메뉴 건너뛰기




Volumn 94, Issue 5, 2006, Pages 830-841

Functional proteomic analysis of GS-NS0 murine myeloma cell lines with varying recombinant monoclonal antibody production rate

Author keywords

Cell specific production; Murine myeloma; Proteomics; Recombinant monoclonal antibody; Unfolded protein response

Indexed keywords

CELL MEMBRANES; ENZYME INHIBITION; MASS SPECTROMETRY; METABOLISM; MOLECULAR STRUCTURE; MONOCLONAL ANTIBODIES;

EID: 33746865348     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.20899     Document Type: Article
Times cited : (63)

References (68)
  • 1
    • 0035829827 scopus 로고    scopus 로고
    • Decoupling cell growth and product formation in Chinese hamster ovary cells through metabolic control
    • Altamirano C, Cairo JJ, Godia F. 2001. Decoupling cell growth and product formation in Chinese hamster ovary cells through metabolic control. Biotechnol Bioeng 76(4):351-360.
    • (2001) Biotechnol Bioeng , vol.76 , Issue.4 , pp. 351-360
    • Altamirano, C.1    Cairo, J.J.2    Godia, F.3
  • 2
    • 0037134782 scopus 로고    scopus 로고
    • Coherent and robust modulation of a metabolic network by cytoskeletal organization and dynamics
    • Aon MA, Cortassa S. 2002. Coherent and robust modulation of a metabolic network by cytoskeletal organization and dynamics. Biophys Chem 97(2-3):213-231.
    • (2002) Biophys Chem , vol.97 , Issue.2-3 , pp. 213-231
    • Aon, M.A.1    Cortassa, S.2
  • 3
    • 0030571217 scopus 로고    scopus 로고
    • Inverse metabolic engineering: A strategy for directed genetic engineering of useful phenotypes
    • Bailey JE, Shurlati A, Hatzimanikatis V, Lee K, Renner WA, Tsai PS. 1996. Inverse metabolic engineering: A strategy for directed genetic engineering of useful phenotypes. Biotechnol Bioeng 52(1):109-121.
    • (1996) Biotechnol Bioeng , vol.52 , Issue.1 , pp. 109-121
    • Bailey, J.E.1    Shurlati, A.2    Hatzimanikatis, V.3    Lee, K.4    Renner, W.A.5    Tsai, P.S.6
  • 4
    • 0031052636 scopus 로고    scopus 로고
    • RNA and cytoskeletal filaments
    • Bassell G, Singer RH. 1997. mRNA and cytoskeletal filaments. Curr Opin Cell Biol 9(1):109-115.
    • (1997) Curr Opin Cell Biol , vol.9 , Issue.1 , pp. 109-115
    • Bassell, G.1    Singer, R.H.2
  • 5
    • 0034801641 scopus 로고    scopus 로고
    • Cofilin activation during Ca(2+)-triggered secretion from adrenal chromaffin cells
    • Birkenfeld J, Kartmann B, Betz H, Roth D. 2001. Cofilin activation during Ca(2+)-triggered secretion from adrenal chromaffin cells. Biochem Biophys Res Commun 286(3):493-498.
    • (2001) Biochem Biophys Res Commun , vol.286 , Issue.3 , pp. 493-498
    • Birkenfeld, J.1    Kartmann, B.2    Betz, H.3    Roth, D.4
  • 6
    • 13544249755 scopus 로고    scopus 로고
    • Effect of increased expression of protein disulphide isomerase and heavy chain binding protein GRP78 on antibody expression in recombinant CHO cells
    • Borth N, Mattanovitch D, Kunert R, Katinger H. 2005. Effect of increased expression of protein disulphide isomerase and heavy chain binding protein GRP78 on antibody expression in recombinant CHO cells. Biotechnol Prog 21(1):106-111.
