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1. Full Text Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion
by Walls, Alexandra C and Xiong, Xiaoli and Park, Young-Jun and Tortorici, M. Alejandra and Snijder, Joost and Quispe, Joel and Cameroni, Elisabetta and Gopal, Robin and Dai, Mian and Lanzavecchia, Antonio and Zambon, Maria and Rey, Félix A and Corti, Davide and Veesler, David
Cell (Cambridge), ISSN 0092-8674, 02/2019, Volume 176, Issue 5, pp. 1026 - 1039.e15
glycoproteomics | spike glycoprotein | SARS-CoV | coronavirus | neutralizing antibodies | MERS-CoV | N-linked glycosylation | class I fusion protein | membrane fusion | Biochemistry, Genetics and Molecular Biology(all) | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | SARS Virus - immunology | Chlorocebus aethiops | Spike Glycoprotein, Coronavirus - metabolism | Immunity, Humoral - immunology | Receptors, Virus - metabolism | Humans | Molecular Mimicry - immunology | Coronavirus Infections - immunology | Middle East Respiratory Syndrome Coronavirus - immunology | SARS Virus - metabolism | Virus Internalization | Coronavirus - immunology | Middle East Respiratory Syndrome Coronavirus - metabolism | Spike Glycoprotein, Coronavirus - physiology | Antibodies, Neutralizing - immunology | Animals | Coronavirus - metabolism | HEK293 Cells | Protein Binding | Antibodies, Viral - immunology | Vero Cells | Antibodies, Monoclonal - immunology | Spike Glycoprotein, Coronavirus - ultrastructure | Viral antibodies | Respiratory tract infections | Analysis | Physiological aspects | Antibodies | Glycoproteins | Mass spectrometry | Health aspects | Index Medicus | Antibodies, Neutralizing | Coronavirus Infections | Antibodies, Monoclonal | Antibodies, Viral | Middle East Respiratory Syndrome Coronavirus | Spike Glycoprotein, Coronavirus | Life Sciences | SARS Virus | Molecular Mimicry | Coronavirus | Immunity, Humoral | Receptors, Virus
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2. Full Text Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer
by Walls, Alexana C and Tortorici, M Alejana and Bosch, Berend-Jan and Frenz, Brandon and Rottier, Peter J M and DiMaio, Frank and Rey, Félix A and Veesler, David
Nature (London), ISSN 0028-0836, 03/2016, Volume 531, Issue 7592, pp. 114 - 117
electron microscopy | antibodies | viral vaccines | Coronacrisis-Taverne | Coronavirus spike glycoprotein | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Protein Multimerization | Models, Molecular | Molecular Sequence Data | Coronavirus Infections - immunology | Virus Internalization | Cryoelectron Microscopy | Murine hepatitis virus - immunology | Antibodies, Neutralizing - immunology | Murine hepatitis virus - chemistry | Animals | Coronavirus Infections - virology | Viral Vaccines - chemistry | Spike Glycoprotein, Coronavirus - immunology | Mice | Drosophila melanogaster | Spike Glycoprotein, Coronavirus - chemistry | Viral Vaccines - immunology | Murine hepatitis virus - ultrastructure | Spike Glycoprotein, Coronavirus - ultrastructure | Usage | Cryoelectron microscopy | Protein S | Coronaviruses | Structure | Identification and classification | Natural history | Physiological aspects | Glycoproteins | Electron microscopy | Methods | Immunoglobulins | Peptides | Microscopy | Respiratory diseases | Viruses | Biochemistry | Index Medicus | Cristallography | Chemical Sciences
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3. Full Text Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy
by Walls, Alexana C and Tortorici, M Alejana and Frenz, Brandon and Snijder, Joost and Li, Wentao and Rey, Félix A and DiMaio, Frank and Bosch, Berend-Jan and Veesler, David
Nature structural & molecular biology, ISSN 1545-9993, 10/2016, Volume 23, Issue 10, pp. 899 - 905
