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1. Full Text Structural Delineation of a Quaternary, Cleavage-Dependent Epitope at the gp41-gp120 Interface on Intact HIV-1 Env Trimers
by Blattner, Claudia and Lee, Peter S and Lee, Jeong Hyun and Sliepen, Kwinten and Derking, Ronald and Falkowska, Emilia and de la Peña, Alba Torrents and Cupo, Albert and Julien, Jean-Philippe and van Gils, Marit and Peng, Wenjie and Paulson, James C and Poignard, Pascal and Burton, Dennis R and Moore, John P and Sanders, Rogier W and Wilson, Ian A and Ward, Andrew B
Immunity, ISSN 1074-7613, 05/2014, Volume 40, Issue 5, pp. 669 - 680
All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we... 
REFINEMENT | SITE | POTENT NEUTRALIZATION | RECOGNITION | BROADLY NEUTRALIZING ANTIBODIES | GP41 | IMMUNOLOGY | IDENTIFICATION | COMBINATION | BINDING | Cell Line | HIV Infections - prevention & control | Binding Sites, Antibody - immunology | env Gene Products, Human Immunodeficiency Virus - immunology | HIV Envelope Protein gp41 - immunology | Humans | Crystallization | HIV Envelope Protein gp41 - metabolism | Molecular Sequence Data | Antibodies, Neutralizing - ultrastructure | Crystallography, X-Ray | Polysaccharides - immunology | Epitopes - immunology | HIV Antibodies - ultrastructure | HIV Envelope Protein gp120 - immunology | Antibodies, Monoclonal - ultrastructure | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV-1 - immunology | HIV Antibodies - immunology | HEK293 Cells | Protein Structure, Quaternary | Antibodies, Monoclonal - immunology | Monoclonal antibodies | Polysaccharides | HIV (Viruses) | Antigenic determinants | Proteins | Medical research | Scholarships & fellowships | Acquired immune deficiency syndrome--AIDS | Councils | Microscopy | Colleges & universities | Chemical bonds | Vaccines | Grants | Viral infections
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2. Full Text Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins
by Diamond, Michael S and Kuhn, Richard J and Rossmann, Michael G and Kostyuchenko, Victor and Battisti, Anthony J and Nybakken, Grant E and Holdaway, Heather A and Roehrig, John T and Fremont, Daved H and Lok, Shee-Mei and Chipman, Paul R and Sukupolvi-Petty, Soila and Sedlak, Dagmar and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature Structural & Molecular Biology, ISSN 1545-9993, 03/2008, Volume 15, Issue 3, pp. 312 - 317
The monoclonal antibody 1A1D-2 has been shown to strongly neutralize dengue virus serotypes 1, 2 and 3, primarily by inhibiting attachment to host cells. A... 
TYPE-2 ENVELOPE PROTEIN | DOMAIN-III | BIOCHEMISTRY & MOLECULAR BIOLOGY | WEST-NILE-VIRUS | ELECTRON-MICROSCOPY | MONOCLONAL-ANTIBODY | CELL BIOLOGY | MEMBRANE-FUSION | BORNE ENCEPHALITIS-VIRUS | EPITOPE | BIOPHYSICS | INFECTION | DEPENDENT ENHANCEMENT | Temperature | Membrane Glycoproteins - chemistry | Dengue Virus - ultrastructure | Crystallography, X-Ray | Neutralization Tests | Dengue Virus - chemistry | Cryoelectron Microscopy | Antibodies, Monoclonal - ultrastructure | Membrane Glycoproteins - ultrastructure | Antibodies, Viral - ultrastructure | Dengue Virus - immunology | Antibodies, Viral - chemistry | Antibodies, Viral - immunology | Membrane Glycoproteins - immunology | Binding Sites | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Physiological aspects | Monoclonal antibodies | Glycoproteins | Research | Dengue viruses | Viruses | Cellular biology | Molecular biology | Binding sites | GLYCOPROTEINS | CRYSTAL STRUCTURE | HOST | ANTIGENS | MATERIALS SCIENCE | MICROSCOPES | MOLECULES | MOTION | IMAGES | DYNAMICS | PROTEINS | UNITS | SURFACES
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3. Full Text Structural Characterization of IgG1 mAb Aggregates and Particles Generated Under Various Stress Conditions
by Telikepalli, Srivalli N and Kumru, Ozan S and Kalonia, Cavan and Esfandiary, Reza and Joshi, Sangeeta B and Middaugh, C. Russell and Volkin, David B
Journal of Pharmaceutical Sciences, ISSN 0022-3549, 03/2014, Volume 103, Issue 3, pp. 796 - 809
IgG1 mAb solutions were prepared with and without sodium chloride and subjected to different environmental stresses. Formation of aggregates and particles of... 