    • (2005) Biotechnol Prog , vol.21 , Issue.1 , pp. 106-111
    • Borth, N.1    Mattanovitch, D.2    Kunert, R.3    Katinger, H.4
  • 7
    • 0033739622 scopus 로고    scopus 로고
    • PERK mediates cell-cycle exit during the mammalian unfolded protein response
    • Brewer JW, Diehl JA. 2000. PERK mediates cell-cycle exit during the mammalian unfolded protein response. Proc Natl Acad Sci USA 97(23):12625-12630.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.23 , pp. 12625-12630
    • Brewer, J.W.1    Diehl, J.A.2
  • 8
    • 3242726864 scopus 로고    scopus 로고
    • Impact of 'omic' analyses on inverse metabolic engineering
    • Bro C, Nielsen J. 2004. Impact of 'omic' analyses on inverse metabolic engineering. Metab Eng 6(3):204-211.
    • (2004) Metab Eng , vol.6 , Issue.3 , pp. 204-211
    • Bro, C.1    Nielsen, J.2
  • 9
    • 0028802746 scopus 로고
    • A hierarchy of ATP-consuming processes in mammalian cells
    • Buttgereit F, Brand MD. 1995. A hierarchy of ATP-consuming processes in mammalian cells. Biochem J 312(Pt 1):163-167.
    • (1995) Biochem J , vol.312 , Issue.PART 1 , pp. 163-167
    • Buttgereit, F.1    Brand, M.D.2
  • 10
    • 0037279250 scopus 로고    scopus 로고
    • Cell growth arrest by nucleotides, nucleosides and bases as a tool for improved production of recombinant proteins
    • Carvalhal AV, Santos SS, Calado J, Haury M, Carrondo MJ. 2003. Cell growth arrest by nucleotides, nucleosides and bases as a tool for improved production of recombinant proteins. Biotechnol Prog 19(1):69-83.
    • (2003) Biotechnol Prog , vol.19 , Issue.1 , pp. 69-83
    • Carvalhal, A.V.1    Santos, S.S.2    Calado, J.3    Haury, M.4    Carrondo, M.J.5
  • 11
    • 11144260096 scopus 로고    scopus 로고
    • Processing of data generated by 2-dimensional gel electrophoresis for statistical analysis: Missing data, normalization and statistics
    • Chang J, Van Remmen H, Ward WF, Regnier FE, Richardson A, Cornell J. 2004. Processing of data generated by 2-dimensional gel electrophoresis for statistical analysis: Missing data, normalization and statistics. J Proteome Res 3(6):1210-1218, 1535-3893.
    • (2004) J Proteome Res , vol.3 , Issue.6 , pp. 1210-1218
    • Chang, J.1    Van Remmen, H.2    Ward, W.F.3    Regnier, F.E.4    Richardson, A.5    Cornell, J.6
  • 12
    • 0346504006 scopus 로고    scopus 로고
    • Quantitative and qualitative measure of intralaboratory two-dimensional protein gel reproducibility and the effects of sample preparation, sample load, and image analysis
    • Choe LH, Lee KH. 2003. Quantitative and qualitative measure of intralaboratory two-dimensional protein gel reproducibility and the effects of sample preparation, sample load, and image analysis. Electrophoresis 24(19-20):3500-3507.
    • (2003) Electrophoresis , vol.24 , Issue.19-20 , pp. 3500-3507
    • Choe, L.H.1    Lee, K.H.2
  • 13
    • 0024041810 scopus 로고
    • The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extracts
    • Dabora SL, Sheetz MP. 1988. The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extracts. Cell 54(1):27-35.
    • (1988) Cell , vol.54 , Issue.1 , pp. 27-35
    • Dabora, S.L.1    Sheetz, M.P.2
  • 15
    • 23844547597 scopus 로고    scopus 로고
    • Engineering mammalian cell factories for improved recombinant monoclonal antibody production: Lessons from nature?
    • Dinnis DM, James DC. 2005. Engineering mammalian cell factories for improved recombinant monoclonal antibody production: lessons from nature? Biotechnol Bioeng 91(2):180-189.
