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The P domain of norovirus capsid protein forms dimer and binds to histo-blood group antigen receptors
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C-terminal arginine cluster is essential for receptor binding of norovirus capsid protein
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Tan M, Meller J, Jiang X. C-terminal arginine cluster is essential for receptor binding of norovirus capsid protein. J Virol 2006; 80:7322-31.
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Structural basis for the receptor binding specificity of Norwalk virus
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Bu W, Mamedova A, Tan M, Xia M, Jiang X, Hegde RS. Structural basis for the receptor binding specificity of Norwalk virus. J Virol 2008; 82:5340-7.
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Structural basis for the recognition of blood group trisaccharides by norovirus
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Cao S, Lou Z, Tan M et al. Structural basis for the recognition of blood group trisaccharides by norovirus. J Virol 2007; 81:5949-57.
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Crystallography of a Lewis-binding norovirus, elucidation of strain-specificity to the polymorphic human histo-blood group antigens
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Chen Y, Tan M, Xia M et al. Crystallography of a Lewis-binding norovirus, elucidation of strain-specificity to the polymorphic human histo-blood group antigens. PLoS Pathogens 2011; 7:e1002152.
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Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus
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Choi JM, Hutson AM, Estes MK, Prasad BV. Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus. Proc Natl Acad Sci U S A 2008; 105:9175-80.
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Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability
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Hansman GS, Biertumpfel C, Georgiev I, McLellan JS, Chen L, Zhou T, Katayama K, Kwong PD. Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. J Virol 2011; 85:6687-701.
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Structural analysis of histo-blood group antigen binding specificity in a norovirus GII.4 epidemic variant: implications for epochal evolution
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Shanker S, Choi JM, Sankaran B, Atmar RL, Estes MK, Prasad BV. Structural analysis of histo-blood group antigen binding specificity in a norovirus GII.4 epidemic variant: implications for epochal evolution. J Virol 2011; 85:8635-45.
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Terminal modifications of norovirus P domain resulted in a new type of subviral particles, the small P particles
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Tan M, Fang PA, Xia M, Chachiyo T, Jiang W, Jiang X. Terminal modifications of norovirus P domain resulted in a new type of subviral particles, the small P particles. Virology 2011; 410:345-52.
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Noroviral P particle: structure, function and applications in virus-host interaction
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Tan M, Fang P, Chachiyo T, Xia M, Huang P, Fang Z, Jiang W, Jiang X. Noroviral P particle: structure, function and applications in virus-host interaction. Virology 2008; 382:115-23.
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Norovirus P particle, a novel platform for vaccine development and antibody production
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The P domain of norovirus capsid protein forms a subviral particle that binds to histo-blood group antigen receptors
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Tan M, Jiang X. The P domain of norovirus capsid protein forms a subviral particle that binds to histo-blood group antigen receptors. J Virol 2005; 79:14017-30.
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Production and characterization of virus-like particles and the P domain protein of GII.4 norovirus
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Conservation of carbohydrate binding interfaces: evidence of human HBGA selection in norovirus evolution
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Tan M, Xia M, Chen Y, Bu W, Hegde RS, Meller J, Li X, Jiang X. Conservation of carbohydrate binding interfaces: evidence of human HBGA selection in norovirus evolution. PLoS One 2009; 4:e5058.
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A candidate dual vaccine against influenza and noroviruses
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Xia M, Tan M, Wei C, Zhong W, Wang L, McNeal M, Jiang X. A candidate dual vaccine against influenza and noroviruses. Vaccine 2011; 29:7670-7.
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