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Journal of Molecular Biology, ISSN 0022-2836, 09/2014, Volume 426, Issue 18, pp. 3166 - 3179
Journal Article
JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, 03/2018, Volume 293, Issue 10, pp. 3477 - 3489
CD16a/Fc gamma receptor IIIa is the most abundant antibody Fc receptor expressed on human natural killer (NK) cells and activates a protective cytotoxic... 
NATURAL-KILLER-CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLYCOFORMS | THERAPEUTIC ANTIBODIES | CARBOHYDRATE | HIGH-AFFINITY BINDING | GLYCOSYLATION | TISSUES | EXPRESSION | CANCER | RIIIA | Immunoglobulin Fc Fragments - metabolism | Humans | Receptors, IgG - chemistry | Male | Recombinant Fusion Proteins - metabolism | Receptors, IgG - metabolism | Receptors, IgG - agonists | Receptors, IgG - genetics | HEK293 Cells | Killer Cells, Natural - immunology | Polysaccharides - chemistry | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Antibodies, Monoclonal - chemistry | Carbohydrate Sequence | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Antibodies, Monoclonal - pharmacology | Cells, Cultured | Solubility | Models, Molecular | Recombinant Proteins - chemistry | Immunoglobulin Fc Fragments - chemistry | Glycosylation | Recombinant Fusion Proteins - chemistry | Polysaccharides - metabolism | Antibodies, Monoclonal - genetics | Cell Lineage | Killer Cells, Natural - cytology | Peptide Fragments - chemistry | Peptide Fragments - agonists | Ligands | Protein Conformation | Aged | Killer Cells, Natural - drug effects | Protein Processing, Post-Translational | Antibodies, Monoclonal - metabolism | Killer Cells, Natural - metabolism | Immunoglobulin Fc Fragments - genetics | Index Medicus | Editors' Picks | post-translational modification (PTM) | Fc γ receptors IIIa | antibody | glycomics | protein glycosylation | glycosylation | N-glycan | Fc γ receptor | protein secretion
Journal Article
Science, ISSN 0036-8075, 4/2008, Volume 320, Issue 5874, pp. 373 - 376
It is well established that high doses of monomeric immunoglobulin G (IgG) purified from pooled human plasma [intravenous immunoglobulin (IVIG)] confer... 
Fc receptors | Polysaccharides | Immunoglobulins | Antiinflammatories | Lectins | Antibodies | Cytotoxicity | Recapitulation theory | Idiopathic thrombocytopenic purpura | Reports | Post hoc | OLIGOSACCHARIDES | SPECIFICITY | PROTECTION | MULTIDISCIPLINARY SCIENCES | SIALYLATION | RECEPTOR | GLYCOSYLATION | IMMUNOGLOBULIN-G | AUTOIMMUNE-DISEASE | BINDING | SIALYLTRANSFERASE | Recombinant Proteins - therapeutic use | Arthritis, Experimental - drug therapy | Immunoglobulin Fc Fragments - metabolism | Humans | Receptors, Fc - metabolism | Immunoglobulins, Intravenous - administration & dosage | Anti-Inflammatory Agents, Non-Steroidal - chemistry | Immunoglobulin Fc Fragments - administration & dosage | Purpura, Thrombocytopenic, Idiopathic - drug therapy | Polysaccharides - chemistry | Immunoglobulin Fc Fragments - therapeutic use | Autoimmune Diseases - drug therapy | Immunoglobulin G - chemistry | Mice, Inbred C57BL | Immunoglobulin G - therapeutic use | Recombinant Proteins - chemistry | Immunoglobulin Fc Fragments - chemistry | Glycosylation | Immunoglobulin G - administration & dosage | N-Acetylneuraminic Acid - chemistry | Galactose - chemistry | Animals | Immunoglobulins, Intravenous - therapeutic use | Anti-Inflammatory Agents, Non-Steroidal - therapeutic use | Anti-Inflammatory Agents, Non-Steroidal - administration & dosage | Mice, Inbred NOD | Immunoglobulins, Intravenous - chemistry | Mice | Carbohydrate Conformation | Immunoglobulin G - metabolism | Influence | Anti-inflammatory drugs | Properties | Recombinant molecules | Immunoglobulin G | Biochemistry | Immunology | Drug therapy | Autoimmune diseases | Immune system | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2013, Volume 110, Issue 24, pp. 9868 - 9872
Immunoglobulins recognize and clear microbial pathogens and toxins through the coupling of variable region specificity to Fc-triggered cellular activation.... 