    • (2005) Biotechnol Bioeng , vol.91 , Issue.2 , pp. 180-189
    • Dinnis, D.M.1    James, D.C.2
  • 17
    • 0035783192 scopus 로고    scopus 로고
    • Review: Cellular substrates of the eukaryotic chaperonin TRiC/CCT
    • Dunn AY, Melville MW, Frydman J. 2001. Review: Cellular substrates of the eukaryotic chaperonin TRiC/CCT. J Struct Biol 135(2):176-184.
    • (2001) J Struct Biol , vol.135 , Issue.2 , pp. 176-184
    • Dunn, A.Y.1    Melville, M.W.2    Frydman, J.3
  • 18
    • 0026592689 scopus 로고
    • Evidence for posttranscriptional stimulation of monoclonal antibody secretion by L-glutamine during slow hybridoma growth
    • Flickinger MC, Goebel NK, Bibila T, Boycejacino S. 1992. Evidence for posttranscriptional stimulation of monoclonal antibody secretion by L-glutamine during slow hybridoma growth. J Biotechnol 22(3):201-226.
    • (1992) J Biotechnol , vol.22 , Issue.3 , pp. 201-226
    • Flickinger, M.C.1    Goebel, N.K.2    Bibila, T.3    Boycejacino, S.4
  • 19
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman J. 2001. Folding of newly translated proteins in vivo: The role of molecular chaperones. Annu Rev Biochem 70:603-647.
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 20
    • 0036179523 scopus 로고    scopus 로고
    • Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbpl
    • Fucini RV, Chen JL, Sharma C, Kessels MM, Stamnes M. 2002. Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbpl. Mol Biol Cell 13(2):621-631.
    • (2002) Mol Biol Cell , vol.13 , Issue.2 , pp. 621-631
    • Fucini, R.V.1    Chen, J.L.2    Sharma, C.3    Kessels, M.M.4    Stamnes, M.5
  • 21
    • 0037073712 scopus 로고    scopus 로고
    • Activation of an unfolded protein response during differentiation of antibody-secreting B cells
    • Gass JN, Gifford NM, Brewer JW. 2002. Activation of an unfolded protein response during differentiation of antibody-secreting B cells. J Biol Chem 277(50):49047-49054.
    • (2002) J Biol Chem , vol.277 , Issue.50 , pp. 49047-49054
    • Gass, J.N.1    Gifford, N.M.2    Brewer, J.W.3
  • 22
    • 0036653675 scopus 로고    scopus 로고
    • Concomitant determination of absolute values of cellular protein amounts, synthesis rates, and turnover rates by quantitative proteome profiling
    • Gerner C, Vejda S, Gelbmann D, Bayer E, Gotzmann J, Schulte-Hermann R, Mikulits W. 2002. Concomitant determination of absolute values of cellular protein amounts, synthesis rates, and turnover rates by quantitative proteome profiling. Mol Cell Proteomics 1(7):528-537.
    • (2002) Mol Cell Proteomics , vol.1 , Issue.7 , pp. 528-537
    • Gerner, C.1    Vejda, S.2    Gelbmann, D.3    Bayer, E.4    Gotzmann, J.5    Schulte-Hermann, R.6    Mikulits, W.7
  • 23
    • 0036794093 scopus 로고    scopus 로고
    • 14-3-3 Regulates actin dynamics by stabilizing phosphorylated cofilin
    • Gohla A, Bokoch GM. 2002. 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin. Curr Biol 12(19):1704-1710.
    • (2002) Curr Biol , vol.12 , Issue.19 , pp. 1704-1710
    • Gohla, A.1    Bokoch, G.M.2
  • 24
    • 0036591973 scopus 로고    scopus 로고
    • BiP is feed-back regulated by control of protein translation efficiency
    • Gulow K, Bienert D, Haas IG. 2002. BiP is feed-back regulated by control of protein translation efficiency. J Cell Sci 115(Pt 11):2443-2452.
