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Volumn 21, Issue 1, 2017, Pages 23-34

Recent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased Avidity

Author keywords

airway; bidentate binding; chemo enzymatic synthesis; extended branched glycans; H3N2; hemagglutinin; influenza virus; poly N acetyl lactosamine; receptor specificity; sialoside microarray

Indexed keywords

GLYCAN; HEMAGGLUTININ; LACTOSE; LIPID; POLY N ACETYL LACTOSAMINE; RECEPTOR; SIALIDASE; UNCLASSIFIED DRUG; GALACTAN; INFLUENZA VIRUS HEMAGGLUTININ; N ACETYLNEURAMINIC ACID; POLY-N-ACETYLGALACTOSAMINE; POLYSACCHARIDE; VIRUS RECEPTOR;

EID: 85009935441     PISSN: 19313128     EISSN: 19346069     Source Type: Journal    
DOI: 10.1016/j.chom.2016.11.004     Document Type: Article
Times cited : (155)

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