메뉴 건너뛰기




Volumn , Issue , 2008, Pages 9-31

Galectins and Their Functions in Plain Language

Author keywords

"neat" lectins and glycosylated lectins; Galectins galactose binding lectins; Galectins natural and artificial ligands

Indexed keywords


EID: 84859510271     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470378076.ch2     Document Type: Chapter
Times cited : (16)

References (59)
  • 1
    • 0024971391 scopus 로고
    • Specificity of ribosome-inactivating proteins with RNA N-glycosidase activity
    • Stirpe F, Hudges RC. Specificity of ribosome-inactivating proteins with RNA N-glycosidase activity. Biochem J 1989;262:1001-1002.
    • (1989) Biochem J , vol.262 , pp. 1001-1002
    • Stirpe, F.1    Hudges, R.C.2
  • 3
    • 0037177882 scopus 로고    scopus 로고
    • Charcot-Leyden crystal protein (galectin-10) is not a dual-function galectin with lysophospholipase activity, but binds a lysophospholipase inhibitor in a novel structural fashion
    • Ackerman SJ, Liu L, Kwatia MA, Savage MP, Leonidas DD, Swaminathan GJ, Acharya KR. Charcot-Leyden crystal protein (galectin-10) is not a dual-function galectin with lysophospholipase activity, but binds a lysophospholipase inhibitor in a novel structural fashion. J Biol Chem 2002;277:14859-14868.
    • (2002) J Biol Chem , vol.277 , pp. 14859-14868
    • Ackerman, S.J.1    Liu, L.2    Kwatia, M.A.3    Savage, M.P.4    Leonidas, D.D.5    Swaminathan, G.J.6    Acharya, K.R.7
  • 5
    • 0032875554 scopus 로고    scopus 로고
    • God must love galectins; He made so many of them
    • Cooper DNW, Barondes SH. God must love galectins; He made so many of them. Glycobiology 1999;9:979-984.
    • (1999) Glycobiology , vol.9 , pp. 979-984
    • Cooper, D.N.W.1    Barondes, S.H.2
  • 7
    • 0029900083 scopus 로고    scopus 로고
    • Expression of galectin-3 modulates T-cell growth and apoptosis
    • Yang RY, Hsu DK, Liu F-T. Expression of galectin-3 modulates T-cell growth and apoptosis. Proc Natl Acad Sci USA 1996;93 (13):6737-6742.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.13 , pp. 6737-6742
    • Yang, R.Y.1    Hsu, D.K.2    Liu, F.-T.3
  • 8
    • 0033215424 scopus 로고    scopus 로고
    • Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by galectin-1
    • Pace KE, Lee C, Stewart PL, Baum LG. Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by galectin-1. J Immunol 1999;163:3801-3811.
    • (1999) J Immunol , vol.163 , pp. 3801-3811
    • Pace, K.E.1    Lee, C.2    Stewart, P.L.3    Baum, L.G.4
  • 9
    • 0033517113 scopus 로고    scopus 로고
    • Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis
    • Rabinovich GA, Daly G, Dreja H, Tailor H, Riera CM, Hirabayashi J, Chernajovsky Y. Recombinant galectin-1 and its genetic delivery suppress collagen-induced arthritis via T cell apoptosis. J Exp Med 1999;190 (3):385-398.
    • (1999) J Exp Med , vol.190 , Issue.3 , pp. 385-398
    • Rabinovich, G.A.1    Daly, G.2    Dreja, H.3    Tailor, H.4    Riera, C.M.5    Hirabayashi, J.6    Chernajovsky, Y.7
  • 10
    • 0034267915 scopus 로고    scopus 로고
    • Cutting edge: CD7 delivers a proapoptotic signal during galectin-1-induced T cell death
    • Pace KE, Hahn HP, Pang M, Nguyen JT, Baum LG. Cutting edge: CD7 delivers a proapoptotic signal during galectin-1-induced T cell death. J Immunol 2000;165:2331-2334.
    • (2000) J Immunol , vol.165 , pp. 2331-2334
    • Pace, K.E.1    Hahn, H.P.2    Pang, M.3    Nguyen, J.T.4    Baum, L.G.5
  • 12
    • 0028986607 scopus 로고
    • Galectin-1, a beta-galactose-binding lectin in Chinese hamster ovary cells. II. Localization and biosynthesis
    • Cho M, Cummings RD. Galectin-1, a beta-galactose-binding lectin in Chinese hamster ovary cells. II. Localization and biosynthesis. J Biol Chem 1995;270:5207-5212.