accelerated stability | protein aggregation | particle sizing | protein | formulation | IgG | particles | monoclonal antibody | stability | CHEMISTRY, MEDICINAL | PERSPECTIVE | MECHANISM | MONOCLONAL-ANTIBODY | INFRARED-SPECTROSCOPY | BIOPHARMACEUTICALS | CHEMISTRY, MULTIDISCIPLINARY | IMMUNOGENICITY | THERAPEUTIC PROTEINS | FORMULATIONS | PHARMACOLOGY & PHARMACY | PHYSICAL STABILITY | Nanoparticles - chemistry | Humans | Immunoglobulin G - ultrastructure | Spectroscopy, Fourier Transform Infrared | Antibodies, Monoclonal - ultrastructure | Excipients - chemistry | Nanoparticles - metabolism | Surface Properties | Chemical Phenomena | Protein Denaturation | Protein Stability | Antibodies, Monoclonal - chemistry | Sodium Chloride - chemistry | Microscopy, Electron, Transmission | Cross-Linking Reagents - chemistry | Hot Temperature - adverse effects | Protein Structure, Secondary | Immunoglobulin G - chemistry | Nanoparticles - ultrastructure | Solubility | Spectrometry, Fluorescence | Cold Temperature - adverse effects | Particle Size | Hydrophobic and Hydrophilic Interactions | Antibodies, Monoclonal - metabolism | Immunoglobulin G - metabolism | Dichloropropane | Chlorides | Immunoglobulin G | Fluorescence | Monoclonal antibodies | Chemical properties | Pharmacists | Electron microscopy | Chromatography | aggregation
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4. Full Text AAV6 K531 serves a dual function in selective receptor and antibody ADK6 recognition
by Bennett, Antonette D and Wong, Kristine and Lewis, Jordyn and Tseng, Yu-Shan and Smith, J. Kennon and Chipman, Paul and McKenna, Robert and Samulski, R. Jude and Kleinschmidt, Jürgen and Agbandje-McKenna, Mavis
Virology, ISSN 0042-6822, 05/2018, Volume 518, pp. 369 - 376
Adeno-associated viruses (AAVs) are being developed as vectors for the treatment of genetic disorders. However, pre-existing antibodies present a significant... 
