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1. Full Text Immunology: Glyco-engineering 'super-self'
by Macauley, Matthew S and Paulson, James C
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
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2. Full Text Molecular Basis for the Generation in Pigs of Influenza A Viruses with Pandemic Potential
by Toshihiro Ito and J. Nelson S. S. Couceiro and Sørge Kelm and Linda G. Baum and Scott Krauss and Maria R. Castrucci and Isabella Donatelli and Hiroshi Kida and James C. Paulson and Robert G. Webster and Yoshihiro Kawaoka
Journal of Virology, ISSN 0022-538X, 09/1998, Volume 72, Issue 9, pp. 7367 - 7373
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
REPLICATION | EVOLUTION | VIROLOGY | H3N2 VIRUSES | HEMAGGLUTININ | SPECIFICITY | A VIRUSES | SWINE | RECEPTOR DETERMINANTS | SEQUENCE | INFECTION | Amino Acid Sequence | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Influenza A virus - physiology | Receptors, Virus - metabolism | Humans | Adaptation, Biological | Molecular Sequence Data | Phylogeny | Hemagglutinin Glycoproteins, Influenza Virus - metabolism | Amino Acids | Ducks | Trachea - virology | Sequence Homology, Amino Acid | Animals | Influenza A virus - metabolism | Receptors, Virus - chemistry | Swine | Influenza A virus - classification | Binding Sites | Animal Viruses
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3. Full Text Siglec-mediated regulation of immune cell function in disease
by Macauley, Matthew S and Crocker, Paul R and Paulson, James C
Nature Reviews Immunology, ISSN 1474-1733, 09/2014, Volume 14, Issue 10, pp. 653 - 666
All mammalian cells display a diverse array of glycan structures that differ from those that are found on microbial pathogens. Siglecs are a family of sialic... 
COMMON VARIANTS | OBSTRUCTIVE PULMONARY-DISEASE | GEMTUZUMAB OZOGAMICIN | ACID-BINDING LECTIN | SIGNALING MOLECULE | DEFICIENT MICE | IMMUNOLOGY | TUMOR-PRODUCED MUCINS | CD33-RELATED SIGLECS | OSTEOCLAST DIFFERENTIATION | GLYCAN LIGANDS | N-Acetylneuraminic Acid - immunology | Sialic Acid Binding Immunoglobulin-like Lectins - metabolism | Humans | Disease Resistance - immunology | Polysaccharides - immunology | Immune System - cytology | Protein Binding - immunology | N-Acetylneuraminic Acid - metabolism | Polysaccharides - metabolism | Sialic Acid Binding Immunoglobulin-like Lectins - immunology | Models, Immunological | Animals | Disease Susceptibility - immunology | Immune System - metabolism | Immune System - immunology | Immune response | Lectins | Physiological aspects | Research | Biological control systems | Health aspects | Immunological research
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4. Full Text Siglecs and their roles in the immune system
by Crocker, Paul R and Varki, Ajit and Paulson, James C
Nature Reviews Immunology, ISSN 1474-1733, 04/2007, Volume 7, Issue 4, pp. 255 - 266
Cell surfaces in the immune system are richly equipped with a complex mixture of glycans, which can be recognized by diverse glycan-binding proteins. The... 
PLASMACYTOID DENDRITIC CELLS | B-CELLS | NATURAL-KILLER-CELLS | ACID-BINDING-RECEPTOR | IMMUNOGLOBULIN-LIKE LECTINS | ALPHA-2,6-LINKED SIALIC ACIDS | PROTEIN-TYROSINE PHOSPHATASES | MYELOID-LEUKEMIA CELLS | IMMUNOLOGY | MYELIN-ASSOCIATED GLYCOPROTEIN | I-TYPE LECTINS | Lymphocytes - metabolism | Protein Structure, Tertiary | Antigens, CD - immunology | Cell Communication - immunology | Lectins - immunology | Humans | Sialic Acid Binding Ig-like Lectin 2 - immunology | N-Acetylneuraminic Acid - metabolism | Antigens, CD - metabolism | N-Acetylneuraminic Acid - chemistry | Signal Transduction - immunology | Endocytosis | Lymphocyte Activation - immunology | Animals | Lymphocytes - immunology | Sialic Acid Binding Ig-like Lectin 2 - metabolism | Antigens, Differentiation, Myelomonocytic - metabolism | Sialic Acid Binding Immunoglobulin-like Lectins | Lectins - chemistry | Sialic Acid Binding Ig-like Lectin 3 | Antigens, Differentiation, Myelomonocytic - immunology | Immunoglobulins | Immune response | Analysis | Regulation | Research | Gene expression | Sialic acids | Membrane proteins
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5. Full Text New World Bats Harbor Diverse Influenza A Viruses
by Tong, Suxiang and Zhu, Xueyong and Li, Yan and Shi, Mang and Zhang, Jing and Bourgeois, Melissa and Yang, Hua and Chen, Xianfeng and Recuenco, Sergio and Gomez, Jorge and Chen, Li-Mei and Johnson, Adam and Tao, Ying and Dreyfus, Cyrille and Yu, Wenli and McBride, Ryan and Carney, Paul J and Gilbert, Amy T and Chang, Jessie and Guo, Zhu and Davis, Charles T and Paulson, James C and Stevens, James and Rupprecht, Charles E and Holmes, Edward C and Wilson, Ian A and Donis, Ruben O
PLoS Pathogens, ISSN 1553-7366, 10/2013, Volume 9, Issue 10, p. e1003657
Aquatic birds harbor diverse influenza A viruses and are a major viral reservoir in nature. The recent discovery of influenza viruses of a new H17N10 subtype... 
