M.A.8
  • 10
    • 2442494215 scopus 로고    scopus 로고
    • Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes
    • Chen JL, Lacomis L, Erdjument-Bromage H, Tempst P, Stamnes M. 2004a. Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes. FEBS Lett 566:281-286.
    • (2004) FEBS Lett , vol.566 , pp. 281-286
    • Chen, J.L.1    Lacomis, L.2    Erdjument-Bromage, H.3    Tempst, P.4    Stamnes, M.5
  • 12
    • 1642460601 scopus 로고    scopus 로고
    • Actin and microtubule regulation of trans-Golgi network architecture and copper-dependent protein transport to the cell surface
    • Cobbold C, Coventry J, Ponhambalam S, Monaco AP. 2004. Actin and microtubule regulation of trans-Golgi network architecture and copper-dependent protein transport to the cell surface. Mol Membr Biol 21:59-66.
    • (2004) Mol Membr Biol , vol.21 , pp. 59-66
    • Cobbold, C.1    Coventry, J.2    Ponhambalam, S.3    Monaco, A.P.4
  • 13
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • De Matteis MA, Morrow JS. 2000. Spectrin tethers and mesh in the biosynthetic pathway. J Cell Sci 113:2331-2343.
    • (2000) J Cell Sci , vol.113 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 14
    • 0031941594 scopus 로고    scopus 로고
    • Mechanism of acidification of the trans-Golgi network (TGN): In situ measurements of pH using retrieval of TGN38 and furin from the cell surface
    • Demaurex N, Furuya W, D'Souza S, Bonifacino JS, Grinstein S. 1998. Mechanism of acidification of the trans-Golgi network (TGN): In situ measurements of pH using retrieval of TGN38 and furin from the cell surface. J Biol Chem 273:2044-2051.
    • (1998) J Biol Chem , vol.273 , pp. 2044-2051
    • Demaurex, N.1    Furuya, W.2    D'Souza, S.3    Bonifacino, J.S.4    Grinstein, S.5
  • 15
    • 0037164808 scopus 로고    scopus 로고
    • Cell migration requires both ion translocation and cytoskeletal anchoring by the Na-H exchanger NHE1
    • Denker SP, Barber DL. 2002. Cell migration requires both ion translocation and cytoskeletal anchoring by the Na-H exchanger NHE1. J Cell Biol 159:1087-1096.
    • (2002) J Cell Biol , vol.159 , pp. 1087-1096
    • Denker, S.P.1    Barber, D.L.2
  • 16
    • 0029898290 scopus 로고    scopus 로고
    • Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds β I σ spectrin and associates with the Golgi apparatus
    • Devarajan P, Stabach PR, Mann AS, Ardito T, Kashgarian M, Morrow JS. 1996. Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds β I σ spectrin and associates with the Golgi apparatus. J Cell Biol 133:819-830.
    • (1996) J Cell Biol , vol.133 , pp. 819-830
    • Devarajan, P.1    Stabach, P.R.2    Mann, A.S.3    Ardito, T.4    Kashgarian, M.5    Morrow, J.S.6
  • 18
    • 0040117958 scopus 로고    scopus 로고
    • Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases
    • Drose S, Altendorf K. 1997. Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases. J Exp Res 200:1-8.
    • (1997) J Exp Res , vol.200 , pp. 1-8
    • Drose, S.1    Altendorf, K.2
  • 21
    • 33644873004 scopus 로고    scopus 로고
    • Actin dynamics at the Golgi complex in mammalian cells
    • Egea G, Lazaro-Dieguez F, Vilella M. 2006. Actin dynamics at the Golgi complex in mammalian cells. Curr Opin Cell Biol 18(2):168-178.
    • (2006) Curr Opin Cell Biol , vol.18 , Issue.2 , pp. 168-178
    • Egea, G.1    Lazaro-Dieguez, F.2    Vilella, M.3
  • 22
    • 0029998595 scopus 로고    scopus 로고
    • Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus
    • Erickson JW, Zhang C, Kahn RA, Evans T, Cerione RA. 1996. Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus. J Biol Chem 271:26850-26854.
