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Volumn 10, Issue 10, 2009, Pages 1405-1413

The role of galectins in protein trafficking

Author keywords

Apical trafficking; Galectin; Non classical secretion; Protein clustering

Indexed keywords

GALECTIN; GALECTIN 3; GALECTIN 4; GLYCOPROTEIN; LECTIN; LIPID;

EID: 70350428098     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2009.00960.x     Document Type: Review
Times cited : (131)

References (77)
  • 2
    • 33645080188 scopus 로고    scopus 로고
    • Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum
    • Williams DB. Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J Cell Sci 2006, 119:615-623.
    • (2006) J Cell Sci , vol.119 , pp. 615-623
    • Williams, D.B.1
  • 4
    • 0028810337 scopus 로고
    • N-glycans as apical sorting signals in epithelial cells
    • Scheiffele P, Peranen J, Simons K. N-glycans as apical sorting signals in epithelial cells. Nature 1995, 378:96-98.
    • (1995) Nature , vol.378 , pp. 96-98
    • Scheiffele, P.1    Peranen, J.2    Simons, K.3
  • 5
    • 0033519624 scopus 로고    scopus 로고
    • O-linked glycans mediate apical sorting of human intestinal sucrase- isomaltase through association with lipid rafts
    • Alfalah M, Jacob R, Preuss U, Zimmer KP, Naim H, Naim HY. O-linked glycans mediate apical sorting of human intestinal sucrase- isomaltase through association with lipid rafts. Curr Biol 1999, 9:593-596.
    • (1999) Curr Biol , vol.9 , pp. 593-596
    • Alfalah, M.1    Jacob, R.2    Preuss, U.3    Zimmer, K.P.4    Naim, H.5    Naim, H.Y.6
  • 7
    • 0034734041 scopus 로고    scopus 로고
    • Lectins and traffic in the secretory pathway
    • Hauri H, Appenzeller C, Kuhn F, Nufer O. Lectins and traffic in the secretory pathway. FEBS Lett 2000, 476:32-37.
    • (2000) FEBS Lett , vol.476 , pp. 32-37
    • Hauri, H.1    Appenzeller, C.2    Kuhn, F.3    Nufer, O.4
  • 11
    • 0037383848 scopus 로고    scopus 로고
    • Polarized epithelial membrane traffic: conservation and plasticity
    • Mostov K, Su T, ter Beest M. Polarized epithelial membrane traffic: conservation and plasticity. Nat Cell Biol 2003, 5:287-293.
    • (2003) Nat Cell Biol , vol.5 , pp. 287-293
    • Mostov, K.1    Su, T.2    ter Beest, M.3
  • 12
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. Functional rafts in cell membranes. Nature 1997, 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 13
  • 14
    • 0035908953 scopus 로고    scopus 로고
    • Apical membrane proteins are transported in distinct vesicular carriers
    • Jacob R, Naim HY. Apical membrane proteins are transported in distinct vesicular carriers. Curr Biol 2001, 11:1444-1450.
    • (2001) Curr Biol , vol.11 , pp. 1444-1450
    • Jacob, R.1    Naim, H.Y.2
  • 16
    • 0029053448 scopus 로고
    • The role of N-glycans in the secretory pathway
    • Fiedler K, Simons K. The role of N-glycans in the secretory pathway. Cell 1995, 81:309-312.
    • (1995) Cell , vol.81 , pp. 309-312
    • Fiedler, K.1    Simons, K.2
  • 18
    • 0027478019 scopus 로고
    • Ricin-resistant Madin-Darby canine kidney cells missort a major endogenous apical sialoglycoprotein
    • Le Bivic A, Garcia M, Rodriguez-Boulan E. Ricin-resistant Madin-Darby canine kidney cells missort a major endogenous apical sialoglycoprotein. J Biol Chem 1993, 268:6909-6916.
    • (1993) J Biol Chem , vol.268 , pp. 6909-6916
    • Le Bivic, A.1    Garcia, M.2    Rodriguez-Boulan, E.3
  • 19
    • 0030051122 scopus 로고    scopus 로고
    • Characterization of VIP36, an animal lectin homologous to leguminous lectins
    • Fiedler K, Simons K. Characterization of VIP36, an animal lectin homologous to leguminous lectins. J Cell Sci 1996, 109:271-276.