NEURAMINIDASE | HEMAGGLUTININ MEMBRANE GLYCOPROTEIN | MAXIMUM-LIKELIHOOD | PHYLOGENIES | VIROLOGY | SEGMENT 3 | PB2 PROTEIN | MICROBIOLOGY | VIRAL POLYMERASE | BINDING | SARS-LIKE | PARASITOLOGY | Orthomyxoviridae Infections - epidemiology | Chiroptera - virology | Animals | Orthomyxoviridae Infections - veterinary | Disease Reservoirs - virology | Influenza A virus - genetics | Peru - epidemiology | Phylogeny | Hemagglutinin Glycoproteins, Influenza Virus - genetics | Orthomyxoviridae Infections - genetics | Influenza viruses | Physiological aspects | Host-parasite relationships | Bats | Research | Health aspects | Studies | Pandemics | Disease control | Influenza
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6. Full Text A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield
by Robert Pejchal and Katie J. Doores and Laura M. Walker and Reza Khayat and Po-Ssu Huang and Sheng-Kai Wang and Robyn L. Stanfield and Jean-Philippe Julien and Alejandra Ramos and Max Crispin and Rafael Depetris and Umesh Katpally and Andre Marozsan and Albert Cupo and Sebastien Maloveste and Yan Liu and Ryan McBride and Yukishige Ito and Rogier W. Sanders and Cassandra Ogohara and James C. Paulson and Ten Feizi and Christopher N. Scanlan and Chi-Huey Wong and John P. Moore and William C. Olson and Andrew B. Ward and Pascal Poignard and William R. Schief and Dennis R. Burton and Ian A. Wilson
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
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7. Full Text Antigen delivery to macrophages using liposomal nanoparticles targeting Sialoadhesin/CD169
by Chen, Weihsu C and Kawasaki, Norihito and Nycholat, Corwin M and Han, Shoufa and Pilotte, Julie and Crocker, Paul R and Paulson, James C
PLoS ONE, ISSN 1932-6203, 06/2012, Volume 7, Issue 6, p. e39039
Sialoadhesin (Sn, Siglec-1, CD169) is a member of the sialic acid binding Ig-like lectin (siglec) family expressed on macrophages. Its macrophage specific... 
B-CELLS | IN-VITRO | DENDRITIC CELLS | LIGANDS | IMMUNE-RESPONSES | MULTIDISCIPLINARY SCIENCES | LYMPH-NODE | LEWIS-X | BINDING-RECEPTOR | RECEPTOR SIALOADHESIN | T-CELLS | Cell Line | Gene Expression | Nanoparticles - chemistry | Ovalbumin - immunology | Humans | Mice, Inbred C57BL | Antigens - metabolism | Muramidase - metabolism | Endosomes - metabolism | Mice, Knockout | Sialic Acid Binding Ig-like Lectin 1 - genetics | Antigens - administration & dosage | CD4-Positive T-Lymphocytes - immunology | Liposomes - chemistry | Lymphocyte Activation - immunology | Macrophages - metabolism | Animals | Ovalbumin - administration & dosage | Sialic Acid Binding Ig-like Lectin 1 - metabolism | Protein Binding | Antigens - immunology | Mice | Macrophages - immunology | Endocytosis - immunology | Nanoparticles | Lectins | Antigens | Amino acids | T cells | Macrophages | Cell proliferation | Antigen presentation | Immunoglobulins | Blood & organ donations | Dendritic cells | Lipids | Lymphocytes T | Organelles | Glycan | Endocytosis | Lymphocytes | Immunotherapy | Bone marrow | Ligands | Physiology | Lymphomas | Liposomes | Molecular biology | Autoimmune diseases | Cancer
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8. Migration-based selections of antibodies that convert bone marrow into trafficking microglia-like cells that reduce brain amyloid ß
by Kyung Ho Han and Britni M Arlian and Matthew S Macauley and James C Paulson and Richard A Lerner
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
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9. Full Text Structure and Receptor Specificity of the Hemagglutinin from an H5N1 Influenza Virus
by James Stevens and Ola Blixt and Terrence M. Tumpey and Jeffery K. Taubenberger and James C. Paulson and Ian A. Wilson
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
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