    • (2002) J Cell Sci , vol.115 , Issue.PART 11 , pp. 2443-2452
    • Gulow, K.1    Bienert, D.2    Haas, I.G.3
  • 25
    • 0034662907 scopus 로고    scopus 로고
    • Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology
    • Gygi SP, Corthals GL, Zhang Y, Rochon Y, Aebersold R. 2000. Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology. Proc Natl Acad Sci USA 97(17):9390-9395.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.17 , pp. 9390-9395
    • Gygi, S.P.1    Corthals, G.L.2    Zhang, Y.3    Rochon, Y.4    Aebersold, R.5
  • 26
    • 0033206211 scopus 로고    scopus 로고
    • Dynamical analysis of gene networks requires both mRNA and protein expression information
    • Hatzimanikatis V, Lee KH. 1999. Dynamical analysis of gene networks requires both mRNA and protein expression information. Metab Eng 1(4):275-281.
    • (1999) Metab Eng , vol.1 , Issue.4 , pp. 275-281
    • Hatzimanikatis, V.1    Lee, K.H.2
  • 27
  • 28
  • 29
    • 0030305457 scopus 로고    scopus 로고
    • R: A language for data analysis and graphics
    • Ihaka R, Gentleman R. 1996. R: A language for data analysis and graphics. J Comput Graphical Stat 5(3):299-314.
    • (1996) J Comput Graphical Stat , vol.5 , Issue.3 , pp. 299-314
    • Ihaka, R.1    Gentleman, R.2
  • 30
    • 0033385223 scopus 로고    scopus 로고
    • Improvement of the primary metabolism of cell cultures by introducing a new cytoplasmic pyruvate carboxylase reaction
    • Irani N, Wirth M, van Den Heuvel J, Wagner R. 1999. Improvement of the primary metabolism of cell cultures by introducing a new cytoplasmic pyruvate carboxylase reaction. Biotechnol Bioeng 66(4):238-246.
    • (1999) Biotechnol Bioeng , vol.66 , Issue.4 , pp. 238-246
    • Irani, N.1    Wirth, M.2    Van Den Heuvel, J.3    Wagner, R.4
  • 31
    • 0026489887 scopus 로고
    • Association of glycolytic enzymes with the cytoskeleton
    • Knull HR, Walsh JL. 1992. Association of glycolytic enzymes with the cytoskeleton. Curr Top Cell Regul 33:15-30.
    • (1992) Curr Top Cell Regul , vol.33 , pp. 15-30
    • Knull, H.R.1    Walsh, J.L.2
  • 32
    • 0346363685 scopus 로고    scopus 로고
    • Large scale gene expression profiling of metabolic shift of mammalian cells in culture
    • Korke R, Gatti Mde L, Lau AL, Lim JW, Seow TK, Chung MC, Hu WS. 2004. Large scale gene expression profiling of metabolic shift of mammalian cells in culture. J Biotechnol 107(1):1-17.
    • (2004) J Biotechnol , vol.107 , Issue.1 , pp. 1-17
    • Korke, R.1    Gatti Mde, L.2    Lau, A.L.3    Lim, J.W.4    Seow, T.K.5    Chung, M.C.6    Hu, W.S.7
  • 33
    • 0032838622 scopus 로고    scopus 로고
    • BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly
    • Lee YK, Brewer JW, Hellman R, Hendershot LM. 1999. BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly. Mol Biol Cell 10(7):2209-2219.
    • (1999) Mol Biol Cell , vol.10 , Issue.7 , pp. 2209-2219
    • Lee, Y.K.1    Brewer, J.W.2    Hellman, R.3    Hendershot, L.M.4
  • 34
    • 0025789619 scopus 로고
    • Regulation of endoplasmic reticulum stress proteins in COS cells transfected with immunoglobulin mu heavy chain cDNA
    • Lenny N, Green M. 1991. Regulation of endoplasmic reticulum stress proteins in COS cells transfected with immunoglobulin mu heavy chain cDNA. J Biol Chem 266(30):20532-20537.
    • (1991) J Biol Chem , vol.266 , Issue.30 , pp. 20532-20537
    • Lenny, N.1    Green, M.2
  • 35
    • 0033735339 scopus 로고    scopus 로고
    • Relationship between cell size, cell cycle and specific recombinant protein productivity
    • Lloyd DR, Holmes P, Jackson LP, Emery AN, Al-Rubeai M. 2000. Relationship between cell size, cell cycle and specific recombinant protein productivity. Cytotechnology 34(1-2):59-70.
