메뉴 건너뛰기




Volumn 122, Issue 18, 2009, Pages 3322-3329

An intrinsic quality-control mechanism ensures unconventional secretion of fibroblast growth factor 2 in a folded conformation

Author keywords

FGF2; Fibroblast growth factor 2; Membrane translocation; Non classical export; Protein folding; Quality control; Unconventional protein secretion

Indexed keywords

FIBROBLAST GROWTH FACTOR 2;

EID: 70350400642     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.049791     Document Type: Article
Times cited : (34)

References (59)
  • 2
    • 0032923377 scopus 로고    scopus 로고
    • The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles
    • Andrei, C., Dazzi, C., Lotti, L., Torrisi, M. R., Chimini, G. and Rubartelli, A. (1999). The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles. Mol. Biol. Cell 10, 1463-1475.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1463-1475
    • Andrei, C.1    Dazzi, C.2    Lotti, L.3    Torrisi, M.R.4    Chimini, G.5    Rubartelli, A.6
  • 3
    • 3042800587 scopus 로고    scopus 로고
    • Phospholipases C and A2 control lysosome-mediated IL-1 beta secretion: Implications for inflammatory processes
    • Andrei, C., Margiocco, P., Poggi, A., Lotti, L. V., Torrisi, M. R. and Rubartelli, A. (2004). Phospholipases C and A2 control lysosome-mediated IL-1 beta secretion: Implications for inflammatory processes. Proc. Natl. Acad. Sci. USA 101, 9745-9750.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9745-9750
    • Andrei, C.1    Margiocco, P.2    Poggi, A.3    Lotti, L.V.4    Torrisi, M.R.5    Rubartelli, A.6
  • 4
    • 19644375795 scopus 로고    scopus 로고
    • Peptide signaling during terminal differentiation of Dictyostelium
    • Anjard, C. and Loomis, W. F. (2005). Peptide signaling during terminal differentiation of Dictyostelium. Proc. Natl. Acad. Sci. USA 102, 7607-7611.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7607-7611
    • Anjard, C.1    Loomis, W.F.2
  • 5
    • 33745609759 scopus 로고    scopus 로고
    • GABA induces terminal differentiation of Dictyostelium through a GABAB receptor
    • Anjard, C. and Loomis, W. F. (2006). GABA induces terminal differentiation of Dictyostelium through a GABAB receptor. Development 133, 2253-2261.
    • (2006) Development , vol.133 , pp. 2253-2261
    • Anjard, C.1    Loomis, W.F.2
  • 6
    • 2342443941 scopus 로고    scopus 로고
    • Unconventional protein secretion: Membrane translocation of FGF-2 does not require protein unfolding
    • Backhaus, R., Zehe, C., Wegehingel, S., Kehlenbach, A., Schwappach, B. and Nickel, W. (2004). Unconventional protein secretion: membrane translocation of FGF-2 does not require protein unfolding. J. Cell Sci. 117, 1727-1736.
    • (2004) J. Cell Sci , vol.117 , pp. 1727-1736
    • Backhaus, R.1    Zehe, C.2    Wegehingel, S.3    Kehlenbach, A.4    Schwappach, B.5    Nickel, W.6
  • 7
    • 0028608099 scopus 로고
    • The stability and unfolding of an IgG binding protein based upon the B domain of protein A from Staphylococcus aureus probed by tryptophan substitution and fluorescence spectroscopy
    • Bottomley, S. P., Popplewell, A. G., Scawen, M., Wan, T., Sutton, B. J. and Gore, M. G. (1994). The stability and unfolding of an IgG binding protein based upon the B domain of protein A from Staphylococcus aureus probed by tryptophan substitution and fluorescence spectroscopy. Protein Eng. 7, 1463-1470.
    • (1994) Protein Eng , vol.7 , pp. 1463-1470
    • Bottomley, S.P.1    Popplewell, A.G.2    Scawen, M.3    Wan, T.4    Sutton, B.J.5    Gore, M.G.6
  • 8
    • 0031002736 scopus 로고    scopus 로고
    • Protein transports: The nonclassical ins and outs
    • Cleves, A. E. (1997). Protein transports: the nonclassical ins and outs. Curr. Biol. 7, R318-R320.