Adeno-associated virus | Epitope | Antibody | Receptor | AAV | Parvoviruses | Viral vectors | Antigenic footprint | Neutralization | COMPLEX | TRANSDUCTION | HEMOPHILIA | IN-VITRO | VIROLOGY | PURIFICATION | GENE-THERAPY | ADENOASSOCIATED VIRUS SEROTYPE-1 | MONOCLONAL-ANTIBODIES | MONKEYS | VECTORS | Cryoelectron Microscopy | Antibodies, Monoclonal - ultrastructure | Antibodies, Neutralizing - immunology | Antibodies, Viral - ultrastructure | Parvovirinae - ultrastructure | Capsid Proteins - immunology | Protein Binding | Antibodies, Neutralizing - ultrastructure | Antibodies, Viral - immunology | Parvovirinae - immunology | Antibodies, Monoclonal - immunology | Capsid Proteins - ultrastructure
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5. Full Text The Marburgvirus-Neutralizing Human Monoclonal Antibody MR191 Targets a Conserved Site to Block Virus Receptor Binding
by King, Liam B and Fusco, Marnie L and Flyak, Andrew I and Ilinykh, Philipp A and Huang, Kai and Gunn, Bronwyn and Kirchdoerfer, Robert N and Hastie, Kathryn M and Sangha, Amandeep K and Meiler, Jens and Alter, Galit and Bukreyev, Alexander and Crowe, James E and Saphire, Erica Ollmann and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Cell Host & Microbe, ISSN 1931-3128, 01/2018, Volume 23, Issue 1, pp. 101 - 109.e4
Since their first identification 50 years ago, marburgviruses have emerged several times, with 83%–90% lethality in the largest outbreaks. Although no vaccines... 
marburgvirus | antibody | Ravn virus | immunotherapeutic | Marburg virus | hemorrhagic fever | structural biology | structure | NONHUMAN-PRIMATES | DOMAIN | PROTEIN | MICROBIOLOGY | PHENIX | EBOLA | ENTRY REQUIRES | CATHEPSINS | VIROLOGY | STRUCTURAL BASIS | GLYCOPROTEIN | PARASITOLOGY | INSIGHTS | Humans | Agrobacterium tumefaciens | Cercopithecus aethiops | Crystallography, X-Ray | Viral Fusion Proteins - immunology | Antibodies, Monoclonal - ultrastructure | Antibodies, Neutralizing - immunology | Binding Sites - immunology | Marburgvirus - immunology | Viral Fusion Proteins - ultrastructure | Membrane Glycoproteins - immunology | Vero Cells | Antibodies, Monoclonal - immunology | Carrier Proteins - immunology | Cell Line | Viral Envelope Proteins - genetics | Receptors, Virus - ultrastructure | Tobacco | Animals | Virus Attachment | Receptors, Virus - immunology | Antibodies, Viral - immunology | Viral Envelope Proteins - immunology | Marburgvirus - metabolism | Drosophila melanogaster | Protection and preservation | Monoclonal antibodies | Structure | Immunotherapy | Marburg virus disease | Crystals
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6. Full Text A Strain-Specific Epitope of Enterovirus 71 Identified by Cryo-Electron Microscopy of the Complex with Fab from Neutralizing Antibody
by Hyunwook Lee and Javier O. Cifuente and Robert E. Ashley and James F. Conway and Alexander M. Makhov and Yoshio Tano and Hiroyuki Shimizu and Yorihiro Nishimura and Susan Hafenstein
Journal of Virology, ISSN 0022-538X, 11/2013, Volume 87, Issue 21, pp. 11363 - 11370
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
PARVOVIRUS CAPSIDS | VIRUS | VIROLOGY | POLIOVIRUS | MECHANISM | DETERMINANTS | NATURAL-SELECTION | RECEPTOR | INFECTION | BINDING | REGION | Immunoglobulin Fab Fragments - ultrastructure | Humans | Enterovirus A, Human - immunology | Child, Preschool | Antibodies, Neutralizing - ultrastructure | Immunoglobulin Fab Fragments - isolation & purification | Antibodies, Monoclonal - isolation & purification | Antibodies, Neutralizing - isolation & purification | Cryoelectron Microscopy | Epitopes - immunology | Antibodies, Monoclonal - ultrastructure | Antibodies, Neutralizing - immunology | Animals | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | Virion - ultrastructure | Enterovirus A, Human - chemistry | Enterovirus A, Human - ultrastructure | Epitopes - chemistry | Mice | Mice, Inbred BALB C | Immunoglobulin Fab Fragments - immunology | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Structure and Assembly
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7. Full Text Structural basis for the neutralization of MERS-CoV by a human monoclonal antibody MERS-27
by Yu, Xiaojuan and Zhang, Senyan and Jiang, Liwei and Cui, Ye and Li, Dongxia and Wang, Dongli and Wang, Nianshuang and Fu, Lili and Shi, Xuanlin and Li, Ziqiang and Zhang, Linqi and Wang, Xinquan
Scientific Reports, ISSN 2045-2322, 08/2015, Volume 5, Issue 1, p. 13133
The recently reported Middle East respiratory syndrome coronavirus (MERS-CoV) causes severe respiratory illness in humans with an approximately 30% mortality... 