    • (1996) J Biol Chem , vol.271 , pp. 26850-26854
    • Erickson, J.W.1    Zhang, C.2    Kahn, R.A.3    Evans, T.4    Cerione, R.A.5
  • 23
    • 0036179523 scopus 로고    scopus 로고
    • Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1
    • Fucini RV, Chen JL, Sharm C, Kessels MM, Stamnes M. 2002. Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1. Mol Biol Cell 13:621-631.
    • (2002) Mol Biol Cell , vol.13 , pp. 621-631
    • Fucini, R.V.1    Chen, J.L.2    Sharm, C.3    Kessels, M.M.4    Stamnes, M.5
  • 25
    • 3242808177 scopus 로고    scopus 로고
    • The spectrin family member Syne-1 functions in retrograde transport from Golgi to ER
    • Gough LL, Beck KA. 2004. The spectrin family member Syne-1 functions in retrograde transport from Golgi to ER. Biochim Biophys Acta 1693:29-36.
    • (2004) Biochim Biophys Acta , vol.1693 , pp. 29-36
    • Gough, L.L.1    Beck, K.A.2
  • 27
    • 0033574528 scopus 로고    scopus 로고
    • Specific isoforms of actin-binding proteins on distinct populations of Golgi-derived vesicles
    • Heimann K, Percival JM, Weinberger R, Gunning P, Stow JL. 1999. Specific isoforms of actin-binding proteins on distinct populations of Golgi-derived vesicles. J Biol Chem 274:10743-10750.
    • (1999) J Biol Chem , vol.274 , pp. 10743-10750
    • Heimann, K.1    Percival, J.M.2    Weinberger, R.3    Gunning, P.4    Stow, J.L.5
  • 28
    • 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, Lippincott-Schwartz J. 1998. 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) 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
  • 29
    • 0038198483 scopus 로고    scopus 로고
    • Targeting of the AE2 anion exchanger to the Golgi apparatus is cell type-dependent and correlates with the expression of Ank(195), a Golgi membrane skeletal protein
    • Holappa K, Kellokumpu S. 2003. Targeting of the AE2 anion exchanger to the Golgi apparatus is cell type-dependent and correlates with the expression of Ank(195), a Golgi membrane skeletal protein. FEBS Lett 546:257-264.
    • (2003) FEBS Lett , vol.546 , pp. 257-264
    • Holappa, K.1    Kellokumpu, S.2
  • 30
    • 0035150705 scopus 로고    scopus 로고
    • Identification of the full-length AE2 (AE2a) isoform as the Golgi-associated anion exchanger in fibroblasts
    • Holappa K, Suokas M, Soininen P, Kellokumpu S. 2001. Identification of the full-length AE2 (AE2a) isoform as the Golgi-associated anion exchanger in fibroblasts. J Histochem Cytochem 49:259-269.
    • (2001) J Histochem Cytochem , vol.49 , pp. 259-269
    • Holappa, K.1    Suokas, M.2    Soininen, P.3    Kellokumpu, S.4
  • 31
    • 1842828896 scopus 로고    scopus 로고
    • The AE2 anion exchanger is necessary for the structural integrity of the Golgi apparatus in mammalian cells
    • Holappa K, Munoz MT, Egea G, Kellokumpu S. 2004. The AE2 anion exchanger is necessary for the structural integrity of the Golgi apparatus in mammalian cells. FEBS Lett 564:97-103.
    • (2004) FEBS Lett , vol.564 , pp. 97-103
    • Holappa, K.1    Munoz, M.T.2    Egea, G.3    Kellokumpu, S.4
  • 32
    • 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, Naim HY. 2003. Distinct cytoskeletal tracks direct individual vesicle populations to the apical membrane of epithelial cells. Curr Biol 13:607-612.
