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Volumn 5, Issue 3, 2015, Pages 1671-1696

Galectin binding to neo-glycoproteins: LacDiNAc conjugated BSA as ligand for human galectin-3

Author keywords

Chemo enzymatic synthesis; Galectin 3; LacDiNAc; Multivalency; Neo glycoproteins

Indexed keywords

BOVINE SERUM ALBUMIN; GALECTIN; GALECTIN 3; LACDINAC LIGAND; LIGAND; NEOGLYCOPROTEIN; UNCLASSIFIED DRUG; GALECTIN 1; GLYCOPROTEIN; LACTOSE; N-ACETYLGALACTOSAMINYL-1-4-N-ACETYLGLUCOSAMINE; PROTEIN BINDING;

EID: 85012053595     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom5031671     Document Type: Article
Times cited : (44)

References (107)
  • 1
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. Biological roles of oligosaccharides: All of the theories are correct. Glycobiology 1993, 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 3
    • 79960720473 scopus 로고    scopus 로고
    • Glycosylation, galectins and cellular signaling
    • Boscher, C.; Dennis, J.W.; Nabi, I.R. Glycosylation, galectins and cellular signaling. Curr. Opin. Cell Biol. 2011, 23, 383-392.
    • (2011) Curr. Opin. Cell Biol , vol.23 , pp. 383-392
    • Boscher, C.1    Dennis, J.W.2    Nabi, I.R.3
  • 4
    • 0037136412 scopus 로고    scopus 로고
    • Binding and cross-linking properties of galectins
    • Fred Brewer, C. Binding and cross-linking properties of galectins. BBA Gen. Subj. 2002, 1572, 255-262.
    • (2002) BBA Gen. Subj , vol.1572 , pp. 255-262
    • Brewer, F.C.1
  • 5
    • 84920873769 scopus 로고    scopus 로고
    • Galectin-3 in angiogenesis and metastasis
    • Funasaka, T.; Raz, A.; Nangia-Makker, P. Galectin-3 in angiogenesis and metastasis. Glycobiology 2014, 24, 886-891.
    • (2014) Glycobiology , vol.24 , pp. 886-891
    • Funasaka, T.1    Raz, A.2    Nangia-Makker, P.3
  • 6
    • 53049084874 scopus 로고    scopus 로고
    • N-glycans in cancer progression
    • Lau, K.S.; Dennis, J.W. N-glycans in cancer progression. Glycobiology 2008, 18, 750-760.
    • (2008) Glycobiology , vol.18 , pp. 750-760
    • Lau, K.S.1    Dennis, J.W.2
  • 8
    • 85015477850 scopus 로고    scopus 로고
    • Platelets and galectins
    • Schattner, M. Platelets and galectins. Ann. Transl. Med. 2014, 2, doi:10.3978/j.issn.2305-5839.2014.09.02.
    • (2014) Ann. Transl. Med , pp. 2
    • Schattner, M.1
  • 9
    • 0036462602 scopus 로고    scopus 로고
    • The cluster glycoside effect
    • Lundquist, J.J.; Toone, E.J. The cluster glycoside effect. Chem. Rev. 2002, 102, 555-578.
    • (2002) Chem. Rev , vol.102 , pp. 555-578
    • Lundquist, J.J.1    Toone, E.J.2
  • 10
    • 84855933231 scopus 로고    scopus 로고
    • Multivalency in protein-carbohydrate recognition
    • Fraser-Reid, B., Tatsuta, K., Thiem, J., Eds.; Springer: Berlin, Heidelberg, Germany
    • Kiessling, L.L.; Young, T.; Gruber, T.D.; Mortell, K.H. Multivalency in protein-carbohydrate recognition. In Glycoscience; Fraser-Reid, B., Tatsuta, K., Thiem, J., Eds.; Springer: Berlin, Heidelberg, Germany, 2008; pp. 2483-2523.
    • (2008) Glycoscience , pp. 2483-2523
    • Kiessling, L.L.1    Young, T.2    Gruber, T.D.3    Mortell, K.H.4
  • 11
    • 67449085400 scopus 로고    scopus 로고
    • Maximising multivalency effects in protein-carbohydrate interactions
    • Pieters, R.J. Maximising multivalency effects in protein-carbohydrate interactions. Org. Biomol. Chem. 2009, 7, 2013-2025.
    • (2009) Org. Biomol. Chem , vol.7 , pp. 2013-2025
    • Pieters, R.J.1
  • 12
    • 67849089171 scopus 로고    scopus 로고
    • Membrane permeabilization by multivalent anti-microbial peptides
    • Pieters, R.J.; Arnusch, C.J.; Breukink, E. Membrane permeabilization by multivalent anti-microbial peptides. Protein Pept. Lett. 2009, 16, 736-742.
    • (2009) Protein Pept. Lett , vol.16 , pp. 736-742
    • Pieters, R.J.1    Arnusch, C.J.2    Breukink, E.3
  • 14
    • 84876735443 scopus 로고    scopus 로고
    • Clustered carbohydrates in synthetic vaccines
    • Peri, F. Clustered carbohydrates in synthetic vaccines. Chem. Soc. Rev. 2013, 42, 4543-4556.
    • (2013) Chem. Soc. Rev , vol.42 , pp. 4543-4556
    • Peri, F.1
  • 15
    • 84877802168 scopus 로고    scopus 로고
    • Bacterial toxin inhibitors based on multivalent scaffolds
    • Branson, T.R.; Turnbull, W.B. Bacterial toxin inhibitors based on multivalent scaffolds. Chem. Soc. Rev. 2013, 42, 4613-4622.
