메뉴 건너뛰기




Volumn 44, Issue , 2017, Pages 1-8

Antibody recognition of aberrant glycosylation on the surface of cancer cells

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; GANGLIOSIDE; TUMOR ANTIGEN; TUMOR ASSOCIATED CARBOHYDRATE ANTIGEN; UNCLASSIFIED DRUG; ANTIBODY; POLYSACCHARIDE;

EID: 84993972005     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2016.10.009     Document Type: Review
Times cited : (31)

References (49)
  • 1
    • 22944456543 scopus 로고    scopus 로고
    • Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours
    • 1 Kobata, A., Amano, J., Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours. Immunol Cell Biol 83 (2005), 429–439.
    • (2005) Immunol Cell Biol , vol.83 , pp. 429-439
    • Kobata, A.1    Amano, J.2
  • 2
    • 79952008246 scopus 로고    scopus 로고
    • A glycobiology review: carbohydrates, lectins and implications in cancer therapeutics
    • 2 Ghazarian, H., Idoni, B., Oppenheimer, S.B., A glycobiology review: carbohydrates, lectins and implications in cancer therapeutics. Acta Histochem 113 (2011), 236–247.
    • (2011) Acta Histochem , vol.113 , pp. 236-247
    • Ghazarian, H.1    Idoni, B.2    Oppenheimer, S.B.3
  • 3
    • 84935084960 scopus 로고    scopus 로고
    • Structural biology of antibody recognition of carbohydrate epitopes and potential uses for targeted cancer immunotherapies
    • A detailed review focusing on the conformational properties of Lewis blood-group related carbohydrates bound to antibodies and lectins. Also discussed, are the implications of these structural data for the design of improved antibodies and vaccines as targeted cancer immunotherapies.
    • 3• Dingjan, T., Spendlove, I., Durrant, L.G., Scott, A.M., Yuriev, E., Ramsland, P.A., Structural biology of antibody recognition of carbohydrate epitopes and potential uses for targeted cancer immunotherapies. Mol Immunol 67 (2015), 75–88 A detailed review focusing on the conformational properties of Lewis blood-group related carbohydrates bound to antibodies and lectins. Also discussed, are the implications of these structural data for the design of improved antibodies and vaccines as targeted cancer immunotherapies.
    • (2015) Mol Immunol , vol.67 , pp. 75-88
    • Dingjan, T.1    Spendlove, I.2    Durrant, L.G.3    Scott, A.M.4    Yuriev, E.5    Ramsland, P.A.6
  • 4
    • 84864597970 scopus 로고    scopus 로고
    • The sweet side of tumor immunotherapy
    • 4 Freire, T., Osinaga, E., The sweet side of tumor immunotherapy. Immunotherapy 4 (2012), 719–734.
    • (2012) Immunotherapy , vol.4 , pp. 719-734
    • Freire, T.1    Osinaga, E.2
  • 5
    • 84937418427 scopus 로고    scopus 로고
    • Antibodies: at the nexus of antigens and cancer vaccines
    • Examines the complex biological activities of tumor-targeting antibodies, particularly those recognizing carbohydrate antigens and details how structure–function studies are leading to new opportunities in vaccines for cancer.
    • 5• Steplewski, Z., Thurin, M., Kieber-Emmons, T., Antibodies: at the nexus of antigens and cancer vaccines. J Infect Dis 212:Suppl. 1 (2015), S59–S66 Examines the complex biological activities of tumor-targeting antibodies, particularly those recognizing carbohydrate antigens and details how structure–function studies are leading to new opportunities in vaccines for cancer.
    • (2015) J Infect Dis , vol.212 , pp. S59-S66
    • Steplewski, Z.1    Thurin, M.2    Kieber-Emmons, T.3
  • 7
    • 84939470826 scopus 로고    scopus 로고
    • Mechanisms of action of therapeutic antibodies for cancer
    • 7 Redman, J.M., Hill, E.M., AlDeghaither, D., Weiner, L.M., Mechanisms of action of therapeutic antibodies for cancer. Mol Immunol 67 (2015), 28–45.