    • (1995) J Biol Chem , vol.270 , pp. 5207-5212
    • Cho, M.1    Cummings, R.D.2
  • 13
    • 0028986609 scopus 로고
    • Galectin-1, a beta-galactose-binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization
    • Cho M, Cummings RD. Galectin-1, a beta-galactose-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
  • 16
    • 0027485050 scopus 로고
    • Normal development of mice carrying a null mutation in the gene encoding the L 14 S-type lectin
    • Poirier F, Robertson EJ. Normal development of mice carrying a null mutation in the gene encoding the L 14 S-type lectin. Development 1993;119:1229-1236.
    • (1993) Development , vol.119 , pp. 1229-1236
    • Poirier, F.1    Robertson, E.J.2
  • 17
    • 0031668035 scopus 로고    scopus 로고
    • Expression of galectins-1 in the mouse olfactory system
    • Tenne-Brown J, Puche AC, Key B. Expression of galectins-1 in the mouse olfactory system. Int J Dev Biol 1998;42:791-799.
    • (1998) Int J Dev Biol , vol.42 , pp. 791-799
    • Tenne-Brown, J.1    Puche, A.C.2    Key, B.3
  • 19
    • 0033870111 scopus 로고    scopus 로고
    • Targeted disruption of the galectin-3 gene results in attenuated peritoneal inflammatory responses
    • Hsu DK, Yang R-Y, Pan Z, Yu L, Salomon DR, Fung-Leung W-P, Liu F-T. Targeted disruption of the galectin-3 gene results in attenuated peritoneal inflammatory responses. Am J Pathol 2000;156:1073-1083.
    • (2000) Am J Pathol , vol.156 , pp. 1073-1083
    • Hsu, D.K.1    Yang, R.-Y.2    Pan, Z.3    Yu, L.4    Salomon, D.R.5    Fung-Leung, W.-P.6    Liu, F.-T.7
  • 21
    • 0033862317 scopus 로고    scopus 로고
    • Glycosylated nuclear lectin CBP70 also associated with endoplasmic reticulum and the Golgi apparatus: does the ''classic pathway'' of glycosylation also apply to nuclear glycoproteins?
    • Rousseau C, Muriel MP, Musset M, Botti J, Seve AP. Glycosylated nuclear lectin CBP70 also associated with endoplasmic reticulum and the Golgi apparatus: does the ''classic pathway'' of glycosylation also apply to nuclear glycoproteins? J Cell Biochem 2000;78: 638-649.
    • (2000) J Cell Biochem , vol.78 , pp. 638-649
    • Rousseau, C.1    Muriel, M.P.2    Musset, M.3    Botti, J.4    Seve, A.P.5
  • 23
    • 0034090403 scopus 로고    scopus 로고
    • Stable expression of functional CBP70 lectin during heat shock
    • Rousseau C, Felin M, Seve AP. Stable expression of functional CBP70 lectin during heat shock. J Cell Biochem 2000;77:615-623.
    • (2000) J Cell Biochem , vol.77 , pp. 615-623
    • Rousseau, C.1    Felin, M.2    Seve, A.P.3
  • 24
    • 0025165935 scopus 로고
    • Analysis of nuclear sugar-binding components in undifferentiated and in vitro differentiated human promyelocytic leukemia cells (HL60)
    • Facy P, Seve AP, Hubert M, Monsigny M, Hubert J. Analysis of nuclear sugar-binding components in undifferentiated and in vitro differentiated human promyelocytic leukemia cells (HL60)Exp Cell Res 1990;190:151-160.
    • (1990) Exp Cell Res , vol.190 , pp. 151-160
    • Facy, P.1    Seve, A.P.2    Hubert, M.3    Monsigny, M.4    Hubert, J.5
  • 26
    • 0035890905 scopus 로고    scopus 로고
    • Identification of N-acetyl-D-glucosamine-specific lectins from rat liver cytosolic and nuclear compartments as heat-shock proteins
    • Lefebvre T, Cieniewski C, Lemoine J, Guerardel Y, Leroy Y, Zanetta JP, Michalski JC. Identification of N-acetyl-D-glucosamine-specific lectins from rat liver cytosolic and nuclear compartments as heat-shock proteins. Biochem J 2001;360:179-188.
    • (2001) Biochem J , vol.360 , pp. 179-188
    • Lefebvre, T.1    Cieniewski, C.2    Lemoine, J.3    Guerardel, Y.4    Leroy, Y.5    Zanetta, J.P.6    Michalski, J.C.7
  • 27
    • 0038495795 scopus 로고    scopus 로고
    • Sugar-dependent nuclear import of glycosylated proteins in living cells
    • Rondanino C, Bousser M-T, Monsigny M, Roche A-C. Sugar-dependent nuclear import of glycosylated proteins in living cells. Glycobiology 2003;13 (7):509-519.