DROMEDARY CAMELS | HKU4 | MULTIDISCIPLINARY SCIENCES | SPIKE PROTEIN | TRANSMISSIBILITY | PIPISTRELLUS BAT CORONAVIRUS | RESPIRATORY SYNDROME CORONAVIRUS | SAUDI-ARABIA | RECEPTOR-BINDING DOMAIN | MIDDLE-EAST | BETACORONAVIRUS | Middle East Respiratory Syndrome Coronavirus - ultrastructure | Models, Chemical | Humans | Structure-Activity Relationship | Viral Envelope Proteins - ultrastructure | Middle East Respiratory Syndrome Coronavirus - chemistry | Antibodies, Monoclonal - ultrastructure | Antiviral Agents - chemistry | Viral Envelope Proteins - chemistry | Protein Binding | Molecular Docking Simulation | Binding Sites | Antibodies, Monoclonal - chemistry | Proteins | Membrane fusion | Respiratory diseases | Fab | Firing rate | Monoclonal antibodies | Infections | Spike glycoprotein | Binding sites | Crystal structure
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8. Full Text Antibody Treatment of Ebola and Sudan Virus Infection via a Uniquely Exposed Epitope within the Glycoprotein Receptor-Binding Site
by Howell, Katie A and Qiu, Xiangguo and Brannan, Jennifer M and Bryan, Christopher and Davidson, Edgar and Holtsberg, Frederick W and Wec, Anna Z and Shulenin, Sergey and Biggins, Julia E and Douglas, Robin and Enterlein, Sven G and Turner, Hannah L and Pallesen, Jesper and Murin, Charles D and He, Shihua and Kroeker, Andrea and Vu, Hong and Herbert, Andrew S and Fusco, Marnie L and Nyakatura, Elisabeth K and Lai, Jonathan R and Keck, Zhen-Yong and Foung, Steven K.H and Saphire, Erica Ollmann and Zeitlin, Larry and Ward, Andrew B and Chandran, Kartik and Doranz, Benjamin J and Kobinger, Gary P and Dye, John M and Aman, M. Javad
Cell Reports, ISSN 2211-1247, 05/2016, Volume 15, Issue 7, pp. 1514 - 1526
Previous efforts to identify cross-neutralizing antibodies to the receptor-binding site (RBS) of ebolavirus glycoproteins have been unsuccessful, largely... 
NONHUMAN-PRIMATES | MOLECULAR CHARACTERIZATION | NIEMANN-PICK C1 | PROPHYLAXIS | FILOVIRUS ENTRY | MARBURG VIRUS | NEUTRALIZING ANTIBODY | DISEASE | GUINEA-PIG | MONOCLONAL-ANTIBODIES | CELL BIOLOGY | Receptors, Virus - metabolism | Humans | Glycoproteins - metabolism | Antibodies, Monoclonal - therapeutic use | Neutralization Tests | Epitopes - immunology | Antibodies, Monoclonal - ultrastructure | HEK293 Cells | Female | Hemorrhagic Fever, Ebola - immunology | Glycoproteins - chemistry | Binding Sites | Antibodies, Monoclonal - chemistry | Disease Models, Animal | Antibodies, Neutralizing | Glycoproteins - genetics | Amino Acid Sequence | Guinea Pigs | Models, Molecular | Treatment Outcome | Negative Staining | Mutation - genetics | Animals | Antibodies, Viral - chemistry | Mice, Inbred BALB C | Kinetics | Ebolavirus - physiology | Glycoproteins - ultrastructure
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9. Full Text West Nile Virus in Complex with the Fab Fragment of a Neutralizing Monoclonal Antibody
by Bärbel Kaufmann and Grant E. Nybakken and Paul R. Chipman and Wei Zhang and Michael S. Diamond and Daved H. Fremont and Richard J. Kuhn and Michael G. Rossmann
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2006, Volume 103, Issue 33, pp. 12400 - 12404
Flaviviruses, such as West Nile virus (WNV), are significant human pathogens. The humoral immune response plays an important role in the control of flavivirus... 