    • (2015) Mol Immunol , vol.67 , pp. 28-45
    • Redman, J.M.1    Hill, E.M.2    AlDeghaither, D.3    Weiner, L.M.4
  • 8
    • 84855803916 scopus 로고    scopus 로고
    • Immunology in the clinic review series; focus on cancer: glycolipids as targets for tumour immunotherapy
    • 8 Durrant, L.G., Noble, P., Spendlove, I., Immunology in the clinic review series; focus on cancer: glycolipids as targets for tumour immunotherapy. Clin Exp Immunol 167 (2012), 206–215.
    • (2012) Clin Exp Immunol , vol.167 , pp. 206-215
    • Durrant, L.G.1    Noble, P.2    Spendlove, I.3
  • 9
    • 84954418340 scopus 로고    scopus 로고
    • Cancer cell associated glycans as targets for immunotherapy
    • A focused mini-review on the complex biological activities of glycolipid-binding antibodies. Mechanisms of direct antibody action including oncosis are discussed.
    • 9• Vankemmelbeke, M., Chua, J.X., Durrant, L.G., Cancer cell associated glycans as targets for immunotherapy. Oncoimmunology, 5, 2016, e1061177 A focused mini-review on the complex biological activities of glycolipid-binding antibodies. Mechanisms of direct antibody action including oncosis are discussed.
    • (2016) Oncoimmunology , vol.5 , pp. e1061177
    • Vankemmelbeke, M.1    Chua, J.X.2    Durrant, L.G.3
  • 10
    • 84859989941 scopus 로고    scopus 로고
    • Chapter 9 — structural glycobiology of antibody recognition in xenotransplantation and cancer immunotherapy
    • P. Kosma S. Muller-Loennies Springer
    • 10 Agostino, M., Farrugia, W., Sandrin, M.S., Scott, A.M., Yuriev, E., Ramsland, P.A., Chapter 9 — structural glycobiology of antibody recognition in xenotransplantation and cancer immunotherapy. Kosma, P., Muller-Loennies, S., (eds.) Anticarbohydrate Antibodies, 2012, Springer, 203–228.
    • (2012) Anticarbohydrate Antibodies , pp. 203-228
    • Agostino, M.1    Farrugia, W.2    Sandrin, M.S.3    Scott, A.M.4    Yuriev, E.5    Ramsland, P.A.6
  • 11
    • 84930177401 scopus 로고    scopus 로고
    • Dinutuximab: first global approval
    • 11 Dhillon, S., Dinutuximab: first global approval. Drugs 75 (2015), 923–927.
    • (2015) Drugs , vol.75 , pp. 923-927
    • Dhillon, S.1
  • 12
    • 84942870291 scopus 로고    scopus 로고
    • Structural basis of GD2 ganglioside and mimetic peptide recognition by 14G2a antibody
    • The first crystal structure of a ganglioside-binding antibody in complex with its target glycan headgroup. Structures of Fab-peptide complexes were also determined, but differences between carbohydrate and peptide recognition indicate functional and not structural mimicry by these peptides.
    • 12•• Horwacik, I., Golik, P., Grudnik, P., Kolinski, M., Zdzalik, M., Rokita, H., Dubin, G., Structural basis of GD2 ganglioside and mimetic peptide recognition by 14G2a antibody. Mol Cell Proteomics 14 (2015), 2577–2590 The first crystal structure of a ganglioside-binding antibody in complex with its target glycan headgroup. Structures of Fab-peptide complexes were also determined, but differences between carbohydrate and peptide recognition indicate functional and not structural mimicry by these peptides.
    • (2015) Mol Cell Proteomics , vol.14 , pp. 2577-2590
    • Horwacik, I.1    Golik, P.2    Grudnik, P.3    Kolinski, M.4    Zdzalik, M.5    Rokita, H.6    Dubin, G.7
  • 13
    • 84978636422 scopus 로고    scopus 로고
    • Perspectives on anti-glycan antibodies gleaned from development of a community resource database
    • 13 Sterner, E., Flanagan, N., Gildersleeve, J.C., Perspectives on anti-glycan antibodies gleaned from development of a community resource database. ACS Chem Biol 11 (2016), 1773–1783.