    • (1997) Curr. Biol , vol.7
    • Cleves, A.E.1
  • 9
    • 56349086943 scopus 로고    scopus 로고
    • Plastid protein import and sorting: Different paths to the same compartments
    • Cline, K. and Dabney-Smith, C. (2008). Plastid protein import and sorting: different paths to the same compartments. Curr. Opin. Plant Biol. 11, 585-592.
    • (2008) Curr. Opin. Plant Biol , vol.11 , pp. 585-592
    • Cline, K.1    Dabney-Smith, C.2
  • 10
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution
    • Deisenhofer, J. (1981). Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution. Biochemistry 20, 2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 11
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • Eilers, M. and Schatz, G. (1986). Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature 322, 228-232.
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 12
    • 0028017537 scopus 로고
    • Chloroplast protein import. Chloroplast envelopes and thylakoids have different abilities to unfold proteins
    • Endo, T., Kawakami, M., Goto, A., America, T., Weisbeek, P. and Nakai, M. (1994). Chloroplast protein import. Chloroplast envelopes and thylakoids have different abilities to unfold proteins. Eur. J. Biochem. 225, 403-409.
    • (1994) Eur. J. Biochem , vol.225 , pp. 403-409
    • Endo, T.1    Kawakami, M.2    Goto, A.3    America, T.4    Weisbeek, P.5    Nakai, M.6
  • 14
    • 0029866647 scopus 로고    scopus 로고
    • Heparin structure and interactions with basic fibroblast growth factor
    • Faham, S., Hileman, R. E., Fromm, J. R., Linhardt, R. J. and Rees, D. C. (1996). Heparin structure and interactions with basic fibroblast growth factor. Science 271, 1116-1120.
    • (1996) Science , vol.271 , pp. 1116-1120
    • Faham, S.1    Hileman, R.E.2    Fromm, J.R.3    Linhardt, R.J.4    Rees, D.C.5
  • 15
    • 0031733974 scopus 로고    scopus 로고
    • Diversity does make a difference: Fibroblast growth factor-heparin interactions
    • Faham, S., Linhardt, R. J. and Rees, D. C. (1998). Diversity does make a difference: fibroblast growth factor-heparin interactions. Curr. Opin. Struct. Biol. 8, 578-586.
    • (1998) Curr. Opin. Struct. Biol , vol.8 , pp. 578-586
    • Faham, S.1    Linhardt, R.J.2    Rees, D.C.3
  • 16
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson, K. M., Lemmon, M. A., Schlessinger, J. and Sigler, P. B. (1995). Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83, 1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 17
    • 0028939001 scopus 로고
    • Quantitative export of FGF-2 occurs through an alternative, energy-dependent, non-ER/Golgi pathway
    • Florkiewicz, R. Z., Majack, R. A., Buechler, R. D. and Florkiewicz, E. (1995). Quantitative export of FGF-2 occurs through an alternative, energy-dependent, non-ER/Golgi pathway. J. Cell Physiol. 162, 388-399.
    • (1995) J. Cell Physiol , vol.162 , pp. 388-399
    • Florkiewicz, R.Z.1    Majack, R.A.2    Buechler, R.D.3    Florkiewicz, E.4
  • 18
    • 0027674916 scopus 로고
    • A strong protein unfolding activity is associated with the binding of precursor chloroplast proteins to chloroplast envelopes
    • Guera, A., America, T., van Waas, M. and Weisbeek, P. J. (1993). A strong protein unfolding activity is associated with the binding of precursor chloroplast proteins to chloroplast envelopes. Plant Mol. Biol. 23, 309-324.