Glycoproteins | Immunology | Coronacrisis-Taverne | Cryoelectron microscopy | Viral membrane fusion | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Cell Line | Coronavirus NL63, Human - immunology | Coronavirus NL63, Human - chemistry | Drosophila | Humans | Protein Multimerization | Models, Molecular | Polysaccharides - immunology | Coronavirus Infections - immunology | Polysaccharides - analysis | Cryoelectron Microscopy | Epitopes - immunology | Antibodies, Neutralizing - immunology | Animals | Coronavirus Infections - virology | Protein Conformation | Spike Glycoprotein, Coronavirus - immunology | Epitopes - chemistry | Spike Glycoprotein, Coronavirus - chemistry | Spike Glycoprotein, Coronavirus - ultrastructure | Polysaccharides | Usage | Analysis | Research | Coronaviruses | Electron microscopy | Antigenic determinants | Viruses | Respiratory system | Immune system | Virology | Index Medicus | Antibodies, Neutralizing | Coronavirus Infections | Biochemistry, Molecular Biology | Epitopes | Cristallography | Chemical Sciences | Spike Glycoprotein, Coronavirus | Life Sciences | Biomolecules | Coronavirus NL63, Human
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4. Full Text Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors
by Park, Young-Jun and Walls, Alexana C and Wang, Zhaoqian and Sauer, Maximillian M and Li, Wentao and Tortorici, M Alejana and Bosch, Berend-Jan and DiMaio, Frank and Veesler, David
Nature structural & molecular biology, ISSN 1545-9993, 12/2019, Volume 26, Issue 12, pp. 1151 - 1157
Sialic Acids/chemistry | Hemagglutination, Viral | Humans | Models, Molecular | Dipeptidyl Peptidase 4/chemistry | Spike Glycoprotein, Coronavirus/chemistry | Structure-Activity Relationship | Coronacrisis-Taverne | Middle East Respiratory Syndrome Coronavirus/chemistry | Protein Interaction Mapping | Cryoelectron Microscopy | Protein Binding | Protein Domains | Protein Conformation | Carbohydrate Conformation | Binding Sites | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Dipeptidyl Peptidase 4 - metabolism | Spike Glycoprotein, Coronavirus - metabolism | Dipeptidyl Peptidase 4 - chemistry | Sialic Acids - metabolism | Middle East Respiratory Syndrome Coronavirus - chemistry | Sialic Acids - chemistry | Dipeptidyl Peptidase 4 - ultrastructure | Spike Glycoprotein, Coronavirus - chemistry | Spike Glycoprotein, Coronavirus - ultrastructure | Amino acids | Coronaviruses | Vaccines | Health aspects | Proteins | Glycoproteins | Genetic aspects | Virulence (Microbiology) | Research | Structure | Virus research | Receptors | Peptidase | Epithelial cells | Respiratory diseases | Attachment | Grooves | Selectivity | Oligosaccharides | Spike glycoprotein | Index Medicus | Dipeptidyl Peptidase 4 | Sialic Acids | Middle East Respiratory Syndrome Coronavirus | Spike Glycoprotein, Coronavirus | Life Sciences | Cryoelectron microscopy | Viral membrane fusion
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5. Full Text Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
by Walls, Alexandra C and Park, Young-Jun and Tortorici, M. Alejandra and Wall, Abigail and McGuire, Andrew T and Veesler, David
Cell (Cambridge), ISSN 0092-8674, 04/2020, Volume 181, Issue 2, pp. 281 - 292.e6