    • (2016) ACS Chem Biol , vol.11 , pp. 1773-1783
    • Sterner, E.1    Flanagan, N.2    Gildersleeve, J.C.3
  • 15
    • 1542572965 scopus 로고    scopus 로고
    • Evidence for structurally conserved recognition of the major carbohydrate xenoantigen by natural antibodies
    • 15 Ramsland, P.A., Farrugia, W., Yuriev, E., Edmundson, A.B., Sandrin, M.S., Evidence for structurally conserved recognition of the major carbohydrate xenoantigen by natural antibodies. Cell Mol Biol 49 (2003), 307–317.
    • (2003) Cell Mol Biol , vol.49 , pp. 307-317
    • Ramsland, P.A.1    Farrugia, W.2    Yuriev, E.3    Edmundson, A.B.4    Sandrin, M.S.5
  • 16
    • 84943254336 scopus 로고    scopus 로고
    • Antibody recognition of carbohydrate epitopes
    • A comprehensive review of all known structures of carbohydrate-antibodies. The text is conveniently divided into disease areas with a major emphasis on infection (e.g. HIV and bacteria) and cancer, but many useful details of other carbohydrate-binding antibodies and the target glycans are provided.
    • 16•• Haji-Ghassemi, O., Blackler, R.J., Martin Young, N., Evans, S.V., Antibody recognition of carbohydrate epitopes. Glycobiology 25 (2015), 920–952 A comprehensive review of all known structures of carbohydrate-antibodies. The text is conveniently divided into disease areas with a major emphasis on infection (e.g. HIV and bacteria) and cancer, but many useful details of other carbohydrate-binding antibodies and the target glycans are provided.
    • (2015) Glycobiology , vol.25 , pp. 920-952
    • Haji-Ghassemi, O.1    Blackler, R.J.2    Martin Young, N.3    Evans, S.V.4
  • 17
    • 84959235038 scopus 로고    scopus 로고
    • Antibody-carbohydrate recognition from docked ensembles using the automap procedure
    • 17 Dingjan, T., Agostino, M., Ramsland, P.A., Yuriev, E., Antibody-carbohydrate recognition from docked ensembles using the automap procedure. Methods Mol Biol 1331 (2015), 41–55.
    • (2015) Methods Mol Biol , vol.1331 , pp. 41-55
    • Dingjan, T.1    Agostino, M.2    Ramsland, P.A.3    Yuriev, E.4
  • 18
    • 22944433255 scopus 로고    scopus 로고
    • Three-dimensional structures of carbohydrate determinants of Lewis system antigens: implications for effective antibody targeting of cancer
    • 18 Yuriev, E., Farrugia, W., Scott, A.M., Ramsland, P.A., Three-dimensional structures of carbohydrate determinants of Lewis system antigens: implications for effective antibody targeting of cancer. Immunol Cell Biol 83 (2005), 709–717.
    • (2005) Immunol Cell Biol , vol.83 , pp. 709-717
    • Yuriev, E.1    Farrugia, W.2    Scott, A.M.3    Ramsland, P.A.4
  • 24
    • 22944474953 scopus 로고    scopus 로고
    • Carbohydrate vaccines as immunotherapy for cancer
    • 24 Slovin, S.F., Keding, S.J., Ragupathi, G., Carbohydrate vaccines as immunotherapy for cancer. Immunol Cell Biol 83 (2005), 418–428.
    • (2005) Immunol Cell Biol , vol.83 , pp. 418-428
    • Slovin, S.F.1    Keding, S.J.2    Ragupathi, G.3
  • 25
    • 84989856789 scopus 로고    scopus 로고
    • A novel chemoenzymatic synthesis of sulfated type 2 tumor-associated carbohydrate antigens via transglycosylation of sulfated Lewis X oxazoline catalyzed by keratanase II
    • 25 Yamazaki, Y., Sezukuri, K., Takada, J., Kimura, S., Ohmae, M., A novel chemoenzymatic synthesis of sulfated type 2 tumor-associated carbohydrate antigens via transglycosylation of sulfated Lewis X oxazoline catalyzed by keratanase II. Chembiochem 17 (2016), 1879–1886.
    • (2016) Chembiochem , vol.17 , pp. 1879-1886
    • Yamazaki, Y.1    Sezukuri, K.2    Takada, J.3    Kimura, S.4    Ohmae, M.5
  • 27
    • 3042561937 scopus 로고    scopus 로고
    • Structural convergence of antibody binding of carbohydrate determinants in Lewis Y tumor antigens
    • 27 Ramsland, P.A., Farrugia, W., Bradford, T.M., Hogarth, P.M., Scott, A.M., Structural convergence of antibody binding of carbohydrate determinants in Lewis Y tumor antigens. J Mol Biol 340 (2004), 809–818.