    • (2000) Cytotechnology , vol.34 , Issue.1-2 , pp. 59-70
    • Lloyd, D.R.1    Holmes, P.2    Jackson, L.P.3    Emery, A.N.4    Al-Rubeai, M.5
  • 36
    • 0033991590 scopus 로고    scopus 로고
    • Cytoarchitecture and physical properties of cytoplasm: Volume, viscosity, diffusion, intracellular surface area
    • Luby-Phelps K. 2000. Cytoarchitecture and physical properties of cytoplasm: Volume, viscosity, diffusion, intracellular surface area. Int Rev Cytol 192:189-221.
    • (2000) Int Rev Cytol , vol.192 , pp. 189-221
    • Luby-Phelps, K.1
  • 37
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • Mackintosh C. 2004. Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem J 381(Pt 2):329-342.
    • (2004) Biochem J , vol.381 , Issue.PART 2 , pp. 329-342
    • Mackintosh, C.1
  • 38
    • 0142151385 scopus 로고    scopus 로고
    • Overcoming technical variation and biological variation in quantitative proteomics
    • Molloy MP, Brzezinski EE, Hang JQ, McDowell MT, VanBogelen RA. 2003. Overcoming technical variation and biological variation in quantitative proteomics. Proteomics 3(10):1912-1919.
    • (2003) Proteomics , vol.3 , Issue.10 , pp. 1912-1919
    • Molloy, M.P.1    Brzezinski, E.E.2    Hang, J.Q.3    McDowell, M.T.4    Vanbogelen, R.A.5
  • 40
    • 0842345408 scopus 로고    scopus 로고
    • On the origin of intracellular compartmentation and organized metabolic systems
    • Ovadi J, Saks V. 2004. On the origin of intracellular compartmentation and organized metabolic systems. Mol Cell Biochem 256-257(1-2):5-12.
    • (2004) Mol Cell Biochem , vol.256-257 , Issue.1-2 , pp. 5-12
    • Ovadi, J.1    Saks, V.2
  • 41
    • 3042710591 scopus 로고    scopus 로고
    • Regulation of cytoskeletal dynamics by actin-monomer-binding proteins
    • Paavilainen VO, Bertling E, Falck S, Lappalainen P. 2004. Regulation of cytoskeletal dynamics by actin-monomer-binding proteins. Trends Cell Biol 14(7):386-394.
    • (2004) Trends Cell Biol , vol.14 , Issue.7 , pp. 386-394
    • Paavilainen, V.O.1    Bertling, E.2    Falck, S.3    Lappalainen, P.4
  • 42
    • 0037338297 scopus 로고    scopus 로고
    • Data analysis - The Achilles heel of proteomics
    • Patterson SD. 2003. Data analysis-The Achilles heel of proteomics. Nat Biotechnol 21(3):221-222.
    • (2003) Nat Biotechnol , vol.21 , Issue.3 , pp. 221-222
    • Patterson, S.D.1
  • 43
    • 10744224197 scopus 로고    scopus 로고
    • Development of human protein reference database as an initial platform for approaching systems biology in humans
    • Peri S, Navarro JD, Amanchy R, et al. 2003. Development of human protein reference database as an initial platform for approaching systems biology in humans. Genome Res 13:2363-2371.
    • (2003) Genome Res , vol.13 , pp. 2363-2371
    • Peri, S.1    Navarro, J.D.2    Amanchy, R.3
  • 45
    • 0041312686 scopus 로고    scopus 로고
    • 14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase
    • Pozuelo Rubio M, Peggie M, Wong BH, Morrice N, MacKintosh C. 2003. 14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase. EMBO J 22(14):3514-3523.