    • (1996) J Cell Sci , vol.109 , pp. 271-276
    • Fiedler, K.1    Simons, K.2
  • 20
    • 0032879945 scopus 로고    scopus 로고
    • VIP36 localisation to the early secretory pathway
    • Fullekrug J, Scheiffele P, Simons K. VIP36 localisation to the early secretory pathway. J Cell Sci 1999, 112:2813-2821.
    • (1999) J Cell Sci , vol.112 , pp. 2813-2821
    • Fullekrug, J.1    Scheiffele, P.2    Simons, K.3
  • 21
    • 0001619084 scopus 로고    scopus 로고
    • VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells
    • Cheong KH, Zacchetti D, Schneeberger EE, Simons K. VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells. Proc Natl Acad Sci U S A 1999, 96:6241-6248.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6241-6248
    • Cheong, K.H.1    Zacchetti, D.2    Schneeberger, E.E.3    Simons, K.4
  • 22
    • 0345683542 scopus 로고    scopus 로고
    • The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin- Darby canine kidney cells
    • Puertollano R, Martin-Belmonte F, Millan J, de Marco MC, Albar JP, Kremer L, Alonso MA. The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin- Darby canine kidney cells. J Cell Biol 1999, 145:141-151.
    • (1999) J Cell Biol , vol.145 , pp. 141-151
    • Puertollano, R.1    Martin-Belmonte, F.2    Millan, J.3    de Marco, M.C.4    Albar, J.P.5    Kremer, L.6    Alonso, M.A.7
  • 26
    • 0037136417 scopus 로고    scopus 로고
    • Principles of structures of animal and plant lectins
    • Loris R. Principles of structures of animal and plant lectins. Biochim Biophys Acta 2002, 1572:198-208.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 198-208
    • Loris, R.1
  • 27
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent beta-galactoside-binding lectins: structure, function and molecular evolution
    • Hirabayashi J, Kasai K. The family of metazoan metal-independent beta-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology 1993, 3:297-304.
    • (1993) Glycobiology , vol.3 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 28
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: finding themes in complexity
    • Cooper DN. Galectinomics: finding themes in complexity. Biochim Biophys Acta 2002, 1572:209-231.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.1
  • 31
    • 11144241063 scopus 로고    scopus 로고
    • Galectins as modulators of tumour progression
    • Liu FT, Rabinovich GA. Galectins as modulators of tumour progression. Nat Rev Cancer 2005, 5:29-41.
    • (2005) Nat Rev Cancer , vol.5 , pp. 29-41
    • Liu, F.T.1    Rabinovich, G.A.2
  • 32
    • 1542343883 scopus 로고    scopus 로고
    • Extracellular functions of galectin-3
    • Ochieng J, Furtak V, Lukyanov P. Extracellular functions of galectin-3. Glycoconj J 2004, 19:527-535.
    • (2004) Glycoconj J , vol.19 , pp. 527-535
    • Ochieng, J.1    Furtak, V.2    Lukyanov, P.3
  • 33
    • 20444419772 scopus 로고    scopus 로고
    • Galectins as immunoregulators during infectious processes: from microbial invasion to the resolution of the disease
    • Rabinovich GA, Gruppi A. Galectins as immunoregulators during infectious processes: from microbial invasion to the resolution of the disease. Parasite Immunol 2005, 27:103-114.
    • (2005) Parasite Immunol , vol.27 , pp. 103-114
    • Rabinovich, G.A.1    Gruppi, A.2
  • 34
    • 0037300960 scopus 로고    scopus 로고
    • Galectins in cell growth and apoptosis
    • Yang RY, Liu FT. Galectins in cell growth and apoptosis. Cell Mol Life Sci 2003, 60:267-276.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 267-276
    • Yang, R.Y.1    Liu, F.T.2
  • 36
    • 0027965708 scopus 로고
    • Galectins. Structure and function of a large family of animal lectins.
    • Barondes SH, Cooper DN, Gitt MA, Leffler H. Galectins. Structure and function of a large family of animal lectins. J Biol Chem 1994, 269:20807-20810.