    • (2004) J Mol Biol , vol.340 , pp. 809-818
    • Ramsland, P.A.1    Farrugia, W.2    Bradford, T.M.3    Hogarth, P.M.4    Scott, A.M.5
  • 29
    • 46049113273 scopus 로고    scopus 로고
    • The hydration features of carbohydrate determinants of Lewis antigens
    • 29 Reynolds, M., Fuchs, A., Lindhorst, T.K., Perez, S., The hydration features of carbohydrate determinants of Lewis antigens. Mol Simul 34 (2008), 447–460.
    • (2008) Mol Simul , vol.34 , pp. 447-460
    • Reynolds, M.1    Fuchs, A.2    Lindhorst, T.K.3    Perez, S.4
  • 30
    • 84945980881 scopus 로고    scopus 로고
    • Uncovering nonconventional and conventional hydrogen bonds in oligosaccharides through NMR experiments and molecular modeling: application to sialyl Lewis-X
    • 30 Battistel, M.D., Azurmendi, H.F., Frank, M., Freedberg, D.I., Uncovering nonconventional and conventional hydrogen bonds in oligosaccharides through NMR experiments and molecular modeling: application to sialyl Lewis-X. J Am Chem Soc 137 (2015), 13444–13447.
    • (2015) J Am Chem Soc , vol.137 , pp. 13444-13447
    • Battistel, M.D.1    Azurmendi, H.F.2    Frank, M.3    Freedberg, D.I.4
  • 31
    • 84894059622 scopus 로고    scopus 로고
    • Evidence for two populated conformations for the dimeric Le(x) and Le(a)Le(x) tumor-associated carbohydrate antigens
    • 31 Jackson, T.A., Robertson, V., Auzanneau, F.I., Evidence for two populated conformations for the dimeric Le(x) and Le(a)Le(x) tumor-associated carbohydrate antigens. J Med Chem 57 (2014), 817–827.
    • (2014) J Med Chem , vol.57 , pp. 817-827
    • Jackson, T.A.1    Robertson, V.2    Auzanneau, F.I.3
  • 32
    • 84978734690 scopus 로고    scopus 로고
    • The hidden conformation of Lewis x, a human histo-blood group antigen, is a determinant for recognition by pathogen lectins
    • x can occur in solution and upon binding. These novel conformational properties of Lewis glycans should now be considered in future antibody development and vaccine design projects.
    • x can occur in solution and upon binding. These novel conformational properties of Lewis glycans should now be considered in future antibody development and vaccine design projects.
    • (2016) ACS Chem Biol , vol.11 , pp. 2011-2020
    • Topin, J.1    Lelimousin, M.2    Arnaud, J.3    Audfray, A.4    Perez, S.5    Varrot, A.6    Imberty, A.7
  • 33
    • 34250368055 scopus 로고    scopus 로고
    • Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling
    • 33 Fujita, A., Cheng, J., Hirakawa, M., Furukawa, K., Kusunoki, S., Fujimoto, T., Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling. Mol Biol Cell 18 (2007), 2112–2122.
    • (2007) Mol Biol Cell , vol.18 , pp. 2112-2122
    • Fujita, A.1    Cheng, J.2    Hirakawa, M.3    Furukawa, K.4    Kusunoki, S.5    Fujimoto, T.6
  • 34
    • 84905647126 scopus 로고    scopus 로고
    • Molecular recognition of gangliosides and their potential for cancer immunotherapies
    • Review of molecular properties and recognition of gangliosides by pathogen proteins and immune system proteins including antibodies. Antibody targeting of gangliosides for cancer immunotherapy is discussed.
    • 34• Krengel, U., Bousquet, P.A., Molecular recognition of gangliosides and their potential for cancer immunotherapies. Front Immunol, 5, 2014, 325 Review of molecular properties and recognition of gangliosides by pathogen proteins and immune system proteins including antibodies. Antibody targeting of gangliosides for cancer immunotherapy is discussed.
