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by Liao, Hua-Xin and Lynch, Rebecca and Zhou, Tongqing and Gao, Feng and Munir Alam, S and Boyd, Scott D and Fire, Andrew Z and Roskin, Krishna M and Schramm, Chaim A and Zhang, Zhenhai and Zhu, Jiang and Shapiro, Lawrence and Mullikin, James C and Gnanakaran, S and Hraber, Peter and Wiehe, Kevin and Kelsoe, Garnett and Yang, Guang and Xia, Shi-Mao and Montefiori, David C and Parks, Robert and Lloyd, Krissey E and Scearce, Richard M and Soderberg, Kelly A and Cohen, Myron and Kamanga, Gift and Louder, Mark K and Tran, Lillian M and Chen, Yue and Cai, Fangping and Chen, Sheri and Moquin, Stephanie and Du, Xiulian and Gordon Joyce, M and Srivatsan, Sanjay and Zhang, Baoshan and Zheng, Anqi and Shaw, George M and Hahn, Beatrice H and Kepler, Thomas B and Korber, Bette T. M and Kwong, Peter D and Mascola, John R and Haynes, Barton F and Becker, Jesse and Benjamin, Betty and Blakesley, Robert and Bouffard, Gerry and Brooks, Shelise and Coleman, Holly and Dekhtyar, Mila and Gregory, Michael and Guan, Xiaobin and Gupta, Jyoti and Han, Joel and Hargrove, April and Ho, Shi-Ling and Johnson, Taccara and Legaspi, Richelle and Lovett, Sean and Maduro, Quino and Masiello, Cathy and Maskeri, Baishali and McDowell, Jenny and Montemayor, Casandra and Mulliki, James and Park, Morgan and Riebow, Nancy and Schandler, Karen and Schmidt, Brian and Sison, Christina and Stantripop, Mal and Thomas, James and Thomas, Pam and Vemulapalli, Meg and Young, Alice and NISC Comparative Sequencing Progra and NISC Comparative Sequencing Program
Nature, ISSN 0028-0836, 04/2013, Volume 496, Issue 7446, pp. 469 - 476
Current human immunodeficiency virus-1 (HIV-1) vaccines elicit strain-specific neutralizing antibodies. However, cross-reactive neutralizing antibodies arise... 
B-CELL RESPONSES | CONFORMATIONAL EPITOPE | POTENT NEUTRALIZATION | CD4 BINDING-SITE | VACCINE DESIGN | MULTIDISCIPLINARY SCIENCES | ENVELOPE GLYCOPROTEIN | HIV-1-INFECTED INDIVIDUALS | HUMAN MONOCLONAL-ANTIBODIES | SUBTYPE-B | IN-SITU PROTEOLYSIS | HIV Envelope Protein gp120 - genetics | Clone Cells - cytology | Humans | AIDS Vaccines - immunology | Molecular Sequence Data | Crystallography, X-Ray | Neutralization Tests | Phylogeny | HIV Envelope Protein gp120 - metabolism | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | HIV-1 - chemistry | HIV Envelope Protein gp120 - chemistry | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Protein Structure, Tertiary | Amino Acid Sequence | CD4 Antigens - immunology | Africa | Cells, Cultured | Models, Molecular | Antibodies, Neutralizing - genetics | Cross Reactions - immunology | HIV Antibodies - chemistry | HIV-1 - classification | Antibodies, Monoclonal - genetics | Cell Lineage | HIV-1 - immunology | CD4 Antigens - chemistry | Antibodies, Neutralizing - chemistry | Epitopes - chemistry | HIV Antibodies - genetics | Mutation | Evolution, Molecular | Monoclonal antibodies | AIDS vaccines | Genetic aspects | Research | HIV (Viruses) | Properties | Proteins | Plasma | Infections | Patients | Binding sites | Crystal structure | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 2008, Volume 3, Issue 12, pp. e3942 - e3942
BACKGROUND: The hemagglutinin (HA) glycoprotein is the principal target of protective humoral immune responses to influenza virus infections but such antibody... 
BIOLOGY | Influenza A Virus, H1N1 Subtype - immunology | Humans | Molecular Sequence Data | Neutralization Tests | Hemagglutinin Glycoproteins, Influenza Virus - immunology | Peptide Library | Immunoglobulin M - immunology | Antibody Specificity - immunology | B-Lymphocytes - virology | Influenza, Human - virology | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Immunologic Memory - immunology | Protein Structure, Tertiary | Amino Acid Sequence | Hemagglutinin Glycoproteins, Influenza Virus - chemistry | Antibodies, Monoclonal - isolation & purification | Antibodies, Viral - isolation & purification | Cross Reactions | Animals | B-Lymphocytes - immunology | Influenza A Virus, H5N1 Subtype - immunology | Antibodies, Viral - chemistry | Dogs | Hydrophobic and Hydrophilic Interactions | Antibodies, Viral - immunology | Mice | Tissue Donors | Binding Sites, Antibody | Influenza, Human - prevention & control | Influenza, Human - immunology | Immunoglobulin M | Pandemics | Laboratories | Prophylaxis | H alpha line | Viruses | Infections | Vaccines | Hydrophobicity | Avian flu | Proteins | Hemagglutinins | Antigens | Immunological memory | Memory cells | Immunoglobulins | Therapeutic applications | Mortality | Glycoprotein | Antigenic variants | Immune response (humoral) | Lymphocytes B | Neutralizing | Influenza | Monoclonal antibodies | Ligands | Combinatorial analysis | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 2014, Volume 515, Issue 7525, pp. 138 - 142
The isolation of human monoclonal antibodies is providing important insights into the specificities that underlie broad neutralization of HIV-1 (reviewed in... 