    • (1994) J Biol Chem , vol.269 , pp. 20807-20810
    • Barondes, S.H.1    Cooper, D.N.2    Gitt, M.A.3    Leffler, H.4
  • 37
    • 4444329794 scopus 로고    scopus 로고
    • Thermodynamic binding studies of bivalent oligosaccharides to galectin-1, galectin-3, and the carbohydrate recognition domain of galectin-3
    • Ahmad N, Gabius HJ, Sabesan S, Oscarson S, Brewer CF. Thermodynamic binding studies of bivalent oligosaccharides to galectin-1, galectin-3, and the carbohydrate recognition domain of galectin-3. Glycobiology 2004, 14:817-825.
    • (2004) Glycobiology , vol.14 , pp. 817-825
    • Ahmad, N.1    Gabius, H.J.2    Sabesan, S.3    Oscarson, S.4    Brewer, C.F.5
  • 38
    • 0028986609 scopus 로고
    • Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization.
    • Cho M, Cummings RD. Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization. J Biol Chem 1995, 270:5198-5206.
    • (1995) J Biol Chem , vol.270 , pp. 5198-5206
    • Cho, M.1    Cummings, R.D.2
  • 39
    • 0000594001 scopus 로고    scopus 로고
    • Role of the carboxyl-terminal lectin domain in self-association of galectin-3
    • Yang RY, Hill PN, Hsu DK, Liu FT. Role of the carboxyl-terminal lectin domain in self-association of galectin-3. Biochemistry 1998, 37:4086-4092.
    • (1998) Biochemistry , vol.37 , pp. 4086-4092
    • Yang, R.Y.1    Hill, P.N.2    Hsu, D.K.3    Liu, F.T.4
  • 40
    • 0028225890 scopus 로고
    • Structure of baby hamster kidney carbohydrate-binding protein CBP30, an S-type animal lectin
    • Mehul B, Bawumia S, Martin SR, Hughes RC. Structure of baby hamster kidney carbohydrate-binding protein CBP30, an S-type animal lectin. J Biol Chem 1994, 269:18250-18258.
    • (1994) J Biol Chem , vol.269 , pp. 18250-18258
    • Mehul, B.1    Bawumia, S.2    Martin, S.R.3    Hughes, R.C.4
  • 41
    • 0026770786 scopus 로고
    • Biochemical and biophysical characterization of human recombinant IgE-binding protein, an S-type animal lectin
    • Hsu DK, Zuberi RI, Liu FT. Biochemical and biophysical characterization of human recombinant IgE-binding protein, an S-type animal lectin. J Biol Chem 1992, 267:14167-14174.
    • (1992) J Biol Chem , vol.267 , pp. 14167-14174
    • Hsu, D.K.1    Zuberi, R.I.2    Liu, F.T.3
  • 42
    • 0035901521 scopus 로고    scopus 로고
    • NMR solution studies of hamster galectin-3 and electron microscopic visualization of surface-adsorbed complexes: evidence for interactions between the N- and C-terminal domains
    • Birdsall B, Feeney J, Burdett ID, Bawumia S, Barboni EA, Hughes RC. NMR solution studies of hamster galectin-3 and electron microscopic visualization of surface-adsorbed complexes: evidence for interactions between the N- and C-terminal domains. Biochemistry 2001, 40:4859-4866.
    • (2001) Biochemistry , vol.40 , pp. 4859-4866
    • Birdsall, B.1    Feeney, J.2    Burdett, I.D.3    Bawumia, S.4    Barboni, E.A.5    Hughes, R.C.6
  • 43
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions
    • Brewer CF, Miceli MC, Baum LG. Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions. Curr Opin Struct Biol 2002, 12:616-623.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 44
    • 0037844879 scopus 로고    scopus 로고
    • Microvillar membrane microdomains exist at physiological temperature. Role of galectin-4 as lipid raft stabilizer revealed by " superrafts" .
    • Braccia A, Villani M, Immerdal L, Niels-Christiansen LL, Nystrom BT, Hansen GH, Danielsen EM. Microvillar membrane microdomains exist at physiological temperature. Role of galectin-4 as lipid raft stabilizer revealed by " superrafts" . J Biol Chem 2003, 278:15679-15684.