    • (2003) Glycobiology , vol.13 , Issue.7 , pp. 509-519
    • Rondanino, C.1    Bousser, M.-T.2    Monsigny, M.3    Roche, A.-C.4
  • 28
    • 29444443797 scopus 로고    scopus 로고
    • Modulation of HSP70 GlcNAc-directed lectin activity by glucose availability and utilization
    • Guinez C, Losfeld M-E, Cacan R, Michalski J-C, Lefebvre T. Modulation of HSP70 GlcNAc-directed lectin activity by glucose availability and utilization. Glycobiology 2006;16:22-28.
    • (2006) Glycobiology , vol.16 , pp. 22-28
    • Guinez, C.1    Losfeld, M.-E.2    Cacan, R.3    Michalski, J.-C.4    Lefebvre, T.5
  • 30
    • 0020961932 scopus 로고
    • Purification and characterization of two new soluble placental tissue proteins (PP13 and PP17)
    • Bohn H, Kraus W, Winckler W. Purification and characterization of two new soluble placental tissue proteins (PP13 and PP17). Oncodev Biol Med 1983;4:343-350.
    • (1983) Oncodev Biol Med , vol.4 , pp. 343-350
    • Bohn, H.1    Kraus, W.2    Winckler, W.3
  • 31
    • 0035863454 scopus 로고    scopus 로고
    • Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation
    • Tinari N, Kuwabara I, Huflejt ME, Shen PF, Iacobelli S, Liu F-T. Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation. Int J Cancer 2000;91:167-172.
    • (2000) Int J Cancer , vol.91 , pp. 167-172
    • Tinari, N.1    Kuwabara, I.2    Huflejt, M.E.3    Shen, P.F.4    Iacobelli, S.5    Liu, F.-T.6
  • 32
    • 0029942555 scopus 로고    scopus 로고
    • Galectin-3 promotes adhesion of human neutrophils to laminin
    • Kuwabara I, Liu F-T. Galectin-3 promotes adhesion of human neutrophils to laminin. J Immunol 1996;156:3939-3944.
    • (1996) J Immunol , vol.156 , pp. 3939-3944
    • Kuwabara, I.1    Liu, F.-T.2
  • 33
    • 0029759376 scopus 로고    scopus 로고
    • Interactions between galectin-3 and Mac-2- binding protein mediate cell-cell adhesion
    • Inohara H, Akahani S, Koths K, Raz A. Interactions between galectin-3 and Mac-2- binding protein mediate cell-cell adhesion. Cancer Res 1996;56:4530-4534.
    • (1996) Cancer Res , vol.56 , pp. 4530-4534
    • Inohara, H.1    Akahani, S.2    Koths, K.3    Raz, A.4
  • 34
    • 0035929631 scopus 로고    scopus 로고
    • Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3
    • Kopitz J, von Reitzenstein C, Andre S, Kaltner H, Uhl J, Ehemann V, Cantz M, Gabius H-J. Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3. J Biol Chem 2001;276:35917-35923.
    • (2001) J Biol Chem , vol.276 , pp. 35917-35923
    • Kopitz, J.1    von Reitzenstein, C.2    Andre, S.3    Kaltner, H.4    Uhl, J.5    Ehemann, V.6    Cantz, M.7    Gabius, H.-J.8
  • 35
    • 0037136412 scopus 로고    scopus 로고
    • Binding and cross-linking properties of galectins
    • Brewer CF. Binding and cross-linking properties of galectins. Biochim Biophys Acta 2002;1572:255-262.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 255-262
    • Brewer, C.F.1
  • 36
    • 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 H-J, 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
  • 37
    • 1642483757 scopus 로고    scopus 로고
    • Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes
    • Ahmad N, Gabius H-J, Andre S, Kaltner H, Sabesan S, Roy R, Liu B, Macaluso F, Brewer CF. Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes. J Biol Chem 2004;279 (12):10841-10847.
    • (2004) J Biol Chem , vol.279 , Issue.12 , pp. 10841-10847
    • Ahmad, N.1    Gabius, H.-J.2    Andre, S.3    Kaltner, H.4    Sabesan, S.5    Roy, R.6    Liu, B.7    Macaluso, F.8    Brewer, C.F.9
  • 38
    • 0026757683 scopus 로고
    • Cross-linking activity of the 14-kilodalton b-galactose-specific vertebrate lectin with asialofetuin: comparison with several galactose-specific plant lectins
    • Mandal DK, Brewer CF. Cross-linking activity of the 14-kilodalton b-galactose-specific vertebrate lectin with asialofetuin: comparison with several galactose-specific plant lectins. Biochemistry 1992;31:8465-8472.