    • (1993) Plant Mol. Biol , vol.23 , pp. 309-324
    • Guera, A.1    America, T.2    van Waas, M.3    Weisbeek, P.J.4
  • 19
    • 0032714092 scopus 로고    scopus 로고
    • Secretion of the galectin family of mammalian carbohydrate-binding proteins
    • Hughes, R. C. (1999). Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim. Biophys. Acta 1473, 172-185.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 172-185
    • Hughes, R.C.1
  • 20
    • 46249121083 scopus 로고    scopus 로고
    • Protein trafficking to plastids: One theme, many variations
    • Inaba, T. and Schnell, D. J. (2008). Protein trafficking to plastids: one theme, many variations. Biochem. J. 413, 15-28.
    • (2008) Biochem. J , vol.413 , pp. 15-28
    • Inaba, T.1    Schnell, D.J.2
  • 21
    • 0037067133 scopus 로고    scopus 로고
    • Toc, tic, and chloroplast protein import
    • Jarvis, P. and Soll, J. (2002). Toc, tic, and chloroplast protein import. Biochim. Biophys. Acta 1590, 177-189.
    • (2002) Biochim. Biophys. Acta , vol.1590 , pp. 177-189
    • Jarvis, P.1    Soll, J.2
  • 22
    • 0030964379 scopus 로고    scopus 로고
    • X-ray structure of the 154-amino-acid form of recombinant human basic fibroblast growth factor. comparison with the truncated 146-amino-acid form
    • Kastrup, J. S., Eriksson, E. S., Dalboge, H. and Flodgaard, H. (1997). X-ray structure of the 154-amino-acid form of recombinant human basic fibroblast growth factor. comparison with the truncated 146-amino-acid form. Acta Crystallogr. D Biol. Crystallogr. 53, 160-168.
    • (1997) Acta Crystallogr. D Biol. Crystallogr , vol.53 , pp. 160-168
    • Kastrup, J.S.1    Eriksson, E.S.2    Dalboge, H.3    Flodgaard, H.4
  • 23
    • 39749084641 scopus 로고    scopus 로고
    • Active caspase-1 is a regulator of unconventional protein secretion
    • Keller, M., Ruegg, A., Werner, S. and Beer, H. D. (2008). Active caspase-1 is a regulator of unconventional protein secretion. Cell 132, 818-831.
    • (2008) Cell , vol.132 , pp. 818-831
    • Keller, M.1    Ruegg, A.2    Werner, S.3    Beer, H.D.4
  • 24
    • 34547604776 scopus 로고    scopus 로고
    • The Golgi-associated protein GRASP is required for unconventional protein secretion during development
    • Kinseth, M. A., Anjard, C., Fuller, D., Guizzunti, G., Loomis, W. F. and Malhotra, V. (2007). The Golgi-associated protein GRASP is required for unconventional protein secretion during development. Cell 130, 524-534.
    • (2007) Cell , vol.130 , pp. 524-534
    • Kinseth, M.A.1    Anjard, C.2    Fuller, D.3    Guizzunti, G.4    Loomis, W.F.5    Malhotra, V.6
  • 25
    • 34247192598 scopus 로고    scopus 로고
    • Further in vivo studies on the role of the molecular chaperone, Hsp93, in plastid protein import
    • Kovacheva, S., Bedard, J., Wardle, A., Patel, R. and Jarvis, P. (2007). Further in vivo studies on the role of the molecular chaperone, Hsp93, in plastid protein import. Plant J. 50, 364-379.
    • (2007) Plant J , vol.50 , pp. 364-379
    • Kovacheva, S.1    Bedard, J.2    Wardle, A.3    Patel, R.4    Jarvis, P.5
  • 26
    • 33750381048 scopus 로고    scopus 로고
    • The bacterial twin-arginine translocation pathway
    • Lee, P. A., Tullman-Ercek, D. and Georgiou, G. (2006). The bacterial twin-arginine translocation pathway. Annu. Rev. Microbiol. 60, 373-395.