    • (2013) Chem. Soc. Rev , vol.42 , pp. 4613-4622
    • Branson, T.R.1    Turnbull, W.B.2
  • 16
    • 84877831631 scopus 로고    scopus 로고
    • Multivalent glycoconjugate syntheses and applications using aromatic scaffolds
    • Chabre, Y.M.; Roy, R. Multivalent glycoconjugate syntheses and applications using aromatic scaffolds. Chem. Soc. Rev. 2013, 42, 4657-4708.
    • (2013) Chem. Soc. Rev , vol.42 , pp. 4657-4708
    • Chabre, Y.M.1    Roy, R.2
  • 17
    • 84876702632 scopus 로고    scopus 로고
    • Glyconanoparticles as multifunctional and multimodal carbohydrate systems
    • Marradi, M.; Chiodo, F.; Garcia, I.; Penades, S. Glyconanoparticles as multifunctional and multimodal carbohydrate systems. Chem. Soc. Rev. 2013, 42, 4728-4745.
    • (2013) Chem. Soc. Rev , vol.42 , pp. 4728-4745
    • Marradi, M.1    Chiodo, F.2    Garcia, I.3    Penades, S.4
  • 18
    • 84873971535 scopus 로고    scopus 로고
    • Cyclodextrin-based multivalent glycodisplays: Covalent and supramolecular conjugates to assess carbohydrate-protein interactions
    • Martinez, A.; Ortiz Mellet, C.; Garcia Fernandez, J.M. Cyclodextrin-based multivalent glycodisplays: Covalent and supramolecular conjugates to assess carbohydrate-protein interactions. Chem. Soc. Rev. 2013, 42, 4746-4773.
    • (2013) Chem. Soc. Rev , vol.42 , pp. 4746-4773
    • Martinez, A.1    Ortiz Mellet, C.2    Garcia Fernandez, J.M.3
  • 20
    • 84877801048 scopus 로고    scopus 로고
    • Sweet carbon nanostructures: Carbohydrate conjugates with carbon nanotubes and graphene and their applications
    • Chen, Y.; Star, A.; Vidal, S. Sweet carbon nanostructures: Carbohydrate conjugates with carbon nanotubes and graphene and their applications. Chem. Soc. Rev. 2013, 42, 4532-4542.
    • (2013) Chem. Soc. Rev , vol.42 , pp. 4532-4542
    • Chen, Y.1    Star, A.2    Vidal, S.3
  • 21
    • 84874951300 scopus 로고    scopus 로고
    • Glycosylated nanoscale surfaces: Preparation and applications in medicine and molecular biology
    • Kennedy, D.C.; Grünstein, D.; Lai, C.-H.; Seeberger, P.H. Glycosylated nanoscale surfaces: Preparation and applications in medicine and molecular biology. Chem. Eur. J. 2013, 19, 3794-3800.
    • (2013) Chem. Eur. J , vol.19 , pp. 3794-3800
    • Kennedy, D.C.1    Grünstein, D.2    Lai, C.-H.3    Seeberger, P.H.4
  • 22
    • 84875926829 scopus 로고    scopus 로고
    • Multivalent glycocalixarenes for recognition of biological macromolecules: Glycocalyx mimics capable of multitasking
    • Sansone, F.; Casnati, A. Multivalent glycocalixarenes for recognition of biological macromolecules: Glycocalyx mimics capable of multitasking. Chem. Soc. Rev. 2013, 42, 4623-4639.
    • (2013) Chem. Soc. Rev , vol.42 , pp. 4623-4639
    • Sansone, F.1    Casnati, A.2
  • 23
    • 84922256616 scopus 로고    scopus 로고
    • Glycomimetics versus multivalent glycoconjugates for the design of high affinity lectin ligands
    • Cecioni, S.; Imberty, A.; Vidal, S. Glycomimetics versus multivalent glycoconjugates for the design of high affinity lectin ligands. Chem. Rev. 2014, 115, 525-561.
    • (2014) Chem. Rev , vol.115 , pp. 525-561
    • Cecioni, S.1    Imberty, A.2    Vidal, S.3
  • 25
    • 79951800443 scopus 로고    scopus 로고
    • Allosteric, chelate, and interannular cooperativity: A mise AU point
    • Ercolani, G.; Schiaffino, L. Allosteric, chelate, and interannular cooperativity: A mise AU point. Angew. Chem. Int. Ed. 2011, 50, 1762-1768.
    • (2011) Angew. Chem. Int. Ed , vol.50 , pp. 1762-1768
    • Ercolani, G.1    Schiaffino, L.2
  • 27
    • 35348855865 scopus 로고    scopus 로고
    • Probing multivalent carbohydrate-lectin interactions by an enzyme-linked lectin assay employing covalently immobilized carbohydrates
    • Maierhofer, C.; Rohmer, K.; Wittmann, V. Probing multivalent carbohydrate-lectin interactions by an enzyme-linked lectin assay employing covalently immobilized carbohydrates. Bioorg. Med. Chem. 2007, 15, 7661-7676.
    • (2007) Bioorg. Med. Chem , vol.15 , pp. 7661-7676
    • Maierhofer, C.1    Rohmer, K.2    Wittmann, V.3
  • 28
    • 0034442307 scopus 로고    scopus 로고
    • Affinity enhancement by multivalent lectin-carbohydrate interaction
    • Lee, R.; Lee, Y. Affinity enhancement by multivalent lectin-carbohydrate interaction. Glycoconj. J. 2000, 17, 543-551.