    • (2003) J Biol Chem , vol.278 , pp. 15679-15684
    • Braccia, A.1    Villani, M.2    Immerdal, L.3    Niels-Christiansen, L.L.4    Nystrom, B.T.5    Hansen, G.H.6    Danielsen, E.M.7
  • 45
    • 14244257721 scopus 로고    scopus 로고
    • Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells
    • Ideo H, Seko A, Yamashita K. Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells. J Biol Chem 2005, 280:4730-4737.
    • (2005) J Biol Chem , vol.280 , pp. 4730-4737
    • Ideo, H.1    Seko, A.2    Yamashita, K.3
  • 47
    • 56149095414 scopus 로고    scopus 로고
    • Apical cargo traverses endosomal compartments on the passage to the cell surface
    • Cramm-Behrens CI, Dienst M, Jacob R. Apical cargo traverses endosomal compartments on the passage to the cell surface. Traffic 2008, 9:2206-2220.
    • (2008) Traffic , vol.9 , pp. 2206-2220
    • Cramm-Behrens, C.I.1    Dienst, M.2    Jacob, R.3
  • 48
    • 0030726211 scopus 로고    scopus 로고
    • The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells
    • Yeaman C, Le Gall AH, Baldwin AN, Monlauzeur L, Le Bivic A, Rodriguez-Boulan E. The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells. J Cell Biol 1997, 139:929-940.
    • (1997) J Cell Biol , vol.139 , pp. 929-940
    • Yeaman, C.1    Le Gall, A.H.2    Baldwin, A.N.3    Monlauzeur, L.4    Le Bivic, A.5    Rodriguez-Boulan, E.6
  • 49
    • 0036061463 scopus 로고    scopus 로고
    • Role of the membrane-proximal O-glycosylation site in sorting of the human receptor for neurotrophins to the apical membrane of MDCK cells
    • Breuza L, Garcia M, Delgrossi MH, Le Bivic A. Role of the membrane-proximal O-glycosylation site in sorting of the human receptor for neurotrophins to the apical membrane of MDCK cells. Exp Cell Res 2002, 273:178-186.
    • (2002) Exp Cell Res , vol.273 , pp. 178-186
    • Breuza, L.1    Garcia, M.2    Delgrossi, M.H.3    Le Bivic, A.4
  • 50
    • 0033179221 scopus 로고    scopus 로고
    • Glycans in post-Golgi apical targeting: sorting signals or structural props?
    • Rodriguez-Boulan E, Gonzalez A. Glycans in post-Golgi apical targeting: sorting signals or structural props?. Trends Cell Biol 1999, 9:291-294.
    • (1999) Trends Cell Biol , vol.9 , pp. 291-294
    • Rodriguez-Boulan, E.1    Gonzalez, A.2
  • 52
    • 0031949975 scopus 로고    scopus 로고
    • Embryonic implantation in galectin 1/galectin 3 double mutant mice
    • Colnot C, Fowlis D, Ripoche MA, Bouchaert I, Poirier F. Embryonic implantation in galectin 1/galectin 3 double mutant mice. Dev Dyn 1998, 211:306-313.
    • (1998) Dev Dyn , vol.211 , pp. 306-313
    • Colnot, C.1    Fowlis, D.2    Ripoche, M.A.3    Bouchaert, I.4    Poirier, F.5
  • 53
    • 0024360758 scopus 로고
    • The sequence of the mouse 14 kDa beta-galactoside-binding lectin and evidence for its synthesis on free cytoplasmic ribosomes
    • Wilson TJ, Firth MN, Powell JT, Harrison FL. The sequence of the mouse 14 kDa beta-galactoside-binding lectin and evidence for its synthesis on free cytoplasmic ribosomes. Biochem J 1989, 261:847-852.
    • (1989) Biochem J , vol.261 , pp. 847-852
    • Wilson, T.J.1    Firth, M.N.2    Powell, J.T.3    Harrison, F.L.4
  • 54
    • 0025335432 scopus 로고
    • Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism
    • Cooper DN, Barondes SH. Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism. J Cell Biol 1990, 110:1681-1691.