    • (2003) EMBO J , vol.22 , Issue.14 , pp. 3514-3523
    • Pozuelo Rubio, M.1    Peggie, M.2    Wong, B.H.3    Morrice, N.4    MacKintosh, C.5
  • 46
    • 2342651419 scopus 로고    scopus 로고
    • 14-3-3-Affmity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking
    • Pozuelo Rubio M, Geraghty KM, Wong BH, Wood NT, Campbell DG, Morrice N, Mackintosh C. 2004. 14-3-3-affmity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking. Biochem J 379(2):395-408.
    • (2004) Biochem J , vol.379 , Issue.2 , pp. 395-408
    • Pozuelo Rubio, M.1    Geraghty, K.M.2    Wong, B.H.3    Wood, N.T.4    Campbell, D.G.5    Morrice, N.6    Mackintosh, C.7
  • 48
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: Coping with stress
    • Rutkowski DT, Kaufman RJ. 2004. A trip to the ER: Coping with stress. Trends Cell Biol 14(1):20-28.
    • (2004) Trends Cell Biol , vol.14 , Issue.1 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 50
    • 13544259722 scopus 로고    scopus 로고
    • On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells
    • Schlatter S, Stansfield SH, Dinnis DM, Racher AJ, Birch JR, James DC. 2005. On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells. Biotechnol Prog 21(1):122-133.
    • (2005) Biotechnol Prog , vol.21 , Issue.1 , pp. 122-133
    • Schlatter, S.1    Stansfield, S.H.2    Dinnis, D.M.3    Racher, A.J.4    Birch, J.R.5    James, D.C.6
  • 52
    • 13544265458 scopus 로고    scopus 로고
    • Modeling hybridoma cell metabolism using a generic genome-scale metabolic model of Mus musculus
    • Sheikh K, Forster J, Nielsen LK. 2005. Modeling hybridoma cell metabolism using a generic genome-scale metabolic model of Mus musculus. Biotechnol Prog 21:112-121.
    • (2005) Biotechnol Prog , vol.21 , pp. 112-121
    • Sheikh, K.1    Forster, J.2    Nielsen, L.K.3
  • 54
    • 33644872577 scopus 로고    scopus 로고
    • Limma: Linear models for microarray data, chapter 23
    • Gentleman R, Carey V, Dudoit S, Irizarry W, Huber W, editors. New York: Springer
    • Smyth GK. 2005. Limma: Linear models for microarray data, chapter 23. In: Gentleman R, Carey V, Dudoit S, Irizarry W, Huber W, editors. Bioinformatics and Computational Biology Solutions using R and Bioconductor. New York: Springer. p 397-420.
    • (2005) Bioinformatics and Computational Biology Solutions Using R and Bioconductor , pp. 397-420
    • Smyth, G.K.1
  • 55
    • 5444222234 scopus 로고    scopus 로고
    • XBP1: A link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum
    • Sriburi R, Jackowski S, Mori K, Brewer JW. 2004. XBP1: A link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum. J Cell Biol 167(1):35-41.
    • (2004) J Cell Biol , vol.167 , Issue.1 , pp. 35-41
    • Sriburi, R.1    Jackowski, S.2    Mori, K.3    Brewer, J.W.4
  • 56
    • 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(4):428-433.
    • (2002) Curr Opin Cell Biol , vol.14 , Issue.4 , pp. 428-433
    • Stamnes, M.1
  • 57
    • 0030868980 scopus 로고    scopus 로고
    • Efficient mammalian protein synthesis requires an intact F-actin system
    • Stapulionis R, Kolli S, Deutscher MP. 1997. Efficient mammalian protein synthesis requires an intact F-actin system. J Biol Chem 272(40):24980-24986.
    • (1997) J Biol Chem , vol.272 , Issue.40 , pp. 24980-24986
    • Stapulionis, R.1    Kolli, S.2    Deutscher, M.P.3
  • 58
    • 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(2):263-279.
    • (1999) Exp Cell Res , vol.246 , Issue.2 , pp. 263-279
    • Thyberg, J.1    Moskalewski, S.2
  • 59
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, Walter P. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101(3):249-258.