    • (2006) Annu. Rev. Microbiol , vol.60 , pp. 373-395
    • Lee, P.A.1    Tullman-Ercek, D.2    Georgiou, G.3
  • 27
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M. A. (2008). Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell Biol. 9, 99-111.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 28
    • 33845318489 scopus 로고    scopus 로고
    • Uniqueness of the mechanism of protein import into the peroxisome matrix: Transport of folded, co-factor-bound and oligomeric proteins by shuttling receptors
    • Leon, S., Goodman, J. M. and Subramani, S. (2006). Uniqueness of the mechanism of protein import into the peroxisome matrix: transport of folded, co-factor-bound and oligomeric proteins by shuttling receptors. Biochim. Biophys. Acta 1763, 1552-1564.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1552-1564
    • Leon, S.1    Goodman, J.M.2    Subramani, S.3
  • 31
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert, W. and Herrmann, J. M. (2007). Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76, 723-749.
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 32
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion
    • Nickel, W. (2003). The mystery of nonclassical protein secretion. Eur. J. Biochem. 270, 2109-2119.
    • (2003) Eur. J. Biochem , vol.270 , pp. 2109-2119
    • Nickel, W.1
  • 33
    • 21844468743 scopus 로고    scopus 로고
    • Unconventional secretory routes: Direct protein export across the plasma membrane of Mammalian cells
    • Nickel, W. (2005). Unconventional secretory routes: direct protein export across the plasma membrane of Mammalian cells. Traffic 6, 607-614.
    • (2005) Traffic , vol.6 , pp. 607-614
    • Nickel, W.1
  • 34
    • 34547743839 scopus 로고    scopus 로고
    • Unconventional secretion: An extracellular trap for export of fibroblast growth factor 2
    • Nickel, W. (2007). Unconventional secretion: an extracellular trap for export of fibroblast growth factor 2. J. Cell Sci. 120, 2295-2299.
    • (2007) J. Cell Sci , vol.120 , pp. 2295-2299
    • Nickel, W.1
  • 35
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • Nickel, W. and Rabouille, C. (2009). Mechanisms of regulated unconventional protein secretion. Nat. Rev. Mol. Cell Biol. 10, 148-155.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 36
    • 55849145075 scopus 로고    scopus 로고
    • Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells
    • Nickel, W. and Seedorf, M. (2008). Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells. Annu. Rev. Cell Dev. Biol. 24, 287-308.
    • (2008) Annu. Rev. Cell Dev. Biol , vol.24 , pp. 287-308
    • Nickel, W.1    Seedorf, M.2
  • 38
    • 0026355460 scopus 로고
    • Synthesis and mutagenesis of an IgG-binding protein based upon protein A of Staphylococcus aureus
    • Popplewell, A. G., Gore, M. G., Scawen, M. and Atkinson, T. (1991). Synthesis and mutagenesis of an IgG-binding protein based upon protein A of Staphylococcus aureus. Protein Eng. 4, 963-970.
    • (1991) Protein Eng , vol.4 , pp. 963-970
    • Popplewell, A.G.1    Gore, M.G.2    Scawen, M.3    Atkinson, T.4
  • 39
    • 0037157841 scopus 로고    scopus 로고
    • The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export
    • Prudovsky, I., Bagala, C., Tarantini, F., Mandinova, A., Soldi, R., Bellum, S. and Maciag, T. (2002). The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export. J. Cell Biol. 158, 201-208.
    • (2002) J. Cell Biol , vol.158 , pp. 201-208
    • Prudovsky, I.1    Bagala, C.2    Tarantini, F.3    Mandinova, A.4    Soldi, R.5    Bellum, S.6    Maciag, T.7
  • 42
    • 34548614009 scopus 로고    scopus 로고
    • Nonclassical IL-1 beta secretion stimulated by P2X7 receptors is dependent on inflammasome activation and correlated with exosome release in murine macrophages
    • Qu, Y., Franchi, L., Nunez, G. and Dubyak, G. R. (2007). Nonclassical IL-1 beta secretion stimulated by P2X7 receptors is dependent on inflammasome activation and correlated with exosome release in murine macrophages. J. Immunol. 179, 1913-1925.