    • (1992) Biochemistry , vol.31 , pp. 8465-8472
    • Mandal, D.K.1    Brewer, C.F.2
  • 39
    • 0030445222 scopus 로고    scopus 로고
    • Comparative cross-linking activities of lactose-specific plant and animal lectins and a natural lactose-binding immunoglobulin G fraction from human serum with asialofetuin
    • Gupta D, Kaltner H, Dong X, Gabius H-J, Brewer CF. Comparative cross-linking activities of lactose-specific plant and animal lectins and a natural lactose-binding immunoglobulin G fraction from human serum with asialofetuin. Glycobiology 1996;6:843-849.
    • (1996) Glycobiology , vol.6 , pp. 843-849
    • Gupta, D.1    Kaltner, H.2    Dong, X.3    Gabius, H.-J.4    Brewer, C.F.5
  • 40
    • 13844256109 scopus 로고    scopus 로고
    • Peptides specific to the galectin-3 carbohydrate recognition domain inhibit metastasis-associated cancer cell adhesion
    • Zou J, Glinsky VV, Landon LA, Matthews L, Deutscher SL. Peptides specific to the galectin-3 carbohydrate recognition domain inhibit metastasis-associated cancer cell adhesion. Carcinogenesis 2005;26:309-319.
    • (2005) Carcinogenesis , vol.26 , pp. 309-319
    • Zou, J.1    Glinsky, V.V.2    Landon, L.A.3    Matthews, L.4    Deutscher, S.L.5
  • 41
    • 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, Nillson 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    Nillson, U.J.4
  • 42
    • 33749000292 scopus 로고    scopus 로고
    • Screening for galectin-3 inhibitors from synthetic lacto-Nbiose libraries using microscale affinity chromatography coupled to mass spectrometry
    • Fort S, Kim H-S, Hindsgaul O. Screening for galectin-3 inhibitors from synthetic lacto-Nbiose libraries using microscale affinity chromatography coupled to mass spectrometry. J Org Chem 2006;71:7146-7154.
    • (2006) J Org Chem , vol.71 , pp. 7146-7154
    • Fort, S.1    Kim, H.-S.2    Hindsgaul, O.3
  • 43
    • 0036941828 scopus 로고    scopus 로고
    • Binding free energy calculations of galectin-3-ligand interactions
    • Mandal TK, Mukhopadhyay C. Binding free energy calculations of galectin-3-ligand interactions. Protein Eng 2002;15:979-986.
    • (2002) Protein Eng , vol.15 , pp. 979-986
    • Mandal, T.K.1    Mukhopadhyay, C.2
  • 44
    • 0036668095 scopus 로고    scopus 로고
    • Novel carbohydrate specificity of the 16-kDa galectin from Caenorhabditis elegans: binding to blood group precursor oligosaccharides (type 1, type 2, Ta, and Tb) and gangliosides
    • Ahmed H, Bianchet MA, Amzel LM, Hirabayashi J, Kasai K-I, Giga-Hama Y, Tohda H, Vasta GR. Novel carbohydrate specificity of the 16-kDa galectin from Caenorhabditis elegans: binding to blood group precursor oligosaccharides (type 1, type 2, Ta, and Tb) and gangliosides. Glycobiology 2002;12:451-461.
    • (2002) Glycobiology , vol.12 , pp. 451-461
    • Ahmed, H.1    Bianchet, M.A.2    Amzel, L.M.3    Hirabayashi, J.4    Kasai, K.-I.5    Giga-Hama, Y.6    Tohda, H.7    Vasta, G.R.8
  • 46
    • 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
  • 47
    • 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
  • 48
    • 0036523463 scopus 로고    scopus 로고
    • Low micromolar inhibitors of galectin-3 based on 30-derivatization of N-acetyllactosamine
    • Sörme P, Qian Y, Nyholm P-G, Leffler H, Nilsson UJ. Low micromolar inhibitors of galectin-3 based on 30-derivatization of N-acetyllactosamine. ChemBioChem 2002;3: 183-189.
    • (2002) ChemBioChem , vol.3 , pp. 183-189
    • Sörme, P.1    Qian, Y.2    Nyholm, P.-G.3    Leffler, H.4    Nilsson, U.J.5
  • 50
    • 13644272606 scopus 로고    scopus 로고
    • Structural and thermodynamic studies on galectin-3 in complex with synthetic inhibitors: carbohydrate -protein affinity enhancements through fine-tuning of an arginine-arene interaction
    • Sörme P, Arnoux P, Kahl-Knutsson B, Leffler H, Rini JM, Nilsson UJ. Structural and thermodynamic studies on galectin-3 in complex with synthetic inhibitors: carbohydrate -protein affinity enhancements through fine-tuning of an arginine-arene interaction. J Am Chem Soc 2005;127:1737-1743.