SARS-CoV-2 | spike glycoprotein | viral receptor | SARS-CoV | coronavirus | neutralizing antibodies | antibodies | cryo-EM | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Amino Acid Sequence | Cell Line | Antigens, Viral - metabolism | Spike Glycoprotein, Coronavirus - metabolism | Receptors, Virus - metabolism | Humans | Antibodies, Neutralizing - metabolism | Models, Molecular | Antibodies, Neutralizing - pharmacology | Antigens, Viral - chemistry | Betacoronavirus - metabolism | Virus Internalization - drug effects | SARS Virus - metabolism | Cryoelectron Microscopy | Angiotensin-Converting Enzyme 2 | Antigens, Viral - immunology | Receptors, Virus - chemistry | Betacoronavirus - chemistry | Peptidyl-Dipeptidase A - metabolism | Spike Glycoprotein, Coronavirus - immunology | Spike Glycoprotein, Coronavirus - chemistry | Spike Glycoprotein, Coronavirus - ultrastructure | Viral antibodies | Medical research | Vaccination | World health | Antibodies | Medicine, Experimental | Glycoproteins | Coronaviruses | Health aspects | Antigenic determinants | Index Medicus | Life Sciences
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6. Full Text Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein
by Zhou, Haixia and Chen, Yingzhu and Zhang, Shuyuan and Niu, Peihua and Qin, Kun and Jia, Wenxu and Huang, Baoying and Zhang, Senyan and Lan, Jun and Zhang, Linqi and Tan, Wenjie and Wang, Xinquan
Nature communications, ISSN 2041-1723, 07/2019, Volume 10, Issue 1, pp. 3068 - 13
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Epitope Mapping | Dipeptidyl Peptidase 4 - metabolism | Antibodies, Viral - metabolism | Humans | Antibodies, Neutralizing - metabolism | Antibodies, Neutralizing - ultrastructure | Crystallography, X-Ray | Neutralization Tests | Antibodies, Viral - blood | Middle East Respiratory Syndrome Coronavirus - immunology | Virus Internalization | Epitopes - immunology | Recombinant Proteins - isolation & purification | Antibodies, Neutralizing - immunology | Coronavirus Infections - blood | HEK293 Cells | Female | Spike Glycoprotein, Coronavirus - immunology | Protein Domains - immunology | Spike Glycoprotein, Coronavirus - isolation & purification | Vero Cells | Disease Models, Animal | Recombinant Proteins - metabolism | Chlorocebus aethiops | Recombinant Proteins - ultrastructure | Spike Glycoprotein, Coronavirus - metabolism | Protein Binding - immunology | Coronavirus Infections - immunology | Middle East Respiratory Syndrome Coronavirus - metabolism | Animals | Antibodies, Viral - ultrastructure | Coronavirus Infections - virology | Recombinant Proteins - immunology | Cell Line, Tumor | Antibodies, Viral - immunology | Mice | Antibodies, Neutralizing - blood | Spike Glycoprotein, Coronavirus - ultrastructure | Binding | Peptidase | Glycoproteins | Epitopes | Coronaviruses | Synergistic effects | Mutagenesis | Respiratory diseases | Cell adhesion | Monoclonal antibodies | Inhibition | Spike glycoprotein | Neutralization | Index Medicus
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7. Full Text Pre-fusion structure of a human coronavirus spike protein
by Kirchdoerfer, Robert N and Cottrell, Christopher A and Wang, Nianshuang and Pallesen, Jesper and Yassine, Hadi M and Turner, Hannah L and Corbett, Kizzmekia S and Graham, Barney S and McLellan, Jason S and Ward, Andrew B
Nature (London), ISSN 0028-0836, 03/2016, Volume 531, Issue 7592, pp. 118 - 121
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Protein Structure, Tertiary | Cell Line | Coronavirus - ultrastructure | Spike Glycoprotein, Coronavirus - metabolism | Membrane Fusion | Receptors, Virus - metabolism | Humans | Protein Multimerization | Models, Molecular | Protein Subunits - metabolism | Virus Internalization | Cryoelectron Microscopy | Coronavirus - chemistry | Proteolysis | Protein Structure, Quaternary | Viral Vaccines - chemistry | Protein Binding | Protein Subunits - chemistry | Spike Glycoprotein, Coronavirus - chemistry | Viral Vaccines - immunology | Spike Glycoprotein, Coronavirus - ultrastructure | Causes of | Protein S | Coronaviruses | Diagnosis | Structure | Respiration disorders | Physiological aspects | Viral proteins | Proteins | Viruses | Microscopy | Molecular structure | Binding sites | Index Medicus
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