    • (2000) Glycoconj. J , vol.17 , pp. 543-551
    • Lee, R.1    Lee, Y.2
  • 29
    • 0040111705 scopus 로고    scopus 로고
    • Bivalent inhibitors of protein tyrosine kinases
    • Profit, A.A.; Lee, T.R.; Lawrence, D.S. Bivalent inhibitors of protein tyrosine kinases. J. Am. Chem. Soc. 1999, 121, 280-283.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 280-283
    • Profit, A.A.1    Lee, T.R.2    Lawrence, D.S.3
  • 31
    • 0032076568 scopus 로고    scopus 로고
    • A trivalent system from vancomycin· d-Ala-d-Ala with higher affinity than avidin·biotin
    • Rao, J.; Lahiri, J.; Isaacs, L.; Weis, R.M.; Whitesides, G.M. A trivalent system from vancomycin· d-Ala-d-Ala with higher affinity than avidin·biotin. Science 1998, 280, 708-711.
    • (1998) Science , vol.280 , pp. 708-711
    • Rao, J.1    Lahiri, J.2    Isaacs, L.3    Weis, R.M.4    Whitesides, G.M.5
  • 32
    • 0033049429 scopus 로고    scopus 로고
    • The neoglycoprotein mannose-bovine serum albumin, but not progesterone, activates T-type calcium channels in human spermatozoa
    • Blackmore, P.F.; Eisoldt, S. The neoglycoprotein mannose-bovine serum albumin, but not progesterone, activates T-type calcium channels in human spermatozoa. Mol. Hum. Reprod. 1999, 5, 498-506.
    • (1999) Mol. Hum. Reprod , vol.5 , pp. 498-506
    • Blackmore, P.F.1    Eisoldt, S.2
  • 33
    • 84886789912 scopus 로고    scopus 로고
    • Fucosyl neoglycoprotein binds to mouse epididymal spermatozoa and inhibits sperm binding to the egg zona pellucida
    • Oh, Y.S.; Ahn, H.S.; Gye, M.C. Fucosyl neoglycoprotein binds to mouse epididymal spermatozoa and inhibits sperm binding to the egg zona pellucida. Andrologia 2013, 45, 363-368.
    • (2013) Andrologia , vol.45 , pp. 363-368
    • Oh, Y.S.1    Ahn, H.S.2    Gye, M.C.3
  • 34
    • 3242772209 scopus 로고    scopus 로고
    • Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry
    • Huang, B.X.; Kim, H.-Y.; Dass, C. Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry. J. Am. Soc. Mass Spectrom. 2004, 15, 1237-1247.
    • (2004) J. Am. Soc. Mass Spectrom , vol.15 , pp. 1237-1247
    • Huang, B.X.1    Kim, H.-Y.2    Dass, C.3
  • 35
    • 70349147430 scopus 로고    scopus 로고
    • Facile preparation of fluorescent neoglycoproteins using p-nitrophenyl anthranilate as a heterobifunctional linker. Bioconjug
    • Luyai, A.; Lasanajak, Y.; Smith, D.F.; Cummings, R.D.; Song, X. Facile preparation of fluorescent neoglycoproteins using p-nitrophenyl anthranilate as a heterobifunctional linker. Bioconjug. Chem. 2009, 20, 1618-1624.
    • (2009) Chem , vol.20 , pp. 1618-1624
    • Luyai, A.1    Lasanajak, Y.2    Smith, D.F.3    Cummings, R.D.4    Song, X.5
  • 36
    • 0037122782 scopus 로고    scopus 로고
    • Structure-activity profiles of complex biantennary glycans with core fucosylation and with/without additional α 2,3/α2,6 sialylation: Synthesis of neoglycoproteins and their properties in lectin assays, cell binding, and organ uptake
    • Unverzagt, C.; André, S.; Seifert, J.; Kojima, S.; Fink, C.; Srikrishna, G.; Freeze, H.; Kayser, K.; Gabius, H.-J. Structure-activity profiles of complex biantennary glycans with core fucosylation and with/without additional α 2,3/α2,6 sialylation: Synthesis of neoglycoproteins and their properties in lectin assays, cell binding, and organ uptake. J. Med. Chem. 2002, 45, 478-491.
    • (2002) J. Med. Chem , vol.45 , pp. 478-491
    • Unverzagt, C.1    André, S.2    Seifert, J.3    Kojima, S.4    Fink, C.5    Srikrishna, G.6    Freeze, H.7    Kayser, K.8    Gabius, H.-J.9
  • 37
    • 0025928878 scopus 로고
    • Neoglycoproteins as tools in glycohistochemistry
    • Gabius, H.J.; Bardosi, A. Neoglycoproteins as tools in glycohistochemistry. Prog. Histochem. Cytochem. 1991, 22, 1-63.
    • (1991) Prog. Histochem. Cytochem , vol.22 , pp. 1-63
    • Gabius, H.J.1    Bardosi, A.2
  • 38
    • 0018886932 scopus 로고
    • Neoglycoproteins the preparation and application of synthetic glycoproteins
    • Tipson, R.S., Derek, H., Eds.; Academic Press: Waltham, MA, USA
    • Stowell, C.P.; Lee, Y.C. Neoglycoproteins the preparation and application of synthetic glycoproteins. In Advances in Carbohydrate Chemistry and Biochemistry; Tipson, R.S., Derek, H., Eds.; Academic Press: Waltham, MA, USA, 1980; Volume 37, pp. 225-281.
