Attachment of norovirus to histo blood group antigens: a cooperative multistep process. - Wikidata - wikimedia - TriplyDB

Attachment of norovirus to histo blood group antigens: a cooperative multistep process.

Attachment of norovirus to histo blood group antigens: a cooperative multistep process.

http://www.wikidata.org/entity/Q41020972

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Human Norovirus Interactions with Histo-Blood Group Antigens and Human Milk Oligosaccharides Current tools for norovirus drug discovery Structural Basis for Norovirus Inhibition by Human Milk Oligosaccharides.Epitope mapping of histo blood group antigens bound to norovirus VLPs using STD NMR experiments reveals fine details of molecular recognition.Recent advances in understanding noroviruses.Molecular analysis of norovirus in specimens from children enrolled in a 1982-1986 study in Belém, Brazil: A community-based longitudinal study.Molecular analysis of norovirus in specimens from children enrolled in a 1982-1986 study in Belém, Brazil: A community-based longitudinal study.Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistep-binding of l-fucose to norovirus particles.A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.Human Norovirus GII.4(MI001) P Dimer Binds Fucosylated and Sialylated Carbohydrates.Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization.

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Attachment of norovirus to histo blood group antigens: a cooperative multistep process.

http://www.wikidata.org/entity/Q41020972

description

2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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name

Attachment of norovirus to histo blood group antigens: a cooperative multistep process.

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Attachment of norovirus to histo blood group antigens: a cooperative multistep process.

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Attachment of norovirus to histo blood group antigens: a cooperative multistep process.

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Angewandte Chemie International Edition

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Attachment of norovirus to histo blood group antigens: a cooperative multistep process.

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Julia Lockhauserbäumer

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Thomas Peters

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P2860

The P domain of norovirus capsid protein forms dimer and binds to histo-blood group antigen receptors

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Structural basis for the recognition of blood group trisaccharides by norovirus

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

Structural Basis for Norovirus Inhibition and Fucose Mimicry by Citrate

The sweet quartet: Binding of fucose to the norovirus capsid

Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction

Human susceptibility and resistance to Norwalk virus infection

Comparison of experimental binding data and theoretical models in proteins containing subunits

Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.

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12014-12019

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scholarly article

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10.1002/ANIE.201505672

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41

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54

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Charlotte Uetrecht

Álvaro Mallagaray

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2015-08-19T00:00:00Z

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26329854

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