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CrystEngComm, ISSN 1466-8033, 04/2016, Volume 18, Issue 16, pp. 2820 - 2824
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 06/2017, Volume 292, Issue 24, pp. 9975 - 9987
Immunoglobulin E and its interactions with receptors Fc is an element of RI and CD23 play a central role in allergic disease. Omalizumab, a clinically approved... 
RECEPTOR COMPLEXES | DOMAIN | FC-EPSILON-RI | CONFORMATIONAL-CHANGES | AFFINITY | CRYSTAL-STRUCTURE | BENT | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOCLONAL-ANTIBODY | MAMMALIAN-CELLS | BINDING | Surface Plasmon Resonance | Omalizumab - genetics | Recombinant Fusion Proteins - pharmacology | Immunoglobulin Fc Fragments - metabolism | Humans | Omalizumab - metabolism | Crystallography, X-Ray | Recombinant Fusion Proteins - metabolism | Receptors, IgE - chemistry | Immunoglobulin E - genetics | Immunoglobulin Fab Fragments - metabolism | Fluorescence Resonance Energy Transfer | Protein Interaction Domains and Motifs | Recombinant Proteins - metabolism | Anti-Asthmatic Agents - pharmacology | Omalizumab - chemistry | Pliability | Immunoglobulin Fab Fragments - genetics | Immunoglobulin E - metabolism | Protein Refolding | Solubility | Models, Molecular | Receptors, IgE - antagonists & inhibitors | Recombinant Proteins - chemistry | Immunoglobulin Fc Fragments - chemistry | Recombinant Fusion Proteins - chemistry | Recombinant Proteins - pharmacology | Immunoglobulin Fab Fragments - pharmacology | Immunoglobulin E - chemistry | Point Mutation | Receptors, IgE - metabolism | Immunoglobulin Fab Fragments - chemistry | Omalizumab - pharmacology | Allosteric Site | Immunoglobulin Fc Fragments - pharmacology | Protein Conformation | Immunoglobulin Fc Fragments - genetics | Amino Acid Substitution | Index Medicus | X-ray crystallography | Immunology | antibody | immunoglobulin E (IgE) | allergy | omalizumab | allosteric regulation
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 03/2013, Volume 110, Issue 13, pp. 5145 - 5150
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
PLoS pathogens, ISSN 1553-7366, 2013, Volume 9, Issue 9, pp. e1003618 - e1003618
A desirable but as yet unachieved property of a human immunodeficiency virus type 1 (HIV-1) vaccine candidate is the ability to induce broadly neutralizing... 
ENVELOPE GLYCOPROTEIN TRIMERS | PROTEIN | VACCINE | GP41 | MICROBIOLOGY | GP120 | CONFORMATIONAL EPITOPE | POTENT | VIROLOGY | IMMUNODEFICIENCY-VIRUS TYPE-1 | BINDING-SITE | MONOCLONAL-ANTIBODIES | PARASITOLOGY | Protein Aggregates | Antibody Specificity | HIV Infections - prevention & control | Molecular Weight | Humans | Antibodies, Neutralizing - metabolism | env Gene Products, Human Immunodeficiency Virus - metabolism | AIDS Vaccines - therapeutic use | HIV Infections - immunology | env Gene Products, Human Immunodeficiency Virus - genetics | Immunoglobulin Fab Fragments - metabolism | env Gene Products, Human Immunodeficiency Virus - antagonists & inhibitors | Protein Stability | Mutant Proteins - antagonists & inhibitors | Peptide Fragments - genetics | env Gene Products, Human Immunodeficiency Virus - chemistry | HIV Antibodies - metabolism | Peptide Fragments - metabolism | Solubility | Antibody Affinity | Mutant Proteins - metabolism | Epitopes | Recombinant Fusion Proteins - chemistry | HIV-1 - immunology | Peptide Fragments - chemistry | Peptide Fragments - antagonists & inhibitors | Mutant Proteins - chemistry | Antibodies, Monoclonal - metabolism | Amino Acid Substitution | Physiological aspects | Genetic aspects | Research | Nucleotide sequencing | HIV (Viruses) | Gene expression | Health aspects | DNA sequencing | Index Medicus | Medical research | AIDS | Human immunodeficiency virus | Vaccines | HIV | Acquired immune deficiency syndrome
Journal Article
Nature Structural and Molecular Biology, ISSN 1545-9993, 07/2013, Volume 20, Issue 7, pp. 804 - 813
HIV-1 uses a diverse N-linked-glycan shield to evade recognition by antibody. Select human antibodies, such as the clonally related PG9 and PG16, recognize... 