    • (2005) J Am Chem Soc , vol.127 , pp. 1737-1743
    • Sörme, P.1    Arnoux, P.2    Kahl-Knutsson, B.3    Leffler, H.4    Rini, J.M.5    Nilsson, U.J.6
  • 51
    • 0036262673 scopus 로고    scopus 로고
    • High-affinity binding of recombinant human galectin-4 to SO3-!3Galb1!3GalNAc pyranoside
    • Ideo H, Seko A, Ohkura T, Matta KL, Yamashita K. High-affinity binding of recombinant human galectin-4 to SO3-!3Galb1!3GalNAc pyranoside. Glycobiology 2002;12: 199-208.
    • (2002) Glycobiology , vol.12 , pp. 199-208
    • Ideo, H.1    Seko, A.2    Ohkura, T.3    Matta, K.L.4    Yamashita, K.5
  • 52
    • 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
  • 53
    • 0023664406 scopus 로고
    • Multiple soluble b-galactoside-binding lectins from human lung
    • Sparrow CP, Leffler H, Barondes SH. Multiple soluble b-galactoside-binding lectins from human lung. J Biol Chem 1987;262:7383-7390.
    • (1987) J Biol Chem , vol.262 , pp. 7383-7390
    • Sparrow, C.P.1    Leffler, H.2    Barondes, S.H.3
  • 54
    • 0036436051 scopus 로고    scopus 로고
    • Thermodynamic binding studies of cell surface carbohydrate epitopes to galectins-1, -3, and -7: evidence for differential binding specificities
    • Ahmad N, Gabius HJ, Kaltner H, Andre S, Kuwabara I, Liu F-T, Oscarson S, Norberg T, Brewer CF. Thermodynamic binding studies of cell surface carbohydrate epitopes to galectins-1, -3, and -7: evidence for differential binding specificities. Can J Chem 2002;80: 1096-1104.
    • (2002) Can J Chem , vol.80 , pp. 1096-1104
    • Ahmad, N.1    Gabius, H.J.2    Kaltner, H.3    Andre, S.4    Kuwabara, I.5    Liu, F.-T.6    Oscarson, S.7    Norberg, T.8    Brewer, C.F.9
  • 55
    • 0029936281 scopus 로고    scopus 로고
    • Eosinophil Charcot-Leyden crystal protein binds to beta-galactoside sugars
    • Dyer KD, Rosenberg HF. Eosinophil Charcot-Leyden crystal protein binds to beta-galactoside sugars. Life Sci 1996;58:2073-2082.
    • (1996) Life Sci , vol.58 , pp. 2073-2082
    • Dyer, K.D.1    Rosenberg, H.F.2
  • 56
    • 0032574694 scopus 로고    scopus 로고
    • Thermodynamics of bovine spleen galectins-1 binding to disaccharides: correlation with structure and its effect on oligomerization at the denatured temperature
    • Schwarz FP, Ahmed H, Bianchet MA, Amzel LM, Vasta GR. Thermodynamics of bovine spleen galectins-1 binding to disaccharides: correlation with structure and its effect on oligomerization at the denatured temperature. Biochemistry 1998;37: 5867-5877.
    • (1998) Biochemistry , vol.37 , pp. 5867-5877
    • Schwarz, F.P.1    Ahmed, H.2    Bianchet, M.A.3    Amzel, L.M.4    Vasta, G.R.5
  • 57
    • 0022854422 scopus 로고
    • Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian beta-galactosides
    • Leffler H, Barondes SH. Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian beta-galactosides. J Biol Chem 1986;261: 10119-10126.
    • (1986) J Biol Chem , vol.261 , pp. 10119-10126
    • Leffler, H.1    Barondes, S.H.2
  • 58
    • 0036630104 scopus 로고    scopus 로고
    • Terminal alpha-linked galactose rather than N-acetyl lactosamine is ligand for bovine heart galectin-1 in N-linked oligosaccharides of glycoproteins
    • Appukuttan PS. Terminal alpha-linked galactose rather than N-acetyl lactosamine is ligand for bovine heart galectin-1 in N-linked oligosaccharides of glycoproteins. J Mol Recognit 2002;15:180-187.
    • (2002) J Mol Recognit , vol.15 , pp. 180-187
    • Appukuttan, P.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.