    • (1980) Advances in Carbohydrate Chemistry and Biochemistry , vol.37 , pp. 225-281
    • Stowell, C.P.1    Lee, Y.C.2
  • 40
    • 0027965708 scopus 로고
    • Galectins. Structure and function of a large family of animal lectins
    • Barondes, S.H.; Cooper, D.N.; Gitt, M.A.; 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
  • 42
    • 85015482004 scopus 로고    scopus 로고
    • Galectins in tumor angiogenesis
    • Griffioen, A.W.; Thijssen, V.L. Galectins in tumor angiogenesis. Ann. Transl. Med. 2014, 2, doi:10.3978/j.issn.2305-5839.2014.09.01.
    • (2014) Ann. Transl. Med , pp. 2
    • Griffioen, A.W.1    Thijssen, V.L.2
  • 44
    • 11144241063 scopus 로고    scopus 로고
    • Galectins as modulators of tumour progression
    • Liu, F.-T.; Rabinovich, G.A. 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
  • 48
    • 18044396712 scopus 로고    scopus 로고
    • On the role of galectin-3 in cancer apoptosis
    • Nakahara, S.; Oka, N.; Raz, A. On the role of galectin-3 in cancer apoptosis. Apoptosis 2005, 10, 267-275.
    • (2005) Apoptosis , vol.10 , pp. 267-275
    • Nakahara, S.1    Oka, N.2    Raz, A.3
  • 49
    • 33745006606 scopus 로고    scopus 로고
    • Galectin-3: An open-ended story
    • Dumic, J.; Dabelic, S.; Flögel, M. Galectin-3: An open-ended story. BBA Gen. Subj. 2006, 1760, 616-635.
    • (2006) BBA Gen. Subj , vol.1760 , pp. 616-635
    • Dumic, J.1    Dabelic, S.2    Flögel, M.3
  • 50
    • 84941122414 scopus 로고    scopus 로고
    • Galectin-3: An emerging all-out player in metabolic disorders and their complications
    • Pugliese, G.; Iacobini, C.; Pesce, C.M.; Menini, S. Galectin-3: An emerging all-out player in metabolic disorders and their complications. Glycobiology 2015, 25, 136-150.
    • (2015) Glycobiology , vol.25 , pp. 136-150
    • Pugliese, G.1    Iacobini, C.2    Pesce, C.M.3    Menini, S.4
  • 53
    • 84880262450 scopus 로고    scopus 로고
    • Human galectin-3 selective and high affinity inhibitors. Present state and future perspectives
    • Téllez-Sanz, R.; Garcia-Fuentes, L.; Vargas-Berenguel, A. Human galectin-3 selective and high affinity inhibitors. Present state and future perspectives. Curr. Med. Chem. 2013, 20, 2979-2990.
    • (2013) Curr. Med. Chem , vol.20 , pp. 2979-2990
    • Téllez-Sanz, R.1    Garcia-Fuentes, L.2    Vargas-Berenguel, A.3
  • 54
    • 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.C.; Macaluso, F.; Brewer, C.F. Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes. J. Biol. Chem. 2004, 279, 10841-10847.
    • (2004) J. Biol. Chem , vol.279 , pp. 10841-10847
    • Ahmad, N.1    Gabius, H.J.2    Andre, S.3    Kaltner, H.4    Sabesan, S.5    Roy, R.6    Liu, B.C.7    Macaluso, F.8    Brewer, C.F.9
  • 55
    • 84862699129 scopus 로고    scopus 로고
    • Ligand induced galectin-3 protein self-association
    • Lepur, A.; Salomonsson, E.; Nilsson, U.J.; Leffler, H. Ligand induced galectin-3 protein self-association. J. Biol. Chem. 2012, 287, 21751-21756.
    • (2012) J. Biol. Chem , vol.287 , pp. 21751-21756
    • Lepur, A.1    Salomonsson, E.2    Nilsson, U.J.3    Leffler, H.4
  • 56
    • 24944450621 scopus 로고    scopus 로고
    • Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants
    • Dam, T.K.; Gabius, H.-J.; André, S.; Kaltner, H.; Lensch, M.; Brewer, C.F. Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants. Biochemistry 2005, 44, 12564-12571.
    • (2005) Biochemistry , vol.44 , pp. 12564-12571
    • Dam, T.K.1    Gabius, H.-J.2    André, S.3    Kaltner, H.4    Lensch, M.5    Brewer, C.F.6
  • 58
    • 84863817165 scopus 로고    scopus 로고
    • Synthesis of multivalent n-acetyl lactosamine modified quantum dots for the study of carbohydrate and galectin-3 interactions
    • Yang, Y.; Xue, X.C.; Jin, X.F.; Wang, L.J.; Sha, Y.L.; Li, Z.J. Synthesis of multivalent n-acetyl lactosamine modified quantum dots for the study of carbohydrate and galectin-3 interactions. Tetrahedron 2012, 68, 7148-7154.
    • (2012) Tetrahedron , vol.68 , pp. 7148-7154
    • Yang, Y.1    Xue, X.C.2    Jin, X.F.3    Wang, L.J.4    Sha, Y.L.5    Li, Z.J.6
  • 59
    • 84928667514 scopus 로고    scopus 로고
    • Glycodendrimers and modified elisas: Tools to elucidate multivalent interactions of galectins 1 and 3
    • Wolfenden, M.; Cousin, J.; Nangia-Makker, P.; Raz, A.; Cloninger, M. Glycodendrimers and modified elisas: Tools to elucidate multivalent interactions of galectins 1 and 3. Molecules 2015, 20, 7059-7096.
    • (2015) Molecules , vol.20 , pp. 7059-7096
    • Wolfenden, M.1    Cousin, J.2    Nangia-Makker, P.3    Raz, A.4    Cloninger, M.5
  • 61
    • 84903639370 scopus 로고    scopus 로고
    • Expression of lacdinac group on N-glycans among human tumors is complex
    • Hirano, K.; Matsuda, A.; Shirai, T.; Furukawa, K. Expression of lacdinac group on N-glycans among human tumors is complex. Biomed. Res. Int. 2014, doi:10.1155/2014/981627.