Molecules | Antibodies | Viruses | Infections | Glycoproteins | Viral morphology | Elbow | Binding sites | Monomers | Crystal structure | Flavivirus | Cryo-electron microscopy | Neutralization | UNITED-STATES | DOMAIN-III | PROTEIN | neutralization | MULTIDISCIPLINARY SCIENCES | FLAVIVIRUS ENVELOPE GLYCOPROTEIN | MEMBRANE-FUSION | TICK-BORNE ENCEPHALITIS | DENGUE-VIRUS | STRUCTURAL BASIS | DC-SIGN | BINDING | cryo-electron microscopy | flavivirus | Immunoglobulin Fab Fragments - ultrastructure | Cell Line | Cricetinae | Viral Fusion Proteins - metabolism | West Nile virus - ultrastructure | Humans | Models, Molecular | Crystallography, X-Ray | Cryoelectron Microscopy | West Nile virus - metabolism | Antibodies, Monoclonal - ultrastructure | Animals | Immunoglobulin Fab Fragments - metabolism | Viral Fusion Proteins - chemistry | Immunoglobulin Fab Fragments - chemistry | West Nile virus - chemistry | Protein Conformation | Viral Fusion Proteins - ultrastructure | Binding Sites | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Hydrogen-Ion Concentration | West Nile virus | Genetic aspects | Research | Biological Sciences
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10. Full Text Functional and structural characterization of human V3-specific monoclonal antibody 2424 with neutralizing activity against HIV-1 JRFL
by Kumar, Rajnish and Pan, Ruimin and Upadhyay, Chitra and Mayr, Luzia and Cohen, Sandra and Wang, Xiao-Hong and Balasubramanian, Preetha and Nádas, Arthur and Seaman, Michael S and Zolla-Pazner, Susan and Gorny, Miroslaw K and Kong, Xiang-Peng and Hioe, Catarina E
Journal of Virology, ISSN 0022-538X, 2015, Volume 89, Issue 17, pp. 9090 - 9102
The V3 region of HIV-1 gp120 is important for virus-coreceptor interaction and highly immunogenic. Although most anti-V3 antibodies neutralize only the... 
V3 DOMAIN | POTENT | VIROLOGY | BROAD NEUTRALIZATION | CD4 BINDING-SITE | VIRUS ENVELOPE GLYCOPROTEIN | 2G12 RECOGNIZES | GLYCAN | GP120 GLYCOPROTEIN | GLYCOSYLATION SITES | EPITOPES | Immunoglobulin Fab Fragments - ultrastructure | Protein Structure, Tertiary | Cell Line | Humans | AIDS Vaccines - immunology | Molecular Sequence Data | Crystallography, X-Ray | Mannosidases - antagonists & inhibitors | Polysaccharides - immunology | Epitopes - immunology | HIV Envelope Protein gp120 - immunology | Antibodies, Monoclonal - ultrastructure | Antibodies, Neutralizing - immunology | HIV-1 - immunology | Antibody Specificity - immunology | HIV Antibodies - immunology | HIV Antigens - immunology | HEK293 Cells | Immunoglobulin Fab Fragments - immunology | Antibodies, Monoclonal - immunology
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