    • (1990) J Cell Biol , vol.110 , pp. 1681-1691
    • Cooper, D.N.1    Barondes, S.H.2
  • 55
    • 0026519309 scopus 로고
    • The 14 kDa beta-galactoside binding lectin in myoblast and myotube cultures: localization by confocal microscopy
    • Harrison FL, Wilson TJ. The 14 kDa beta-galactoside binding lectin in myoblast and myotube cultures: localization by confocal microscopy. J Cell Sci 1992, 101:635-646.
    • (1992) J Cell Sci , vol.101 , pp. 635-646
    • Harrison, F.L.1    Wilson, T.J.2
  • 56
    • 0030994878 scopus 로고    scopus 로고
    • Plasma membrane targetting, vesicular budding and release of galectin 3 from the cytoplasm of mammalian cells during secretion
    • Mehul B, Hughes RC. Plasma membrane targetting, vesicular budding and release of galectin 3 from the cytoplasm of mammalian cells during secretion. J Cell Sci 1997, 110:1169-1178.
    • (1997) J Cell Sci , vol.110 , pp. 1169-1178
    • Mehul, B.1    Hughes, R.C.2
  • 57
    • 0035877018 scopus 로고    scopus 로고
    • Proteomic analysis of dendritic cell-derived exosomes: a secreted subcellular compartment distinct from apoptotic vesicles
    • Thery C, Boussac M, Veron P, Ricciardi-Castagnoli P, Raposo G, Garin J, Amigorena S. Proteomic analysis of dendritic cell-derived exosomes: a secreted subcellular compartment distinct from apoptotic vesicles. J Immunol 2001, 166:7309-7318.
    • (2001) J Immunol , vol.166 , pp. 7309-7318
    • Thery, C.1    Boussac, M.2    Veron, P.3    Ricciardi-Castagnoli, P.4    Raposo, G.5    Garin, J.6    Amigorena, S.7
  • 59
    • 33846864645 scopus 로고    scopus 로고
    • Exosomes released by EBV-infected nasopharyngeal carcinoma cells convey the viral latent membrane protein 1 and the immunomodulatory protein galectin 9
    • Keryer-Bibens C, Pioche-Durieu C, Villemant C, Souquere S, Nishi N, Hirashima M, Middeldorp J, Busson P. Exosomes released by EBV-infected nasopharyngeal carcinoma cells convey the viral latent membrane protein 1 and the immunomodulatory protein galectin 9. BMC Cancer 2006, 6:283.
    • (2006) BMC Cancer , vol.6 , pp. 283
    • Keryer-Bibens, C.1    Pioche-Durieu, C.2    Villemant, C.3    Souquere, S.4    Nishi, N.5    Hirashima, M.6    Middeldorp, J.7    Busson, P.8
  • 60
    • 27744588938 scopus 로고    scopus 로고
    • Galectin-3 interacts with membrane lipids and penetrates the lipid bilayer
    • Lukyanov P, Furtak V, Ochieng J. Galectin-3 interacts with membrane lipids and penetrates the lipid bilayer. Biochem Biophys Res Commun 2005, 338:1031-1036.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 1031-1036
    • Lukyanov, P.1    Furtak, V.2    Ochieng, J.3
  • 61
    • 1342325441 scopus 로고    scopus 로고
    • Unconventional secretion of fibroblast growth factor 2 is mediated by direct translocation across the plasma membrane of mammalian cells
    • Schafer T, Zentgraf H, Zehe C, Brugger B, Bernhagen J, Nickel W. Unconventional secretion of fibroblast growth factor 2 is mediated by direct translocation across the plasma membrane of mammalian cells. J Biol Chem 2004, 279:6244-6251.
    • (2004) J Biol Chem , vol.279 , pp. 6244-6251
    • Schafer, T.1    Zentgraf, H.2    Zehe, C.3    Brugger, B.4    Bernhagen, J.5    Nickel, W.6
  • 62
    • 0027212532 scopus 로고
    • Apical secretion of a cytosolic protein by Madin-Darby canine kidney cells. Evidence for polarized release of an endogenous lectin by a nonclassical secretory pathway.