    • (2007) J. Immunol , vol.179 , pp. 1913-1925
    • Qu, Y.1    Franchi, L.2    Nunez, G.3    Dubyak, G.R.4
  • 44
  • 45
    • 0025255629 scopus 로고
    • A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence
    • Rubartelli, A., Cozzolino, F., Talio, M. and Sitia, R. (1990). A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence. EMBO J. 9, 1503-1510.
    • (1990) EMBO J , vol.9 , pp. 1503-1510
    • Rubartelli, A.1    Cozzolino, F.2    Talio, M.3    Sitia, R.4
  • 46
    • 36749045913 scopus 로고    scopus 로고
    • The twin-arginine transport system: Moving folded proteins across membranes
    • Sargent, F. (2007). The twin-arginine transport system: moving folded proteins across membranes. Biochem. Soc. Trans. 35, 835-847.
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 835-847
    • Sargent, F.1
  • 47
    • 1342325441 scopus 로고    scopus 로고
    • Unconventional secretion of fibroblast growth factor 2 is mediated by direct translocation across the plasma membrane of mammalian cells
    • Schäfer, T., Zentgraf, H., Zehe, C., Brügger, B., Bernhagen, J. and Nickel, W. (2004). Unconventional secretion of fibroblast growth factor 2 is mediated by direct translocation across the plasma membrane of mammalian cells. J. Biol. Chem. 279, 6244-6251.
    • (2004) J. Biol. Chem , vol.279 , pp. 6244-6251
    • Schäfer, T.1    Zentgraf, H.2    Zehe, C.3    Brügger, B.4    Bernhagen, J.5    Nickel, W.6
  • 48
    • 27544483286 scopus 로고    scopus 로고
    • Cell surface counter receptors are essential components of the unconventional export machinery of galectin-1
    • Seelenmeyer, C., Wegehingel, S., Tews, I., Kunzler, M., Aebi, M. and Nickel, W. (2005). Cell surface counter receptors are essential components of the unconventional export machinery of galectin-1. J. Cell Biol. 171, 373-381.
    • (2005) J. Cell Biol , vol.171 , pp. 373-381
    • Seelenmeyer, C.1    Wegehingel, S.2    Tews, I.3    Kunzler, M.4    Aebi, M.5    Nickel, W.6
  • 49
    • 0030872950 scopus 로고    scopus 로고
    • The cell adhesion molecule DdCAD-1 in Dictyostelium is targeted to the cell surface by a nonclassical transport pathway involving contractile vacuoles
    • Sesaki, H., Wong, E. F. and Siu, C. H. (1997). The cell adhesion molecule DdCAD-1 in Dictyostelium is targeted to the cell surface by a nonclassical transport pathway involving contractile vacuoles. J. Cell Biol. 138, 939-951.
    • (1997) J. Cell Biol , vol.138 , pp. 939-951
    • Sesaki, H.1    Wong, E.F.2    Siu, C.H.3
  • 50
    • 1542374116 scopus 로고    scopus 로고
    • Protein import into chloroplasts
    • Soll, J. and Schleiff, E. (2004). Protein import into chloroplasts. Nat. Rev. Mol. Cell Biol. 5, 198-208.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 198-208
    • Soll, J.1    Schleiff, E.2
  • 51
    • 0029131806 scopus 로고
    • Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins
    • Tashiro, M. and Montelione, G. T. (1995). Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins. Curr. Opin. Struct. Biol. 5, 471-481.
    • (1995) Curr. Opin. Struct. Biol , vol.5 , pp. 471-481
    • Tashiro, M.1    Montelione, G.T.2
  • 52
    • 46349098379 scopus 로고    scopus 로고
    • A direct role for phosphatidylinositol-4,5-bisphosphate in unconventional secretion of fibroblast growth factor 2
    • Temmerman, K., Ebert, A. D., Muller, H. M., Sinning, I., Tews, I. and Nickel, W. (2008). A direct role for phosphatidylinositol-4,5-bisphosphate in unconventional secretion of fibroblast growth factor 2. Traffic 9, 1204-1217.