    • (2014) Biomed. Res. Int
    • Hirano, K.1    Matsuda, A.2    Shirai, T.3    Furukawa, K.4
  • 62
    • 0030891265 scopus 로고    scopus 로고
    • Differential expression of lacdinac sequences (GalNAc1-4GlcNAc-R) in glycoproteins synthesized by chinese hamster ovary and human 293 cells
    • Do, K.-Y.; Do, S.; Cummings, R.D. Differential expression of lacdinac sequences (GalNAc1-4GlcNAc-R) in glycoproteins synthesized by chinese hamster ovary and human 293 cells. Glycobiology 1997, 7, 183-194.
    • (1997) Glycobiology , vol.7 , pp. 183-194
    • Do, K.-Y.1    Do, S.2    Cummings, R.D.3
  • 63
    • 84863190461 scopus 로고    scopus 로고
    • Presence of terminal N-acetylgalactosamine_1-4N-acetylglucosamine residues on O-linked oligosaccharides from gastric MUC5AC: Involvement in helicobacter pylori colonization?
    • Kenny, D.T.; Skoog, E.C.; Lindén, S.K.; Struwe, W.B.; Rudd, P.M.; Karlsson, N.G. Presence of terminal N-acetylgalactosamine_1-4N-acetylglucosamine residues on O-linked oligosaccharides from gastric MUC5AC: Involvement in helicobacter pylori colonization? Glycobiology 2012, 22, 1077-1085.
    • (2012) Glycobiology , vol.22 , pp. 1077-1085
    • Kenny, D.T.1    Skoog, E.C.2    Lindén, S.K.3    Struwe, W.B.4    Rudd, P.M.5    Karlsson, N.G.6
  • 68
    • 0029962092 scopus 로고    scopus 로고
    • Use of diethyl squarate for the coupling of oligosaccharide amines to carrier proteins and characterization of the resulting neoglycoproteins by MALDI-TOF mass spectrometry
    • Kamath, V.P.; Diedrich, P.; Hindsgaul, O. Use of diethyl squarate for the coupling of oligosaccharide amines to carrier proteins and characterization of the resulting neoglycoproteins by MALDI-TOF mass spectrometry. Glycoconj. J. 1996, 13, 315-319.
    • (1996) Glycoconj. J , vol.13 , pp. 315-319
    • Kamath, V.P.1    Diedrich, P.2    Hindsgaul, O.3
  • 69
    • 33845297637 scopus 로고
    • Anticancer agents, 15. Squaric acid diethyl ester: A new coupling reagent for the formation of drug biopolymer conjugates. Synthesis of squaric acid ester amides and diamides
    • Tietze, L.F.; Arlt, M.; Beller, M.; gl üsenkamp, K.-H.; Jähde, E.; Rajewsky, M.F. Anticancer agents, 15. Squaric acid diethyl ester: A new coupling reagent for the formation of drug biopolymer conjugates. Synthesis of squaric acid ester amides and diamides. Chem. Ber. 1991, 124, 1215-1221.
    • (1991) Chem. Ber , vol.124 , pp. 1215-1221
    • Tietze, L.F.1    Arlt, M.2    Beller, M.3    Gl Üsenkamp, K.-H.4    Jähde, E.5    Rajewsky, M.F.6
  • 70
    • 0026164295 scopus 로고
    • Conjugation of p-aminophenyl glycosides with squaric acid diester to a carrier protein and the use of the neoglycoprotein in the histochemical detection of lectins
    • Tietze, L.F.; Schroeter, C.; Gabius, S.; Brinck, U.; Goerlach-Graw, A.; Gabius, H.J. Conjugation of p-aminophenyl glycosides with squaric acid diester to a carrier protein and the use of the neoglycoprotein in the histochemical detection of lectins. Bioconjug. Chem. 1991, 2, 148-153.
    • (1991) Bioconjug. Chem , vol.2 , pp. 148-153
    • Tietze, L.F.1    Schroeter, C.2    Gabius, S.3    Brinck, U.4    Goerlach-Graw, A.5    Gabius, H.J.6
  • 71
    • 77957572230 scopus 로고    scopus 로고
    • Synthesis of a BSA-Lex glycoconjugate and recognition of Lex analogues by the anti-Lex monoclonal antibody sh1: The identification of a non-cross reactive analogue
    • Wang, J.W.; Asnani, A.; Auzanneau, F.I. Synthesis of a BSA-Lex glycoconjugate and recognition of Lex analogues by the anti-Lex monoclonal antibody sh1: The identification of a non-cross reactive analogue. Bioorg. Med. Chem. 2010, 18, 7174-7185.
    • (2010) Bioorg. Med. Chem , vol.18 , pp. 7174-7185
    • Wang, J.W.1    Asnani, A.2    Auzanneau, F.I.3
  • 72
    • 84885089490 scopus 로고    scopus 로고
    • Be squared: Expanding the horizon of squaric acid-mediated conjugations
    • Wurm, F.R.; Klok, H.A. Be squared: Expanding the horizon of squaric acid-mediated conjugations. Chem. Soc. Rev. 2013, 42, 8220-8236.