    • Lindstedt R, Apodaca G, Barondes SH, Mostov KE, Leffler H. Apical secretion of a cytosolic protein by Madin-Darby canine kidney cells. Evidence for polarized release of an endogenous lectin by a nonclassical secretory pathway. J Biol Chem 1993, 268:11750-11757.
    • (1993) J Biol Chem , vol.268 , pp. 11750-11757
    • Lindstedt, R.1    Apodaca, G.2    Barondes, S.H.3    Mostov, K.E.4    Leffler, H.5
  • 63
    • 0030000860 scopus 로고    scopus 로고
    • A new pathway for protein export in Saccharomyces cerevisiae
    • Cleves AE, Cooper DN, Barondes SH, Kelly RB. A new pathway for protein export in Saccharomyces cerevisiae. J Cell Biol 1996, 133:1017-1026.
    • (1996) J Cell Biol , vol.133 , pp. 1017-1026
    • Cleves, A.E.1    Cooper, D.N.2    Barondes, S.H.3    Kelly, R.B.4
  • 64
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons K, Wandinger-Ness A. Polarized sorting in epithelia. Cell 1990, 62:207-210.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 65
    • 30744445427 scopus 로고    scopus 로고
    • Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death
    • Stillman BN, Hsu DK, Pang M, Brewer CF, Johnson P, Liu FT, Baum LG. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death. J Immunol 2006, 176:778-789.
    • (2006) J Immunol , vol.176 , pp. 778-789
    • Stillman, B.N.1    Hsu, D.K.2    Pang, M.3    Brewer, C.F.4    Johnson, P.5    Liu, F.T.6    Baum, L.G.7
  • 66
    • 0033230170 scopus 로고    scopus 로고
    • Export of galectin-3 from nuclei of digitonin-permeabilized mouse 3T3 fibroblasts
    • Tsay YG, Lin NY, Voss PG, Patterson RJ, Wang JL. Export of galectin-3 from nuclei of digitonin-permeabilized mouse 3T3 fibroblasts. Exp Cell Res 1999, 252:250-261.
    • (1999) Exp Cell Res , vol.252 , pp. 250-261
    • Tsay, Y.G.1    Lin, N.Y.2    Voss, P.G.3    Patterson, R.J.4    Wang, J.L.5
  • 67
    • 0033199579 scopus 로고    scopus 로고
    • Determinants in the N-terminal domains of galectin-3 for secretion by a novel pathway circumventing the endoplasmic reticulum-Golgi complex
    • Menon RP, Hughes RC. Determinants in the N-terminal domains of galectin-3 for secretion by a novel pathway circumventing the endoplasmic reticulum-Golgi complex. Eur J Biochem 1999, 264:569-576.
    • (1999) Eur J Biochem , vol.264 , pp. 569-576
    • Menon, R.P.1    Hughes, R.C.2
  • 68
    • 33750558541 scopus 로고    scopus 로고
    • Characterization of the nuclear import pathways of galectin-3
    • Nakahara S, Oka N, Wang Y, Hogan V, Inohara H, Raz A. Characterization of the nuclear import pathways of galectin-3. Cancer Res 2006, 66:9995-10006.
    • (2006) Cancer Res , vol.66 , pp. 9995-10006
    • Nakahara, S.1    Oka, N.2    Wang, Y.3    Hogan, V.4    Inohara, H.5    Raz, A.6
  • 69
    • 0030952080 scopus 로고    scopus 로고
    • Strikingly different localization of galectin-3 and galectin-4 in human colon adenocarcinoma T84 cells. Galectin-4 is localized at sites of cell adhesion.
    • Huflejt ME, Jordan ET, Gitt MA, Barondes SH, Leffler H. Strikingly different localization of galectin-3 and galectin-4 in human colon adenocarcinoma T84 cells. Galectin-4 is localized at sites of cell adhesion. J Biol Chem 1997, 272:14294-14303.
    • (1997) J Biol Chem , vol.272 , pp. 14294-14303
    • Huflejt, M.E.1    Jordan, E.T.2    Gitt, M.A.3    Barondes, S.H.4    Leffler, H.5
  • 70
    • 34548736515 scopus 로고    scopus 로고
    • Intracellular sorting of galectin-8 based on carbohydrate fine specificity
    • Carlsson S, Carlsson MC, Leffler H. Intracellular sorting of galectin-8 based on carbohydrate fine specificity. Glycobiology 2007, 17:906-912.
