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H5N1 chicken influenza viruses display a high binding affinity for Neu5Acα2-3Galβ1-4(6-HSO 3)GlcNAc-containing receptors

Virology (New York, N.Y.), 2004-09, Vol.326 (2), p.310-316

2004

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Specification of Receptor-Binding Phenotypes of Influenza Virus Isolates from Different Hosts Using Synthetic Sialylglycopolymers: Non-Egg-Adapted Human H1 and H3 Influenza A and Influenza B Viruses Share a Common High Binding Affinity for 6′-Sialyl(N-acetyllactosamine)

Virology (New York, N.Y.), 1997-06, Vol.232 (2), p.345-350

1997

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Natural antibodies to glycans

Biochemistry (Moscow), 2013-07, Vol.78 (7), p.786-797

Bovin, N. V.

2013

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Postreassortment Changes in Influenza A Virus Hemagglutinin Restoring HA–NA Functional Match

Virology (New York, N.Y.), 1998-05, Vol.244 (2), p.315-321

1998

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Hypotheses of the origin of natural antibodies: A glycobiologist’s opinion

Biochemistry (Moscow), 2015-07, Vol.80 (7), p.820-835

2015

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Assessment of core-shell nanoparticles surface structure heterogeneity by SAXS contrast variation and ab initio modeling

Colloids and surfaces, B, Biointerfaces, 2023-04, Vol.224, p.113183-113183, Article 113183

2023

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Effects of Host-Dependent Glycosylation of Hemagglutinin on Receptor-Binding Properties of H1N1 Human Influenza A Virus Grown in MDCK Cells and in Embryonated Eggs

Virology (New York, N.Y.), 1998-08, Vol.247 (2), p.170-177

1998

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Human antibodies eluted from ligand-free Sepharose capable of binding bacterial polysaccharides and sulfated glycans

Molecular immunology, 2019-02, Vol.106, p.63-68

2019

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Specificity of human galectins on cell surfaces

Biochemistry (Moscow), 2015-07, Vol.80 (7), p.846-856

2015

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Expression of fucosylated glycans in endothelial glycocalyces of placental villi at early and late fetal growth restriction

Placenta (Eastbourne), 2020-01, Vol.90, p.98-102

2020

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The Repertoire of Human Antiglycan Antibodies and Its Dynamics in the First Year of Life

Biochemistry (Moscow), 2019-06, Vol.84 (6), p.608-616

2019

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Changes in the Receptor-Binding Properties of H3N2 Viruses during Long-Term Circulation in Humans

Biochemistry (Moscow), 2019-10, Vol.84 (10), p.1177-1185

2019

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Ligands for Siglec-8 and Siglec-F: Binding Characteristics and Tissue Distribution

Journal of allergy and clinical immunology, 2007, Vol.119 (1), p.S299-S299

2007

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Receptor specificity of H5 influenza virus escape mutants

Virus research, 2004-03, Vol.100 (2), p.237-241

2004

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Localization of Galectins within Glycocalyx

Biochemistry (Moscow), 2018-06, Vol.83 (6), p.727-737

2018

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Isolation of IgG Associated with Human Placenta

Bulletin of experimental biology and medicine, 2019-05, Vol.167 (1), p.120-122

2019

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Probing of the Receptor-Binding Sites of the H1 and H3 Influenza A and Influenza B Virus Hemagglutinins by Synthetic and Natural Sialosides

Virology (New York, N.Y.), 1993-09, Vol.196 (1), p.111-121

1993

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Structure, functions, and biosynthesis of glycoconjugates of Leishmania spp. cell surface

Biochemistry (Moscow), 2010-06, Vol.75 (6), p.686-694

2010

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Endogenous lectins as targets for drug delivery

Advanced drug delivery reviews, 2000-09, Vol.43 (2), p.225-244

2000

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Synthetic polymeric sialoside inhibitors of influenza virus receptor-binding activity

FEBS letters, 1990-10, Vol.272 (1), p.209-212

1990

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Design of carbohydrate multiarrays

Biochimica et biophysica acta, 2006-04, Vol.1760 (4), p.603-609

2006

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Hydrogel glycan microarrays

Analytical biochemistry, 2005-12, Vol.347 (1), p.94-105

2005

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GlycoChip: multiarray for the study of carbohydrate-binding proteins

Lab on a chip, 2003-01, Vol.3 (4), p.260-265

2003

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Carbohydrate specificity of chicken and human tandem-repeat-type galectins-8 in composition of cells

Biochemistry (Moscow), 2011-10, Vol.76 (10), p.1185-1192

2011

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Galectins promote the interaction of influenza virus with its target cell

Biochemistry (Moscow), 2011-08, Vol.76 (8), p.958-967

2011

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H5N1 chicken influenza viruses display a high binding affinity for Neu5Acα2-3Galβ1-4(6-HSO 3)GlcNAc-containing receptors

Specification of Receptor-Binding Phenotypes of Influenza Virus Isolates from Different Hosts Using Synthetic Sialylglycopolymers: Non-Egg-Adapted Human H1 and H3 Influenza A and Influenza B Viruses Share a Common High Binding Affinity for 6′-Sialyl(N-acetyllactosamine)

Natural antibodies to glycans

Postreassortment Changes in Influenza A Virus Hemagglutinin Restoring HA–NA Functional Match

Hypotheses of the origin of natural antibodies: A glycobiologist’s opinion

Assessment of core-shell nanoparticles surface structure heterogeneity by SAXS contrast variation and ab initio modeling

Effects of Host-Dependent Glycosylation of Hemagglutinin on Receptor-Binding Properties of H1N1 Human Influenza A Virus Grown in MDCK Cells and in Embryonated Eggs

Human antibodies eluted from ligand-free Sepharose capable of binding bacterial polysaccharides and sulfated glycans

Specificity of human galectins on cell surfaces

Expression of fucosylated glycans in endothelial glycocalyces of placental villi at early and late fetal growth restriction

The Repertoire of Human Antiglycan Antibodies and Its Dynamics in the First Year of Life

Changes in the Receptor-Binding Properties of H3N2 Viruses during Long-Term Circulation in Humans

Ligands for Siglec-8 and Siglec-F: Binding Characteristics and Tissue Distribution

Receptor specificity of H5 influenza virus escape mutants

Localization of Galectins within Glycocalyx

Isolation of IgG Associated with Human Placenta

Probing of the Receptor-Binding Sites of the H1 and H3 Influenza A and Influenza B Virus Hemagglutinins by Synthetic and Natural Sialosides

Structure, functions, and biosynthesis of glycoconjugates of Leishmania spp. cell surface

Endogenous lectins as targets for drug delivery

Synthetic polymeric sialoside inhibitors of influenza virus receptor-binding activity

Design of carbohydrate multiarrays

Hydrogel glycan microarrays

GlycoChip: multiarray for the study of carbohydrate-binding proteins

Carbohydrate specificity of chicken and human tandem-repeat-type galectins-8 in composition of cells

Galectins promote the interaction of influenza virus with its target cell

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