    • (2013) Chem. Soc. Rev , vol.42 , pp. 8220-8236
    • Wurm, F.R.1    Klok, H.A.2
  • 73
    • 84920836156 scopus 로고    scopus 로고
    • Synthesis of a pentasaccharide and neoglycoconjugates related to fungal alpha-(1α3)-glucan and their use in the generation of antibodies to trace aspergillus fumigatus cell wall
    • Komarova, B.S.; Orekhova, M.V.; Tsvetkov, Y.E.; Beau, R.; Aimanianda, V.; Latge, J.P.; Nifantiev, N.E. Synthesis of a pentasaccharide and neoglycoconjugates related to fungal alpha-(1α3)-glucan and their use in the generation of antibodies to trace aspergillus fumigatus cell wall. Chemistry 2015, 21, 1029-1035.
    • (2015) Chemistry , vol.21 , pp. 1029-1035
    • Komarova, B.S.1    Orekhova, M.V.2    Tsvetkov, Y.E.3    Beau, R.4    Aimanianda, V.5    Latge, J.P.6    Nifantiev, N.E.7
  • 74
    • 84857534589 scopus 로고    scopus 로고
    • Determination of glycation sites by tandem mass spectrometry in a synthetic lactose-bovine serum albumin conjugate, a vaccine model prepared by dialkyl squarate chemistry
    • Jahouh, F.; Hou, S.J.; Kovac, P.; Banoub, J.H. Determination of glycation sites by tandem mass spectrometry in a synthetic lactose-bovine serum albumin conjugate, a vaccine model prepared by dialkyl squarate chemistry. Rapid. Commun. Mass Spectrom. 2012, 26, 749-758.
    • (2012) Rapid. Commun. Mass Spectrom , vol.26 , pp. 749-758
    • Jahouh, F.1    Hou, S.J.2    Kovac, P.3    Banoub, J.H.4
  • 75
    • 84885640683 scopus 로고    scopus 로고
    • Mapping the glycation sites in the neoglycoconjugate from hexasaccharide antigen of vibrio cholerae, serotype ogawa and the recombinant tetanus toxin C-fragment carrier
    • Jahouh, F.; Xu, P.; Vann, W.F.; Kovac, P.; Banoub, J.H. Mapping the glycation sites in the neoglycoconjugate from hexasaccharide antigen of vibrio cholerae, serotype ogawa and the recombinant tetanus toxin C-fragment carrier. J. Mass Spectrom. 2013, 48, 1083-1090.
    • (2013) J. Mass Spectrom , vol.48 , pp. 1083-1090
    • Jahouh, F.1    Xu, P.2    Vann, W.F.3    Kovac, P.4    Banoub, J.H.5
  • 76
    • 36849070325 scopus 로고    scopus 로고
    • Characterization of recombinant fusion constructs of human _1,4-galactosyltransferase 1 and the lipase pre-propeptide from staphylococcus hyicus
    • Sauerzapfe, B.; Namdjou, D.J.; Schumacher, T.; Linden, N.; Kenek, K.; Ken, V.; Elling, L. Characterization of recombinant fusion constructs of human _1,4-galactosyltransferase 1 and the lipase pre-propeptide from staphylococcus hyicus. J. Mol. Catal. B Enzym. 2008, 50, 128-140.
    • (2008) J. Mol. Catal. B Enzym , vol.50 , pp. 128-140
    • Sauerzapfe, B.1    Namdjou, D.J.2    Schumacher, T.3    Linden, N.4    Kenek, K.5    Ken, V.6    Elling, L.7
  • 78
    • 84861159382 scopus 로고    scopus 로고
    • Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDINAc) based on galactose oxidase treatment
    • Kupper, C.E.; Rosencrantz, R.R.; Henssen, B.; Pelantová, H.; Thönes, S.; Drozdova, A.; Ken, V.; Elling, L. Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDINAc) based on galactose oxidase treatment. Beilstein J. Org. Chem. 2012, 8, 712-725.
    • (2012) Beilstein J. Org. Chem , vol.8 , pp. 712-725
    • Kupper, C.E.1    Rosencrantz, R.R.2    Henssen, B.3    Pelantová, H.4    Thönes, S.5    Drozdova, A.6    Ken, V.7    Elling, L.8
  • 79
    • 38049064951 scopus 로고    scopus 로고
    • Preparation of glycoconjugates by dialkyl squarate chemistry revisited
    • Hou, S.J.; Saksena, R.; Kovac, P. Preparation of glycoconjugates by dialkyl squarate chemistry revisited. Carbohydr. Res. 2008, 343, 196-210.
    • (2008) Carbohydr. Res , vol.343 , pp. 196-210
    • Hou, S.J.1    Saksena, R.2    Kovac, P.3
  • 80
    • 0031194458 scopus 로고    scopus 로고
    • The quantification of protein amino groups by the trinitrobenzenesulfonic acid method: A reexamination
    • Cayot, P.; Tainturier, G. The quantification of protein amino groups by the trinitrobenzenesulfonic acid method: A reexamination. Anal. Biochem. 1997, 249, 184-200.
    • (1997) Anal. Biochem , vol.249 , pp. 184-200
    • Cayot, P.1    Tainturier, G.2
  • 81
    • 84884187149 scopus 로고    scopus 로고
    • Identification and quantification of protein glycosylation
    • Roth, Z.; Yehezkel, G.; Khalaila, I. Identification and quantification of protein glycosylation. Int. J. Carbohydr. Chem. 2012, doi:10.1155/2012/640923.