    • (2007) Glycobiology , vol.17 , pp. 906-912
    • Carlsson, S.1    Carlsson, M.C.2    Leffler, H.3
  • 71
    • 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, Nickel W. Cell surface counter receptors are essential components of the unconventional export machinery of galectin-1. J Cell Biol 2005, 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
  • 72
    • 23944500772 scopus 로고    scopus 로고
    • C2-symmetrical thiodigalactoside bis-benzamido derivatives as high-affinity inhibitors of galectin-3: efficient lectin inhibition through double arginine-arene interactions
    • Cumpstey I, Sundin A, Leffler H, Nilsson UJ. C2-symmetrical thiodigalactoside bis-benzamido derivatives as high-affinity inhibitors of galectin-3: efficient lectin inhibition through double arginine-arene interactions. Angew Chem Int Ed Engl 2005, 44:5110-5112.
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 5110-5112
    • Cumpstey, I.1    Sundin, A.2    Leffler, H.3    Nilsson, U.J.4
  • 73
    • 20644448817 scopus 로고    scopus 로고
    • 3-(1,2,3-Triazol-1-yl)-1-thio-galactosides as small, efficient, and hydrolytically stable inhibitors of galectin-3
    • Salameh BA, Leffler H, Nilsson UJ. 3-(1,2,3-Triazol-1-yl)-1-thio-galactosides as small, efficient, and hydrolytically stable inhibitors of galectin-3. Bioorg Med Chem Lett 2005, 15:3344-3346.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 3344-3346
    • Salameh, B.A.1    Leffler, H.2    Nilsson, U.J.3
  • 74
    • 30344486680 scopus 로고    scopus 로고
    • Thioureido N-acetyllactosamine derivatives as potent galectin-7 and 9N inhibitors
    • Salameh BA, Sundin A, Leffler H, Nilsson UJ. Thioureido N-acetyllactosamine derivatives as potent galectin-7 and 9N inhibitors. Bioorg Med Chem 2006, 14:1215-1220.
    • (2006) Bioorg Med Chem , vol.14 , pp. 1215-1220
    • Salameh, B.A.1    Sundin, A.2    Leffler, H.3    Nilsson, U.J.4
  • 75
    • 17244375741 scopus 로고    scopus 로고
    • Synthesis of O-galactosyl aldoximes as potent LacNAc-mimetic galectin-3 inhibitors
    • Tejler J, Leffler H, Nilsson UJ. Synthesis of O-galactosyl aldoximes as potent LacNAc-mimetic galectin-3 inhibitors. Bioorg Med Chem Lett 2005, 15:2343-2345.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 2343-2345
    • Tejler, J.1    Leffler, H.2    Nilsson, U.J.3
  • 76
    • 33646946320 scopus 로고    scopus 로고
    • Synthesis of multivalent lactose derivatives by 1,3-dipolar cycloadditions: selective galectin-1 inhibition
    • Tejler J, Tullberg E, Frejd T, Leffler H, Nilsson UJ. Synthesis of multivalent lactose derivatives by 1,3-dipolar cycloadditions: selective galectin-1 inhibition. Carbohydr Res 2006, 341:1353-1362.
    • (2006) Carbohydr Res , vol.341 , pp. 1353-1362
    • Tejler, J.1    Tullberg, E.2    Frejd, T.3    Leffler, H.4    Nilsson, U.J.5
  • 77
    • 34447315866 scopus 로고    scopus 로고
    • Synthesis of galactose-mimicking 1H-(1,2,3-triazol-1-yl)-mannosides as selective galectin-3 and 9N inhibitors
    • Tejler J, Skogman F, Leffler H, Nilsson UJ. Synthesis of galactose-mimicking 1H-(1,2,3-triazol-1-yl)-mannosides as selective galectin-3 and 9N inhibitors. Carbohydr Res 2007, 342:1869-1875.
    • (2007) Carbohydr Res , vol.342 , pp. 1869-1875
    • Tejler, J.1    Skogman, F.2    Leffler, H.3    Nilsson, U.J.4


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