B-CELLS | SPECIFICITIES | MULTIDISCIPLINARY SCIENCES | SERA | IMMUNODEFICIENCY-VIRUS TYPE-1 | ENV TRIMERS | VULNERABILITY | GP120 | HUMAN MONOCLONAL-ANTIBODIES | CLEAVAGE | DEPENDENT EPITOPE | Immunoglobulin Fab Fragments - ultrastructure | Antibody Specificity | Epitope Mapping | HIV Envelope Protein gp41 - immunology | Humans | AIDS Vaccines - immunology | Molecular Sequence Data | Leukocytes, Mononuclear | HIV Envelope Protein gp41 - chemistry | Virus Internalization - drug effects | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Neutralizing - immunology | Receptors, CCR5 - metabolism | HIV Antibodies - immunology | Conserved Sequence | Inhibitory Concentration 50 | HIV Envelope Protein gp120 - chemistry | HIV Antibodies - pharmacology | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Cell Line | Immunoglobulin Fab Fragments - genetics | HIV-1 - drug effects | Antibodies, Monoclonal - pharmacology | Models, Molecular | Antibodies, Neutralizing - pharmacology | Antibody Affinity | Antibodies, Neutralizing - genetics | HIV Antibodies - chemistry | AIDS Vaccines - chemistry | Antibodies, Monoclonal - genetics | HIV-1 - immunology | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | Cell Membrane - virology | Epitopes - chemistry | HIV Antibodies - genetics | Immunoglobulin Fab Fragments - immunology | CD4 Antigens - metabolism | Viral antibodies | Care and treatment | Antibodies | Physiological aspects | Genetic aspects | Research | HIV infection | Antigenic determinants | Amino acids | Mutation | Vaccines | Human immunodeficiency virus--HIV | Binding sites | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 2013, Volume 501, Issue 7467, pp. 439 - 443
Broadly neutralizing antibodies reactive against most and even all variants of the same viral species have been described for influenza and HIV-1 (ref. 1).... 
IN-VITRO | MEMORY B-CELLS | TRACT DISEASE | MULTIDISCIPLINARY SCIENCES | HUMAN METAPNEUMOVIRUS | FUSION PROTEIN | ELECTRON-MICROSCOPY | INFECTION | RESPIRATORY SYNCYTIAL VIRUS | YOUNG-CHILDREN | F-GLYCOPROTEIN | Humans | Immunoglobulin Variable Region - chemistry | Paramyxoviridae - classification | Pneumovirus Infections - prevention & control | Molecular Sequence Data | Antibodies, Monoclonal - therapeutic use | Immunoglobulin Variable Region - immunology | Respiratory Syncytial Virus Infections - immunology | Viral Fusion Proteins - immunology | Murine pneumonia virus - immunology | Epitopes - immunology | Immunoglobulin Light Chains - chemistry | Antibodies, Neutralizing - immunology | Antibody Specificity - immunology | Paramyxoviridae Infections - virology | Viral Fusion Proteins - chemistry | Cattle | Antibodies, Neutralizing - therapeutic use | Respiratory Syncytial Virus Infections - prevention & control | Respiratory Syncytial Virus, Bovine - immunology | Respiratory Syncytial Virus Infections - virology | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Immunoglobulin Light Chains - immunology | Amino Acid Sequence | Metapneumovirus - immunology | Paramyxoviridae Infections - therapy | Models, Molecular | Antibodies, Monoclonal - isolation & purification | Cross Reactions - immunology | Pneumovirus Infections - virology | Antibodies, Neutralizing - isolation & purification | Paramyxoviridae Infections - immunology | Pneumovirus Infections - immunology | Paramyxoviridae - immunology | Animals | Respiratory Syncytial Virus, Human - immunology | Antibodies, Neutralizing - chemistry | Viral Vaccines - chemistry | Mice | Paramyxoviridae Infections - prevention & control | Respiratory Syncytial Virus Infections - therapy | Viral Vaccines - immunology | Monoclonal antibodies | Paramyxoviruses | Control | Health aspects | Proteins | Competition | Viruses | Glycoproteins | Infections | Mutation | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 08/2013, Volume 110, Issue 32, pp. E2987 - E2996
Binding of hepatocyte growth factor (HGF) to the receptor tyrosine kinase MET is implicated in the malignant process of multiple cancers, making disruption of... 