    • (2000) Cell , vol.101 , Issue.3 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 60
    • 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(1):9-17.
    • (1998) Eur J Cell Biol , vol.76 , Issue.1 , pp. 9-17
    • Valderrama, F.1    Babia, T.2    Ayala, I.3    Kok, J.W.4    Renau-Piqueras, J.5    Egea, G.6
  • 62
    • 0037332128 scopus 로고    scopus 로고
    • Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion
    • van Anken E, Romijn EP, Maggioni C, Mezghrani A, Sitia R, Braakman I, Heck AJ. 2003. Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity 18(2):243-253.
    • (2003) Immunity , vol.18 , Issue.2 , pp. 243-253
    • Van Anken, E.1    Romijn, E.P.2    Maggioni, C.3    Mezghrani, A.4    Sitia, R.5    Braakman, I.6    Heck, A.J.7
  • 63
    • 0029092245 scopus 로고
    • Effect of ATP depletion and DTT on the transport of membrane proteins from the endoplasmic reticulum and the intermediate compartment to the Golgi complex
    • Verde C, Pascale MC, Martire G, Lotti LV, Torrisi MR, Helenius A, Bonatti S. 1995. Effect of ATP depletion and DTT on the transport of membrane proteins from the endoplasmic reticulum and the intermediate compartment to the Golgi complex. Eur J Cell Biol 67(3):267-274.
    • (1995) Eur J Cell Biol , vol.67 , Issue.3 , pp. 267-274
    • Verde, C.1    Pascale, M.C.2    Martire, G.3    Lotti, L.V.4    Torrisi, M.R.5    Helenius, A.6    Bonatti, S.7
  • 64
    • 0037009130 scopus 로고    scopus 로고
    • Molecular chaperones as essential mediators of mitochondrial biogenesis
    • Voos W, Rottgers K. 2002. Molecular chaperones as essential mediators of mitochondrial biogenesis. Biochim Biophys Acta 1592(1):51-62.
    • (2002) Biochim Biophys Acta , vol.1592 , Issue.1 , pp. 51-62
    • Voos, W.1    Rottgers, K.2
  • 65
    • 0027405024 scopus 로고
    • Hsc70, immunoglobulin heavy chain binding protein, and Hsp90 differ in their ability to stimulate transport of precursor proteins into mammalian microsomes
    • Wiech H, Buchner J, Zimmermann M, Zimmermann R, Jakob U. 1993. Hsc70, immunoglobulin heavy chain binding protein, and Hsp90 differ in their ability to stimulate transport of precursor proteins into mammalian microsomes. J Biol Chem 268(10):7414-7421.
    • (1993) J Biol Chem , vol.268 , Issue.10 , pp. 7414-7421
    • Wiech, H.1    Buchner, J.2    Zimmermann, M.3    Zimmermann, R.4    Jakob, U.5
  • 66
    • 9144228073 scopus 로고    scopus 로고
    • Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II
    • Yamamoto K, Yoshida H, Kokame K, Kaufman RJ, Mori K. 2004. Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II. J Biochem (Tokyo) 136(3):343-350.
    • (2004) J Biochem (Tokyo) , vol.136 , Issue.3 , pp. 343-350
    • Yamamoto, K.1    Yoshida, H.2    Kokame, K.3    Kaufman, R.J.4    Mori, K.5
  • 67
    • 13244273546 scopus 로고    scopus 로고
    • Kinesin, walking, crawling or sliding along?
    • Yildiz A, Selvin PR. 2005. Kinesin, walking, crawling or sliding along? Trends Cell Biol 15(2):112-120.
    • (2005) Trends Cell Biol , vol.15 , Issue.2 , pp. 112-120
    • Yildiz, A.1    Selvin, P.R.2
  • 68
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: Localized functions of cytosolic chaperones
    • Young JC, Barral JM, Ulrich Hartl F. 2003. More than folding: Localized functions of cytosolic chaperones. Trends Biochem Sci 28(10):541-547.
    • (2003) Trends Biochem Sci , vol.28 , Issue.10 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Ulrich Hartl, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.