    • (2012) Int. J. Carbohydr. Chem
    • Roth, Z.1    Yehezkel, G.2    Khalaila, I.3
  • 82
    • 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, H.J.; Kaltner, H.; Andre, S.; Kuwabara, I.; Liu, F.T.; Oscarson, S.; Norberg, T.; Brewer, C.F. 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
  • 83
    • 41549129317 scopus 로고    scopus 로고
    • Galectin-loaded cells as a platform for the profiling of lectin specificity by fluorescent neoglycoconjugates: A case study on galectins-1 and-3 and the impact of assay setting
    • Rapoport, E.M.; Andre, S.; Kurmyshkina, O.V.; Pochechueva, T.V.; Severov, V.V.; Pazynina, G.V.; Gabius, H.J.; Bovin, N.V. Galectin-loaded cells as a platform for the profiling of lectin specificity by fluorescent neoglycoconjugates: A case study on galectins-1 and-3 and the impact of assay setting. Glycobiology 2008, 18, 315-324.
    • (2008) Glycobiology , vol.18 , pp. 315-324
    • Rapoport, E.M.1    Andre, S.2    Kurmyshkina, O.V.3    Pochechueva, T.V.4    Severov, V.V.5    Pazynina, G.V.6    Gabius, H.J.7    Bovin, N.V.8
  • 85
    • 14044272136 scopus 로고    scopus 로고
    • Dimeric galectin-1 binds with high affinity to alpha 2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans
    • Leppänen, A.; Stowell, S.; Blixt, O.; Cummings, R.D. Dimeric galectin-1 binds with high affinity to alpha 2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. J. Biol. Chem. 2005, 280, 5549-5562.
    • (2005) J. Biol. Chem , vol.280 , pp. 5549-5562
    • Leppänen, A.1    Stowell, S.2    Blixt, O.3    Cummings, R.D.4
  • 86
    • 0032913440 scopus 로고    scopus 로고
    • Enzymatic synthesis of natural and C-13 enriched linear poly-N-acetyllactosamines as ligands for galectin-1
    • Di Virgilio, S.; Glushka, J.; Moremen, K.; Pierce, M. Enzymatic synthesis of natural and C-13 enriched linear poly-N-acetyllactosamines as ligands for galectin-1. Glycobiology 1999, 9, 353-364.
    • (1999) Glycobiology , vol.9 , pp. 353-364
    • Di Virgilio, S.1    Glushka, J.2    Moremen, K.3    Pierce, M.4
  • 87
    • 0027162467 scopus 로고
    • L-14 lectin recognition of laminin and its promotion of in vitro cell adhesion
    • Qun, Z.; Cummings, R.D. L-14 lectin recognition of laminin and its promotion of in vitro cell adhesion. Arch. Biochem. Biophys. 1993, 300, 6-17.
    • (1993) Arch. Biochem. Biophys , vol.300 , pp. 6-17
    • Qun, Z.1    Cummings, R.D.2
  • 88
    • 84875214623 scopus 로고    scopus 로고
    • Design and synthesis of glycoprotein-based multivalent glyco-ligands for influenza hemagglutinin and human galectin-3
    • Wang, H.; Huang, W.; Orwenyo, J.; Banerjee, A.; Vasta, G.R.; Wang, L.X. Design and synthesis of glycoprotein-based multivalent glyco-ligands for influenza hemagglutinin and human galectin-3. Bioorg. Med. Chem. 2013, 21, 2037-2044.
    • (2013) Bioorg. Med. Chem , vol.21 , pp. 2037-2044
    • Wang, H.1    Huang, W.2    Orwenyo, J.3    Banerjee, A.4    Vasta, G.R.5    Wang, L.X.6
  • 89
    • 48649102319 scopus 로고    scopus 로고
    • Arene-based glycoclusters: Bioactivity of thiourea-linked galactose/lactose moieties as inhibitors of binding of medically relevant lectins to a glycoprotein and cell-surface glycoconjugates and selectivity among human adhesion/growth-regulatory galectins
    • André, S.; Sansone, F.; Kaltner, H.; Casnati, A.; Kopitz, J.; Gabius, H.J.; Ungaro, R. Calix N arene-based glycoclusters: Bioactivity of thiourea-linked galactose/lactose moieties as inhibitors of binding of medically relevant lectins to a glycoprotein and cell-surface glycoconjugates and selectivity among human adhesion/growth-regulatory galectins. ChemBioChem 2008, 9, 1649-1661.
    • (2008) Chembiochem , vol.9 , pp. 1649-1661
    • André, S.1    Sansone, F.2    Kaltner, H.3    Casnati, A.4    Kopitz, J.5    Gabius, H.J.6    Ungaro, R.7    Calix, N.8
  • 90
    • 79956088428 scopus 로고    scopus 로고
    • Combining carbohydrate substitutions at bioinspired positions with multivalent presentation towards optimising lectin inhibitors: Case study with calixarenes
    • André, S.; Grandjean, C.; Gautier, F.M.; Bernardi, S.; Sansone, F.; Gabius, H.J.; Ungaro, R. Combining carbohydrate substitutions at bioinspired positions with multivalent presentation towards optimising lectin inhibitors: Case study with calixarenes. Chem. Commun. 2011, 47, 6126-6128.
    • (2011) Chem. Commun , vol.47 , pp. 6126-6128
    • André, S.1    Grandjean, C.2    Gautier, F.M.3    Bernardi, S.4    Sansone, F.5    Gabius, H.J.6    Ungaro, R.7
  • 91
    • 0035814138 scopus 로고    scopus 로고
    • Wedgelike glycodendrimers as inhibitors of binding of mammalian galectins to glycoproteins, lactose maxiclusters, and cell surface glycoconjugates
    • André, S.; Pieters, R.J.; Vrasidas, I.; Kaltner, H.; Kuwabara, I.; Liu, F.T.; Liskamp, R.M.; Gabius, H.J. Wedgelike glycodendrimers as inhibitors of binding of mammalian galectins to glycoproteins, lactose maxiclusters, and cell surface glycoconjugates. ChemBioChem 2001, 2, 822-830.