Molecules | Polysaccharides | Receptors | Immunoglobulins | Antiinflammatories | Hydrogen bonds | Surface areas | Lectins | Amino acids | Biochemistry | Conformational change | Sialylated IgG Fc | ANTIINFLAMMATORY ACTIVITY | FC-EPSILON-RI | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | GLYCOSYLATION | conformational change | HUMAN-IGG-FC | sialylated IgG Fc | DC-SIGN | FRAGMENT | CD23 | BINDING | REVEALS | Cell Adhesion Molecules - genetics | Cricetulus | Immunoglobulin Fc Fragments - metabolism | Humans | Lectins, C-Type - immunology | Cell Adhesion Molecules - immunology | Lectins, C-Type - genetics | Receptors, IgG - metabolism | Lectins, C-Type - metabolism | Thermodynamics | Immunoglobulin Fc Fragments - immunology | Receptors, IgE - immunology | Binding Sites | Circular Dichroism | CHO Cells | Binding, Competitive | Protein Structure, Tertiary | Cricetinae | Sialic Acids - metabolism | Models, Molecular | Receptors, Cell Surface - metabolism | Immunoglobulin Fc Fragments - chemistry | Glycosylation | Receptors, IgE - genetics | Receptors, IgG - immunology | Cell Adhesion Molecules - metabolism | Receptors, Cell Surface - immunology | Spectrophotometry, Ultraviolet | Animals | Receptors, IgE - metabolism | Protein Binding | Receptors, Cell Surface - genetics | Physiological aspects | Dendritic cells | Health aspects | Ligands (Biochemistry) | Pathogens | Toxins | Microbiology | Cell adhesion & migration | Index Medicus | Biological Sciences
Journal Article
Journal Article
Blood, ISSN 0006-4971, 2014, Volume 124, Issue 25, pp. 3709 - 3718
Journal Article
Journal Article
NATURE IMMUNOLOGY, ISSN 1529-2908, 08/2017, Volume 18, Issue 8, pp. 889 - 889
Journal Article
Journal of Thrombosis and Haemostasis, ISSN 1538-7933, 01/2013, Volume 11, Issue 1, pp. 132 - 141
Background:  Hemophilia A results from a deficiency in factor VIII activity. Current treatment regimens require frequent dosing, owing to the short half‐life... 
Fc fusion | hemophilia A | long‐acting | rFVIIIFc | Factor VIII | RFVIIIFc | Long-acting | Hemophilia A | DOMAIN | HEMOPHILIA-A | FACTOR-IX | PROLONGED ACTIVITY | PERIPHERAL VASCULAR DISEASE | HEMATOLOGY | long-acting | Recombinant Fusion Proteins - pharmacology | Immunoglobulin Fc Fragments - metabolism | Factor VIII - pharmacokinetics | Humans | Half-Life | Male | Structure-Activity Relationship | Coagulants - chemistry | Neoplasm Proteins - metabolism | Cysteine Endopeptidases - metabolism | Coagulants - pharmacology | Mass Spectrometry | Cloning, Molecular | Protein Engineering | Coagulants - pharmacokinetics | Protein Stability | Binding Sites | Disease Models, Animal | von Willebrand Factor - metabolism | Amino Acid Sequence | Thrombelastography | Factor VIII - chemistry | Factor VIII - genetics | Immunoglobulin Fc Fragments - chemistry | Peptide Mapping - methods | Hemophilia A - blood | Animals | Blood Coagulation - drug effects | Partial Thromboplastin Time | Recombinant Fusion Proteins - pharmacokinetics | Factor VIII - pharmacology | Protein Conformation | Mice | Protein C - metabolism | Hemophilia A - drug therapy | Immunoglobulin Fc Fragments - genetics | Proteins | Blood coagulation factor VIII | Medical examination | Analysis | Immunoglobulin G | Questions and answers | Hemophilia | Thrombin | Liquid chromatography | Chemical properties | Mass spectrometry | Blood | Index Medicus | Coagulation
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2006, Volume 103, Issue 11, pp. 4005 - 4010
Journal Article