    • (2008) Traffic , vol.9 , pp. 1204-1217
    • Temmerman, K.1    Ebert, A.D.2    Muller, H.M.3    Sinning, I.4    Tews, I.5    Nickel, W.6
  • 53
    • 67649844238 scopus 로고    scopus 로고
    • A novel flow cytometric assay to quantify interactions between proteins and membrane lipids
    • Temmerman, K. and Nickel, W. (2009). A novel flow cytometric assay to quantify interactions between proteins and membrane lipids. J. Lipid Res. 50, 1245-1254.
    • (2009) J. Lipid Res , vol.50 , pp. 1245-1254
    • Temmerman, K.1    Nickel, W.2
  • 54
    • 0033795350 scopus 로고    scopus 로고
    • Translocation of FGF2 to the cell surface without release into conditioned media
    • In Process Citation
    • Trudel, C., Faure-Desire, V., Florkiewicz, R. Z. and Baird, A. (2000). Translocation of FGF2 to the cell surface without release into conditioned media [In Process Citation]. J. Cell Physiol. 185, 260-268.
    • (2000) J. Cell Physiol , vol.185 , pp. 260-268
    • Trudel, C.1    Faure-Desire, V.2    Florkiewicz, R.Z.3    Baird, A.4
  • 55
    • 0030043099 scopus 로고    scopus 로고
    • Ricin A chain fused to a chloroplast-targeting signal is unfolded on the chloroplast surface prior to import across the envelope membranes
    • Walker, D., Chaddock, A. M., Chaddock, J. A., Roberts, L. M., Lord, J. M. and Robinson, C. (1996). Ricin A chain fused to a chloroplast-targeting signal is unfolded on the chloroplast surface prior to import across the envelope membranes. J. Biol. Chem. 271, 4082-4085.
    • (1996) J. Biol. Chem , vol.271 , pp. 4082-4085
    • Walker, D.1    Chaddock, A.M.2    Chaddock, J.A.3    Roberts, L.M.4    Lord, J.M.5    Robinson, C.6
  • 56
    • 0030845899 scopus 로고    scopus 로고
    • Perturbation of the antigen-binding site and staphylococcal protein A-binding site of IgG before significant changes in global conformation during denaturation: An equilibrium study
    • Wang, X. D., Luo, J., Guo, Z. Q., Zhou, J. M. and Tsou, C. L. (1997). Perturbation of the antigen-binding site and staphylococcal protein A-binding site of IgG before significant changes in global conformation during denaturation: an equilibrium study. Biochem. J. 325, 707-710.
    • (1997) Biochem. J , vol.325 , pp. 707-710
    • Wang, X.D.1    Luo, J.2    Guo, Z.Q.3    Zhou, J.M.4    Tsou, C.L.5
  • 57
    • 45549099915 scopus 로고    scopus 로고
    • Rerouting of fibroblast growth factor 2 to the classical secretory pathway results in post-translational modifications that block binding to heparan sulfate proteoglycans
    • Wegehingel, S., Zehe, C. and Nickel, W. (2008). Rerouting of fibroblast growth factor 2 to the classical secretory pathway results in post-translational modifications that block binding to heparan sulfate proteoglycans. FEBS Lett. 582, 2387-2392.
    • (2008) FEBS Lett , vol.582 , pp. 2387-2392
    • Wegehingel, S.1    Zehe, C.2    Nickel, W.3
  • 59
    • 33750299160 scopus 로고    scopus 로고
    • Cell-surface heparan sulfate proteoglycans are essential components of the unconventional export machinery of FGF-2
    • Zehe, C., Engling, A., Wegehingel, S., Schäfer, T. and Nickel, W. (2006). Cell-surface heparan sulfate proteoglycans are essential components of the unconventional export machinery of FGF-2. Proc. Natl. Acad. Sci. USA 103, 15479-15484.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15479-15484
    • Zehe, C.1    Engling, A.2    Wegehingel, S.3    Schäfer, T.4    Nickel, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.