    • (2003) Curr Biol , vol.13 , pp. 607-612
    • Jacob, R.1    Heine, M.2    Alfalah, M.3    Naim, H.Y.4
  • 33
    • 0036320223 scopus 로고    scopus 로고
    • Small GTP-binding protein TC10 differentially regulates two distinct populations of filamentous actin in 3T3L1 adipocytes
    • Kanzaki M, Watson RT, Hou JC, Stamnes M, Saltiel AR, Pessin JE. 2002. Small GTP-binding protein TC10 differentially regulates two distinct populations of filamentous actin in 3T3L1 adipocytes. Mol Biol Cell 13:2334-2346.
    • (2002) Mol Biol Cell , vol.13 , pp. 2334-2346
    • Kanzaki, M.1    Watson, R.T.2    Hou, J.C.3    Stamnes, M.4    Saltiel, A.R.5    Pessin, J.E.6
  • 34
    • 0024230490 scopus 로고
    • A 115-kD polypeptide immunologically related to erythrocyte Band 3 is present in Golgi membranes
    • Kellokumpu S, Neff L, Jamsa-Kellokumpu S, Kopito R, Baron R. 1988. A 115-kD polypeptide immunologically related to erythrocyte Band 3 is present in Golgi membranes. Science 242:1308-1311.
    • (1988) Science , vol.242 , pp. 1308-1311
    • Kellokumpu, S.1    Neff, L.2    Jamsa-Kellokumpu, S.3    Kopito, R.4    Baron, R.5
  • 35
    • 0037051978 scopus 로고    scopus 로고
    • Abnormal glycosylation and altered Golgi structure in colorectal cancer: Dependence on intra-Golgi pH
    • Kellokumpu S, Sormunen R, Kellokumpu I. 2002. Abnormal glycosylation and altered Golgi structure in colorectal cancer: Dependence on intra-Golgi pH. FEBS Lett 516:217-224.
    • (2002) FEBS Lett , vol.516 , pp. 217-224
    • Kellokumpu, S.1    Sormunen, R.2    Kellokumpu, I.3
  • 36
    • 0037112944 scopus 로고    scopus 로고
    • Syndapins integrate N-WASP in receptor-mediated endocytosis
    • Kessels MM, Qualmann B. 2002. Syndapins integrate N-WASP in receptor-mediated endocytosis. EMBO J 21:6083-6094.
    • (2002) EMBO J , vol.21 , pp. 6083-6094
    • Kessels, M.M.1    Qualmann, B.2
  • 37
    • 4344619558 scopus 로고    scopus 로고
    • The syndapin protein family: Linking membrane trafficking with the cytoskeleton
    • Kessels MM, Qualmann B. 2004. The syndapin protein family: Linking membrane trafficking with the cytoskeleton. J Cell Sci 117:3077-3086.
    • (2004) J Cell Sci , vol.117 , pp. 3077-3086
    • Kessels, M.M.1    Qualmann, B.2
  • 38
    • 0025690859 scopus 로고
    • Molecular biology of the anion exchanger gene family
    • Kopito RR. 1990. Molecular biology of the anion exchanger gene family. Int Rev Cytol 123:177-199.
    • (1990) Int Rev Cytol , vol.123 , pp. 177-199
    • Kopito, R.R.1
  • 39
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer JR, Mastronarde DN, McIntosh JR. 1996. Computer visualization of three-dimensional image data using IMOD. J Struct Biol 116:71-76.
    • (1996) J Struct Biol , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 41
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopis J, McCaffery JM, Miyawaki A, Farquhar MG, Tsien RY. 1998. Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc Natl Acad Sci USA 95:6803-6808.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6803-6808
    • Llopis, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 43
    • 0022168490 scopus 로고
    • Stabilizing infrastructure of cell membranes
    • Marchesi VT. 1985. Stabilizing infrastructure of cell membranes. Annu Rev Cell Biol 1:531-561.
    • (1985) Annu Rev Cell Biol , vol.1 , pp. 531-561
    • Marchesi, V.T.1
  • 44
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: An approach with alignment methods that preserve resolution
    • Mastronarde DN. 1997. Dual-axis tomography: An approach with alignment methods that preserve resolution. J Struct Biol 120:343-352.