COMPLEX | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GP120 | 2G12 RECOGNIZES | GLYCOSYLATION SITES | CELL BIOLOGY | POTENT | BIOPHYSICS | HAMSTER OVARY CELLS | BROADLY NEUTRALIZING ANTIBODIES | IMMUNODEFICIENCY-VIRUS TYPE-1 | HIV-1 ENVELOPE GLYCOPROTEINS | Antibody Specificity | Epitopes - metabolism | Humans | Antibodies, Neutralizing - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Structure-Activity Relationship | Glycosylation - drug effects | HIV Envelope Protein gp120 - metabolism | Antigen-Antibody Reactions | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | Immunoglobulin Fab Fragments - metabolism | Protein Processing, Post-Translational - drug effects | Peptide Fragments - immunology | HEK293 Cells | Polysaccharides - chemistry | HIV Envelope Protein gp120 - chemistry | Swainsonine - pharmacology | Carbohydrate Sequence | HIV Antibodies - metabolism | Amino Acid Sequence | Peptide Fragments - metabolism | Models, Molecular | Polysaccharides - immunology | HIV Antibodies - chemistry | Amino Acid Motifs | Polysaccharides - metabolism | Peptide Fragments - chemistry | Antibodies, Neutralizing - chemistry | Protein Conformation | Epitopes - chemistry | Immunoglobulin Fab Fragments - immunology | Binding Sites, Antibody | Carbohydrate Conformation | Antigen-antibody reactions | Physiological aspects | Genetic aspects | Research | HIV (Viruses) | Structure | Health aspects | Antigenic determinants | Mutagenesis | Molecular biology | Human immunodeficiency virus--HIV | Polyclonal antibodies | Index Medicus
Journal Article
Transfusion, ISSN 0041-1132, 06/2015, Volume 55, Issue 6pt2, pp. 1501 - 1511
Journal Article
NATURE, ISSN 0028-0836, 01/2011, Volume 469, Issue 7329, pp. 175 - 180
Journal Article
Nuclear Physics, Section A, ISSN 0375-9474, 05/2012, Volume 882, pp. 71 - 89
Journal Article
Biochemical Journal, ISSN 0264-6021, 12/2015, Volume 472, Issue 2, pp. 169 - 181
High temperature requirement A1 (HtrA1) is a trypsin-fold serine protease implicated in the progression of age-related macular degeneration (AMD). Our interest... 
Serine protease | Phage display | HtrA1 | Age-related macular degeneration | Antibody | SYSTEM | antibody | INCREASED EXPRESSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | SUSCEPTIBILITY | MACULAR DEGENERATION | GENETIC-VARIANTS | POLYMORPHISM | serine protease | phage display | PDZ DOMAINS | SMALL-VESSEL DISEASE | FUNCTIONAL-ANALYSIS | age-related macular degeneration | RETINAL-PIGMENT EPITHELIUM | Antibody Specificity | Allosteric Regulation | Humans | Antibodies, Neutralizing - metabolism | Neoplasm Proteins - antagonists & inhibitors | Mutant Proteins - pharmacology | Serine Endopeptidases - genetics | Neoplasm Proteins - genetics | Peptide Fragments - genetics | Protein Subunits - genetics | Immunoglobulin G - chemistry | High-Temperature Requirement A Serine Peptidase 1 | Protease Inhibitors - chemistry | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Protease Inhibitors - metabolism | Serine Endopeptidases - chemistry | Antibodies, Neutralizing - genetics | Peptide Fragments - chemistry | Immunoglobulin G - genetics | Antigen-Antibody Complex - chemistry | Immunoglobulin Fab Fragments - chemistry | Cell Line, Tumor | Mice | Protein Subunits - antagonists & inhibitors | Immunoglobulin G - metabolism | Epitope Mapping | Melanoma - enzymology | Peptide Fragments - pharmacology | Neoplasm Proteins - metabolism | Protein Subunits - metabolism | Antineoplastic Agents - metabolism | Protease Inhibitors - pharmacology | Immunoglobulin Fab Fragments - metabolism | Immunoglobulin G - pharmacology | Antineoplastic Agents - pharmacology | Melanoma - metabolism | Recombinant Proteins - metabolism | Catalytic Domain | Peptide Fragments - metabolism | Immunoglobulin Fab Fragments - genetics | Antibodies, Neutralizing - pharmacology | Mutant Proteins - metabolism | Recombinant Proteins - pharmacology | Antineoplastic Agents - chemistry | Immunoglobulin Fab Fragments - pharmacology | Animals | Antibodies, Neutralizing - chemistry | Melanoma - drug therapy | Mutant Proteins - chemistry | Protein Subunits - chemistry | Serine Endopeptidases - metabolism | Binding Sites, Antibody | Amino Acid Substitution | Index Medicus
Journal Article
mAbs, ISSN 1942-0862, 11/2011, Volume 3, Issue 6, pp. 546 - 557
Bispecific antibodies based on full-length antibody structures are more optimal than fragment-based formats because they benefit from the favorable properties... 
Proteins | Binding | Landes | Calcium | Biology | Bioscience | Cell | Cycle | Organogenesis | Cancer | Anti-tumor | CD3 | HM1.24 | Bispecific | CD16 | HER2 | Heterodimer | mAb-Fv | MEDICINE, RESEARCH & EXPERIMENTAL | ACTIVATION | VARIABLE-DOMAIN IMMUNOGLOBULIN | CRYSTAL-STRUCTURE | IGG | HUMAN B-CELLS | MONOCLONAL-ANTIBODY | ANTITUMOR-ACTIVITY | CANCER-THERAPY | anti-tumor | GROWTH-FACTOR RECEPTOR | bispecific | heterodimer | cancer | T-CELLS | Immunoglobulin Fragments - chemistry | Protein Engineering - methods | Immunoglobulin Fc Fragments - metabolism | Humans | Antibody-Dependent Cell Cytotoxicity - immunology | Antibodies, Bispecific - genetics | Receptors, IgG - metabolism | Receptors, IgG - genetics | CD3 Complex - genetics | Immunoglobulin Fc Fragments - immunology | HEK293 Cells | Killer Cells, Natural - immunology | Dimerization | Models, Molecular | Immunoglobulin Fc Fragments - chemistry | Receptors, IgG - immunology | Antibodies, Bispecific - immunology | CD3 Complex - metabolism | Immunoglobulin Fragments - metabolism | Animals | Antibodies, Bispecific - metabolism | Immunoglobulin Fragments - immunology | CD3 Complex - immunology | Antibodies, Bispecific - chemistry | Immunoglobulin Fragments - genetics | T-Lymphocytes - immunology | Mice | Immunoglobulin Fc Fragments - genetics | Index Medicus | Report
Journal Article