MetMAb | HGFR | OA5D5 | Scatter factor | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | HEPATOCYTE GROWTH-FACTOR | PHARMACOKINETIC PK | DOSE-ESCALATION | SINGLE-AGENT | scatter factor | C-MET | BINDING-SITE | RECEPTOR MET | MONOCLONAL-ANTIBODIES | Proto-Oncogene Proteins c-met - metabolism | Humans | Molecular Sequence Data | Crystallography, X-Ray | Hepatocyte Growth Factor - pharmacology | Antibodies, Monoclonal, Humanized - genetics | Antibodies, Monoclonal, Humanized - pharmacology | Protein Binding - drug effects | Drug Design | Antineoplastic Agents - pharmacology | Hepatocyte Growth Factor - chemistry | Antibodies, Monoclonal - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | Immunoglobulin Fab Fragments - genetics | Proto-Oncogene Proteins c-met - antagonists & inhibitors | Antibodies, Monoclonal - pharmacology | Models, Molecular | Mice, Transgenic | Antineoplastic Agents - chemistry | Mice, SCID | Immunoglobulin Fab Fragments - pharmacology | Mice, Inbred C3H | Hepatocyte Growth Factor - metabolism | Neoplasms - drug therapy | Sequence Homology, Amino Acid | Xenograft Model Antitumor Assays | Antibodies, Monoclonal - genetics | Animals | Mice, Nude | Immunoglobulin Fab Fragments - chemistry | Cell Line, Tumor | Cell Proliferation - drug effects | Mice | Mice, Inbred BALB C | Antibodies, Monoclonal - metabolism | Proto-Oncogene Proteins c-met - chemistry | Neoplasms - pathology | Antibodies, Monoclonal, Humanized - chemistry | Prescription drugs | Antigens | Phosphorylation | Monoclonal antibodies | Biochemistry | Binding sites | Tumors | Index Medicus | Biological Sciences | PNAS Plus
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2015, Volume 10, Issue 7, pp. e0131177 - e0131177
Antibody drug conjugates (ADCs) have recently been proven to be highly potent anti-tumor drugs, typically exceeding the efficacy of conventional monoclonal... 
RECOMBINANT IMMUNOTOXIN | IMMUNOGENICITY | MULTIDISCIPLINARY SCIENCES | PURIFICATION | SURFACE-PROTEINS | STAPHYLOCOCCUS-AUREUS | ANTITUMOR-ACTIVITY | MONOCLONAL-ANTIBODIES | FRAGMENTATION | CANCER-THERAPY | PROTEIN LIGATION | Cysteine Endopeptidases - chemistry | Staphylococcus aureus - enzymology | Aminoacyltransferases - immunology | Receptor, ErbB-2 - genetics | Humans | Bacterial Proteins - chemistry | Ovarian Neoplasms - pathology | Ki-1 Antigen - immunology | Maytansine - pharmacology | Immunoconjugates - immunology | Immunoconjugates - pharmacology | Antibodies, Monoclonal, Humanized - pharmacology | Protein Engineering | Maytansine - chemistry | Female | Antineoplastic Agents - pharmacology | Bacterial Proteins - immunology | Receptor, ErbB-2 - antagonists & inhibitors | Receptor, ErbB-2 - immunology | Oligopeptides - chemistry | Ovarian Neoplasms - drug therapy | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Aminoacyltransferases - chemistry | Antineoplastic Agents - immunology | Maytansine - analogs & derivatives | Antibodies, Monoclonal - pharmacology | Oligopeptides - immunology | Antineoplastic Agents - chemistry | Immunoconjugates - chemistry | Staphylococcus aureus - chemistry | Xenograft Model Antitumor Assays | Animals | Mice, Nude | Ki-1 Antigen - antagonists & inhibitors | Mice | Antibodies, Monoclonal, Humanized - immunology | Cysteine Endopeptidases - immunology | Maytansine - immunology | Trastuzumab | Antibodies, Monoclonal, Humanized - chemistry | Ki-1 Antigen - genetics | Ovarian Neoplasms - immunology | Monoclonal antibodies | Enzymes | Cysteine | Peptides | Biopharmaceutics | Drugs | Conjugates | Addition polymerization | Ovarian carcinoma | Clinical trials | Pentaglycine | Cancer therapies | Molecular weight | Ovarian cancer | Proteins | Tubulin | CD30 antigen | Xenografts | Medical research | Immunoglobulins | Polypeptides | Cloning | Polymerization | Breast cancer | ErbB-2 protein | Substrates | Chemotherapy | Lysine | Heavy chains | Toxins | Conjugation | Sortase | Tumors | Cancer | Index Medicus
Journal Article