    • (1997) J Struct Biol , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 45
    • 7244238111 scopus 로고    scopus 로고
    • Association of Cdc42/N-WASP/Arp2/3 signaling pathway with Golgi membranes
    • Matas OB, Martinez-Menarguez JA, Egea G. 2004. Association of Cdc42/N-WASP/Arp2/3 signaling pathway with Golgi membranes. Traffic 5:838-846.
    • (2004) Traffic , vol.5 , pp. 838-846
    • Matas, O.B.1    Martinez-Menarguez, J.A.2    Egea, G.3
  • 46
    • 0024962604 scopus 로고    scopus 로고
    • +-ATPase and its subunit structures
    • +-ATPase and its subunit structures. J Biol Chem 264:18445-18450.
    • (1998) J Biol Chem , vol.264 , pp. 18445-18450
    • Moriyama, Y.1    Nelson, N.2
  • 47
    • 0019121161 scopus 로고
    • Cytochalasin D does not produce net depolymerization of actin filaments in HEp-2 cells
    • Morris A, Tannenbaum J. 1980. Cytochalasin D does not produce net depolymerization of actin filaments in HEp-2 cells. Nature 287:637-639.
    • (1980) Nature , vol.287 , pp. 637-639
    • Morris, A.1    Tannenbaum, J.2
  • 48
    • 12544258841 scopus 로고    scopus 로고
    • + exchanger isoforms are distributed to Golgi and post-Golgi compartments and are involved in organeile pH regulation
    • + exchanger isoforms are distributed to Golgi and post-Golgi compartments and are involved in organeile pH regulation. J Biol Chem 280:1561-1572.
    • (2005) J Biol Chem , vol.280 , pp. 1561-1572
    • Nakamura, N.1    Tanaka, S.2    Teko, Y.3    Mitsui, K.4    Kanazawa, H.5
  • 49
    • 0036481562 scopus 로고    scopus 로고
    • +)-ATPases-Nature's most versatile proton pumps
    • +)-ATPases-Nature's most versatile proton pumps. Nat Rev Mol Cell Biol 3:94-103.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 50
    • 0037223631 scopus 로고    scopus 로고
    • The Golgi apparatus at the cell centre
    • Rios RM, Bornens M. 2003. The Golgi apparatus at the cell centre. Curr Opin Cell Biol 15:60-66.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 60-66
    • Rios, R.M.1    Bornens, M.2
  • 52
    • 0035344650 scopus 로고    scopus 로고
    • Cell control by membrane-cytoskeleton adhesion
    • Sheetz MP. 2001. Cell control by membrane-cytoskeleton adhesion. Nat Rev Mol Cell Biol 2:392-396.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 392-396
    • Sheetz, M.P.1
  • 53
    • 0036702196 scopus 로고    scopus 로고
    • Regulating the actin cytoskeleton during vesicular transport
    • Stamnes M. 2002. Regulating the actin cytoskeleton during vesicular transport. Curr Opin Cell Biol 14:428-433.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 428-433
    • Stamnes, M.1
  • 54
    • 0034529158 scopus 로고    scopus 로고
    • Regulation of the epithelial Na(+)/H(+) exchanger isoform by the cytoskeleton
    • Szaszi K, Grinstein S, Orlowski J, Kapus A. 2000. Regulation of the epithelial Na(+)/H(+) exchanger isoform by the cytoskeleton. Cell Physiol Biochem 10:265-272.
    • (2000) Cell Physiol Biochem , vol.10 , pp. 265-272
    • Szaszi, K.1    Grinstein, S.2    Orlowski, J.3    Kapus, A.4
  • 55
    • 0037044788 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis and recycling of the neuron-specific Na+/H+ exchanger NHE5 isoform: Regulation by phosphatidylinositol 3′-kinase and the actin cytoskeleton
    • Szaszi K, Paulsen A, Szabo EZ, Numata M, Grinstein S, Orlowski J. 2002. Clathrin-mediated endocytosis and recycling of the neuron-specific Na+/H+ exchanger NHE5 isoform: Regulation by phosphatidylinositol 3′-kinase and the actin cytoskeleton. J Biol Chem 277:42623-42632.
