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Nature Chemical Biology, ISSN 1552-4450, 01/2014, Volume 10, Issue 1, pp. 7 - 8
Altered glycosylation of cancer cells confers phenotypic changes that promote spread and evasion of immune responses. A new method for engineering cell surface... 
B-CELL | SIGLECS | BIOCHEMISTRY & MOLECULAR BIOLOGY | Killer Cells, Natural - immunology | Immune Evasion | Glycocalyx - immunology | Humans | Sialic Acid Binding Immunoglobulin-like Lectins - physiology | Bioengineering | Genotype & phenotype | Glycoproteins | Glycosylation | Immunology | Cancer
Journal Article
Journal Article
Journal Article
Science, ISSN 0036-8075, 11/2011, Volume 334, Issue 6059, pp. 1097 - 1103
The HIV envelope (Env) protein gpl20 is protected from antibody recognition by a dense glycan shield. However, several of the recently identified PGT broadly... 
Polysaccharides | HIV | Neutralizing antibodies | RESEARCH ARTICLES | Antibodies | Viruses | Trimers | Epitopes | Grants | Binding sites | Crystal structure | PANEL | TRIMERS | MULTIDISCIPLINARY SCIENCES | IMMUNOGENS | ENVELOPE GLYCOPROTEIN COMPLEX | GP120 | HUMAN-IMMUNODEFICIENCY-VIRUS | MONOCLONAL-ANTIBODIES | TYPE-1 | Antibody Specificity | Mannose - immunology | Disaccharides - metabolism | Humans | Antibodies, Neutralizing - metabolism | Crystallography, X-Ray | Disaccharides - chemistry | Mannosides - chemistry | HIV Envelope Protein gp120 - metabolism | HIV Envelope Protein gp120 - immunology | Mannose - metabolism | Antibodies, Neutralizing - immunology | HIV-1 - physiology | HIV Antibodies - immunology | Immunoglobulin Fab Fragments - metabolism | Oligosaccharides - chemistry | Polysaccharides - chemistry | HIV Envelope Protein gp120 - chemistry | Mannose - chemistry | HIV Antibodies - metabolism | Protein Structure, Tertiary | Cell Line | Models, Molecular | Antibodies, Neutralizing - genetics | Glycosylation | Polysaccharides - immunology | Oligosaccharides - metabolism | HIV Antibodies - chemistry | Polysaccharides - metabolism | HIV-1 - immunology | Hydrogen Bonding | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | Oligosaccharides - immunology | Protein Conformation | Mannosides - metabolism | HIV Antibodies - genetics | Immunoglobulin Fab Fragments - immunology | Mutation | Binding Sites, Antibody | Carbohydrate Conformation | Viral antibodies | Physiological aspects | Development and progression | Glycoproteins | HIV (Viruses) | Health aspects | Proteins | Antigens | Immunoglobulins | Human immunodeficiency virus--HIV
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2012, Volume 7, Issue 6, p. e39039
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 01/2018, Volume 115, Issue 3, p. E372
One goal of regenerative medicine is to repair damaged tissue. This requires not only generating new cells of the proper phenotype, but also selecting for... 
Brain | Immunoglobulins | Phenotypes | Neurodegenerative diseases | Tissue engineering | Trafficking | Antibodies | Stem cell transplantation | Regeneration (physiology) | Microglia | Embryonic growth stage | Regeneration | Embryogenesis | Presenilin 1 | Stem cells | Bone marrow | Brain damage | Adults | Bone | Alzheimers disease | Alzheimer's disease | Cell migration
Journal Article
Science, ISSN 0036-8075, 4/2006, Volume 312, Issue 5772, pp. 404 - 410
The hemagglutinin (HA) structure at 2.9 angstrom resolution, from a highly pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918 and other... 
Polysaccharides | Receptors | Viruses | Ligands | Trimers | Viral morphology | Research Articles | H5N1 subtype influenza A virus | Genetic mutation | Monomers | Virology | OLIGOSACCHARIDES | EVOLUTION | FUSION | DETERMINANTS | SUBTYPES | MULTIDISCIPLINARY SCIENCES | HUMANS | SIALIC-ACID | GLYCOSYLATION | GLYCOPEPTIDES | BINDING PROPERTIES | Species Specificity | Receptors, Virus - metabolism | Humans | Virulence | Molecular Sequence Data | Crystallography, X-Ray | Influenza A Virus, H5N1 Subtype - genetics | Respiratory Mucosa - virology | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Sialic Acids - chemistry | Hemagglutinin Glycoproteins, Influenza Virus - genetics | Lung - virology | Cloning, Molecular | Influenza A Virus, H5N1 Subtype - metabolism | Binding Sites | Protein Structure, Tertiary | Amino Acid Sequence | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Antigenic Variation | Sialic Acids - metabolism | Models, Molecular | Birds | Glycosylation | Hemagglutinin Glycoproteins, Influenza Virus - metabolism | Protein Folding | Polysaccharides - metabolism | Animals | Receptors, Virus - chemistry | Influenza A Virus, H5N1 Subtype - chemistry | Influenza A Virus, H5N1 Subtype - pathogenicity | Protein Conformation | Mutation | Carbohydrate Conformation | Amino Acid Substitution | Avian influenza | Agglutination tests | Research | Analysis
Journal Article