    • (2014) Front Immunol , vol.5 , pp. 325
    • Krengel, U.1    Bousquet, P.A.2
  • 35
    • 84877805975 scopus 로고    scopus 로고
    • In silico driven redesign of a clinically relevant antibody for the treatment of GD2 positive tumors
    • 35 Ahmed, M., Goldgur, Y., Hu, J., Guo, H.F., Cheung, N.K., In silico driven redesign of a clinically relevant antibody for the treatment of GD2 positive tumors. PLoS One, 8, 2013, e63359.
    • (2013) PLoS One , vol.8 , pp. e63359
    • Ahmed, M.1    Goldgur, Y.2    Hu, J.3    Guo, H.F.4    Cheung, N.K.5
  • 36
    • 0031171367 scopus 로고    scopus 로고
    • The crystal structure of a Fab fragment to the melanoma-associated GD2 ganglioside
    • 36 Pichla, S.L., Murali, R., Burnett, R.M., The crystal structure of a Fab fragment to the melanoma-associated GD2 ganglioside. J Struct Biol 119 (1997), 6–16.
    • (1997) J Struct Biol , vol.119 , pp. 6-16
    • Pichla, S.L.1    Murali, R.2    Burnett, R.M.3
  • 37
    • 84859941752 scopus 로고    scopus 로고
    • Antibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping
    • 37 Agostino, M., Yuriev, E., Ramsland, P.A., Antibody recognition of cancer-related gangliosides and their mimics investigated using in silico site mapping. PLoS One, 7, 2012, e35457.
    • (2012) PLoS One , vol.7 , pp. e35457
    • Agostino, M.1    Yuriev, E.2    Ramsland, P.A.3
  • 38
    • 0033605251 scopus 로고    scopus 로고
    • The role of homophilic binding in anti-tumor antibody R24 recognition of molecular surfaces. Demonstration of an intermolecular beta-sheet interaction between VH domains
    • 38 Kaminski, M.J., MacKenzie, C.R., Mooibroek, M.J., Dahms, T.E., Hirama, T., Houghton, A.N., Chapman, P.B., Evans, S.V., The role of homophilic binding in anti-tumor antibody R24 recognition of molecular surfaces. Demonstration of an intermolecular beta-sheet interaction between VH domains. J Biol Chem 274 (1999), 5597–5604.
    • (1999) J Biol Chem , vol.274 , pp. 5597-5604
    • Kaminski, M.J.1    MacKenzie, C.R.2    Mooibroek, M.J.3    Dahms, T.E.4    Hirama, T.5    Houghton, A.N.6    Chapman, P.B.7    Evans, S.V.8
  • 39
    • 1242272043 scopus 로고    scopus 로고
    • Structure and molecular interactions of a unique antitumor antibody specific for N-glycolyl GM3
    • 39 Krengel, U., Olsson, L.L., Martinez, C., Talavera, A., Rojas, G., Mier, E., Angstrom, J., Moreno, E., Structure and molecular interactions of a unique antitumor antibody specific for N-glycolyl GM3. J Biol Chem 279 (2004), 5597–5603.
    • (2004) J Biol Chem , vol.279 , pp. 5597-5603
    • Krengel, U.1    Olsson, L.L.2    Martinez, C.3    Talavera, A.4    Rojas, G.5    Mier, E.6    Angstrom, J.7    Moreno, E.8
  • 40
    • 70349464667 scopus 로고    scopus 로고
    • Crystal structure of an anti-ganglioside antibody, and modelling of the functional mimicry of its NeuGc-GM3 antigen by an anti-idiotypic antibody
    • 40 Talavera, A., Eriksson, A., Okvist, M., Lopez-Requena, A., Fernandez-Marrero, Y., Perez, R., Moreno, E., Krengel, U., Crystal structure of an anti-ganglioside antibody, and modelling of the functional mimicry of its NeuGc-GM3 antigen by an anti-idiotypic antibody. Mol Immunol 46 (2009), 3466–3475.
    • (2009) Mol Immunol , vol.46 , pp. 3466-3475
    • Talavera, A.1    Eriksson, A.2    Okvist, M.3    Lopez-Requena, A.4    Fernandez-Marrero, Y.5    Perez, R.6    Moreno, E.7    Krengel, U.8
  • 41
    • 33845596453 scopus 로고    scopus 로고
    • Gangliosides as components of lipid membrane domains
    • 41 Sonnino, S., Mauri, L., Chigorno, V., Prinetti, A., Gangliosides as components of lipid membrane domains. Glycobiology 17 (2007), 1R–13R.