    • (2001) Chembiochem , vol.2 , pp. 822-830
    • André, S.1    Pieters, R.J.2    Vrasidas, I.3    Kaltner, H.4    Kuwabara, I.5    Liu, F.T.6    Liskamp, R.M.7    Gabius, H.J.8
  • 93
    • 37049015985 scopus 로고    scopus 로고
    • The determination of the levels of circulating galectin-1 and α-3 in HNSCC patients could be used to monitor tumor progression and/or responses to therapy
    • Saussez, S.; Lorfevre, F.; Lequeux, T.; Laurent, G.; Chantrain, G.; Vertongen, F.; Toubeau, G.R.; Decaestecker, C.; Kiss, R. The determination of the levels of circulating galectin-1 and α-3 in HNSCC patients could be used to monitor tumor progression and/or responses to therapy. Oral. Oncol. 2008, 44, 86-93.
    • (2008) Oral. Oncol , vol.44 , pp. 86-93
    • Saussez, S.1    Lorfevre, F.2    Lequeux, T.3    Laurent, G.4    Chantrain, G.5    Vertongen, F.6    Toubeau, G.R.7    Decaestecker, C.8    Kiss, R.9
  • 97
    • 13644272606 scopus 로고    scopus 로고
    • Structural and thermodynamic studies on cation-Pi interactions in lectin-ligand complexes: High-affinity galectin-3 inhibitors through fine-tuning of an arginine-arene interaction
    • Sörme, P.; Arnoux, P.; Kahl-Knutsson, B.; Leffler, H.; Rini, J.M.; Nilsson, U.J. Structural and thermodynamic studies on cation-Pi interactions in lectin-ligand complexes: High-affinity galectin-3 inhibitors 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
  • 98
    • 0037132694 scopus 로고    scopus 로고
    • Inhibition of human cancer cell growth and metastasis in nude mice by oral intake of modified citrus pectin
    • Nangia-Makker, P.; Hogan, V.; Honjo, Y.; Baccarini, S.; Tait, L.; Bresalier, R.; Raz, A. Inhibition of human cancer cell growth and metastasis in nude mice by oral intake of modified citrus pectin. J. Natl. Cancer Inst. 2002, 94, 1854-1862.
    • (2002) J. Natl. Cancer Inst , vol.94 , pp. 1854-1862
    • Nangia-Makker, P.1    Hogan, V.2    Honjo, Y.3    Baccarini, S.4    Tait, L.5    Bresalier, R.6    Raz, A.7
  • 100
    • 84908253095 scopus 로고    scopus 로고
    • Lactose-functionalized dendrimers arbitrate the interaction of galectin-3/muc1 mediated cancer cellular aggregation
    • Michel, A.K.; Nangia-Makker, P.; Raz, A.; Cloninger, M.J. Lactose-functionalized dendrimers arbitrate the interaction of galectin-3/muc1 mediated cancer cellular aggregation. ChemBioChem 2014, 15, 2106-2112.
    • (2014) Chembiochem , vol.15 , pp. 2106-2112
    • Michel, A.K.1    Nangia-Makker, P.2    Raz, A.3    Cloninger, M.J.4
  • 102
    • 0020445290 scopus 로고
    • Neoglycoproteins. Preparation and in vivo clearance of serum albumin derivatives containing ovalbumin oligosaccharides
    • Mencke, A.J.; Wold, F. Neoglycoproteins. Preparation and in vivo clearance of serum albumin derivatives containing ovalbumin oligosaccharides. J. Biol. Chem. 1982, 257, 14799-14805.
    • (1982) J. Biol. Chem , vol.257 , pp. 14799-14805
    • Mencke, A.J.1    Wold, F.2
  • 105
    • 60449095770 scopus 로고    scopus 로고
    • Chemo-enzymatic synthesis of poly-N-acetyllactosamine (Poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ecm glycoproteins to biomaterial surfaces
    • Sauerzapfe, B.; Krenek, K.; Schmiedel, J.; Wakarchuk, W.W.; Pelantova, H.; Kren, V.; Elling, L. Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ecm glycoproteins to biomaterial surfaces. Glycoconj. J. 2009, 26, 141-159.
    • (2009) Glycoconj. J , vol.26 , pp. 141-159
    • Sauerzapfe, B.1    Krenek, K.2    Schmiedel, J.3    Wakarchuk, W.W.4    Pelantova, H.5    Kren, V.6    Elling, L.7
  • 106
    • 0014216041 scopus 로고
    • Removal of fatty acids from serum albumin by charcoal treatment
    • Chen, R.F. Removal of fatty acids from serum albumin by charcoal treatment. J. Biol. Chem. 1967, 242, 173-181.
    • (1967) J. Biol. Chem , vol.242 , pp. 173-181
    • Chen, R.F.1
  • 107
    • 79960372202 scopus 로고    scopus 로고
    • Glyco-DNA-gold nanoparticles: Lectin-mediated assembly and dual-stimuli response
    • Witten, K.G.; Rech, C.; Eckert, T.; Charrak, S.; Richtering, W.; Elling, L.; Simon, U. Glyco-DNA-gold nanoparticles: Lectin-mediated assembly and dual-stimuli response. Small 2011, 7, 1954-1960.
    • (2011) Small , vol.7 , pp. 1954-1960
    • Witten, K.G.1    Rech, C.2    Eckert, T.3    Charrak, S.4    Richtering, W.5    Elling, L.6    Simon, U.7


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