    • (2002) J Biol Chem , vol.277 , pp. 42623-42632
    • Szaszi, K.1    Paulsen, A.2    Szabo, E.Z.3    Numata, M.4    Grinstein, S.5    Orlowski, J.6
  • 57
    • 0033080404 scopus 로고    scopus 로고
    • Role of microtubules in the organization of the Golgi complex
    • Thyberg J, Moskalewski S. 1999. Role of microtubules in the organization of the Golgi complex. Exp Cell Res 246:263-279.
    • (1999) Exp Cell Res , vol.246 , pp. 263-279
    • Thyberg, J.1    Moskalewski, S.2
  • 58
    • 2142753950 scopus 로고    scopus 로고
    • Tension in tubulovesicular networks of Golgi and endoplasmic reticulum membranes
    • Upadhyaya A, Sheetz MP. 2004. Tension in tubulovesicular networks of Golgi and endoplasmic reticulum membranes. Biophys J 86:2923-2928.
    • (2004) Biophys J , vol.86 , pp. 2923-2928
    • Upadhyaya, A.1    Sheetz, M.P.2
  • 59
    • 0031779777 scopus 로고    scopus 로고
    • Actin microfilaments are essential for the cytological positioning and morphology of the Golgi complex
    • Valderrama F, Babia T, Ayala I, Kok JW, Renau-Piqueras J, Egea G. 1998. Actin microfilaments are essential for the cytological positioning and morphology of the Golgi complex. Eur J Cell Biol 76:9-17.
    • (1998) Eur J Cell Biol , vol.76 , pp. 9-17
    • Valderrama, F.1    Babia, T.2    Ayala, I.3    Kok, J.W.4    Renau-Piqueras, J.5    Egea, G.6
  • 61
    • 0034800091 scopus 로고    scopus 로고
    • Actin microfilaments facilitate the retrograde transport from the Golgi complex to the endoplasmic reticulum in mammalian cells
    • Valderrama F, Duran JM, Babia T, Barth H, Renau-Piqueras J, Egea G. 2001. Actin microfilaments facilitate the retrograde transport from the Golgi complex to the endoplasmic reticulum in mammalian cells. Traffic 2:717-726.
    • (2001) Traffic , vol.2 , pp. 717-726
    • Valderrama, F.1    Duran, J.M.2    Babia, T.3    Barth, H.4    Renau-Piqueras, J.5    Egea, G.6
  • 63
    • 0033539088 scopus 로고    scopus 로고
    • Sensitivity of the yellow variant of green fluorescent protein to halides and nitrate
    • Wachter RM, Remington SJ. 1999. Sensitivity of the yellow variant of green fluorescent protein to halides and nitrate. Curr Biol 9: R628-R629.
    • (1999) Curr Biol , vol.9
    • Wachter, R.M.1    Remington, S.J.2
  • 64
    • 0034604399 scopus 로고    scopus 로고
    • Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein
    • Wachter RM, Yarbrough D, Kallio K, Remington SJ. 2000. Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein. J Mol Biol 301:157-171.
    • (2000) J Mol Biol , vol.301 , pp. 157-171
    • Wachter, R.M.1    Yarbrough, D.2    Kallio, K.3    Remington, S.J.4
  • 66
    • 0027163325 scopus 로고
    • Involvement of the vacuolar H(+)-ATPases in the secretory pathway of HepG2 cells
    • Yilla M, Tan A, Ito K, Miwa K, Ploegh HL. 1993. Involvement of the vacuolar H(+)-ATPases in the secretory pathway of HepG2 cells. J Biol Chem 268:19092-19100.
    • (1993) J Biol Chem , vol.268 , pp. 19092-19100
    • Yilla, M.1    Tan, A.2    Ito, K.3    Miwa, K.4    Ploegh, H.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.