    • (2007) Glycobiology , vol.17 , pp. 1R-13R
    • Sonnino, S.1    Mauri, L.2    Chigorno, V.3    Prinetti, A.4
  • 42
    • 84908326414 scopus 로고    scopus 로고
    • Lipid clustering correlates with membrane curvature as revealed by molecular simulations of complex lipid bilayers
    • Excellent theoretical study of the complex nature of biological membranes. Using molecular dynamics, the structure of a multicomponent lipid bilayer was simulated and among other observations it showed how gangliosides spontaneously cluster and are associated with regions of membrane curvature.
    • 42•• Koldso, H., Shorthouse, D., Helie, J., Sansom, M.S., Lipid clustering correlates with membrane curvature as revealed by molecular simulations of complex lipid bilayers. PLoS Comput Biol, 10, 2014, e1003911 Excellent theoretical study of the complex nature of biological membranes. Using molecular dynamics, the structure of a multicomponent lipid bilayer was simulated and among other observations it showed how gangliosides spontaneously cluster and are associated with regions of membrane curvature.
    • (2014) PLoS Comput Biol , vol.10 , pp. e1003911
    • Koldso, H.1    Shorthouse, D.2    Helie, J.3    Sansom, M.S.4
  • 43
    • 84923082197 scopus 로고    scopus 로고
    • Plasma membrane reorganization: a glycolipid gateway for microbes
    • Comprehensive review of the structural and molecular mechanisms for membrane reorganization, uptake and invasion mediated by pathogens and toxins. A major topic covered is the membrane protrusions and indentations that are associated with clustering of gangliosides, which may be of relevance to the direct membrane effects of many glycolipid-binding antibodies.
    • 43• Aigal, S., Claudinon, J., Romer, W., Plasma membrane reorganization: a glycolipid gateway for microbes. Biochim Biophys Acta 1853 (2015), 858–871 Comprehensive review of the structural and molecular mechanisms for membrane reorganization, uptake and invasion mediated by pathogens and toxins. A major topic covered is the membrane protrusions and indentations that are associated with clustering of gangliosides, which may be of relevance to the direct membrane effects of many glycolipid-binding antibodies.
    • (2015) Biochim Biophys Acta , vol.1853 , pp. 858-871
    • Aigal, S.1    Claudinon, J.2    Romer, W.3
  • 44
    • 84894442500 scopus 로고    scopus 로고
    • Immunoactive two-dimensional self-assembly of monoclonal antibodies in aqueous solution revealed by atomic force microscopy
    • 44 Ido, S., Kimiya, H., Kobayashi, K., Kominami, H., Matsushige, K., Yamada, H., Immunoactive two-dimensional self-assembly of monoclonal antibodies in aqueous solution revealed by atomic force microscopy. Nat Mater 13 (2014), 264–270.
    • (2014) Nat Mater , vol.13 , pp. 264-270
    • Ido, S.1    Kimiya, H.2    Kobayashi, K.3    Kominami, H.4    Matsushige, K.5    Yamada, H.6
  • 45
    • 0030604686 scopus 로고    scopus 로고
    • X-ray structure of the uncomplexed anti-tumor antibody BR96 and comparison with its antigen-bound form
    • 45 Sheriff, S., Chang, C.Y., Jeffrey, P.D., Bajorath, J., X-ray structure of the uncomplexed anti-tumor antibody BR96 and comparison with its antigen-bound form. J Mol Biol 259 (1996), 938–946.
    • (1996) J Mol Biol , vol.259 , pp. 938-946
    • Sheriff, S.1    Chang, C.Y.2    Jeffrey, P.D.3    Bajorath, J.4
  • 46
    • 70450187110 scopus 로고    scopus 로고
    • A possible role for metallic ions in the carbohydrate cluster recognition displayed by a Lewis Y specific antibody
    • 46 Farrugia, W., Scott, A.M., Ramsland, P.A., A possible role for metallic ions in the carbohydrate cluster recognition displayed by a Lewis Y specific antibody. PLoS One, 4, 2009, e7777.
    • (2009) PLoS One , vol.4 , pp. e7777
    • Farrugia, W.1    Scott, A.M.2    Ramsland, P.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.