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1
Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding
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Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding

Cell, 2020-09, Vol.182 (5), p.1295-1310.e20 [Peer Reviewed Journal]

2020 The Author(s) ;Copyright © 2020 The Author(s). Published by Elsevier Inc. All rights reserved. ;2020. Not withstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.elsevier.com/legal/elsevier-website-terms-and-conditions ;Distributed under a Creative Commons Attribution 4.0 International License ;2020 The Author(s) 2020 ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2020.08.012 ;PMID: 32841599

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2
Complete Mapping of Mutations to the SARS-CoV-2 Spike Receptor-Binding Domain that Escape Antibody Recognition
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Complete Mapping of Mutations to the SARS-CoV-2 Spike Receptor-Binding Domain that Escape Antibody Recognition

Cell Host & Microbe, 2021-01, Vol.29 (1), p.44-57.e9 [Peer Reviewed Journal]

2020 The Authors ;Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved. ;2020. Not withstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.elsevier.com/legal/elsevier-website-terms-and-conditions ;2020 The Authors 2020 ;ISSN: 1931-3128 ;EISSN: 1934-6069 ;DOI: 10.1016/j.chom.2020.11.007 ;PMID: 33259788

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3
Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
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Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

Cell, 2020-04, Vol.181 (2), p.281-292.e6 [Peer Reviewed Journal]

2020 Elsevier Inc. ;Copyright © 2020 Elsevier Inc. All rights reserved. ;2020. Not withstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.elsevier.com/legal/elsevier-website-terms-and-conditions ;Distributed under a Creative Commons Attribution 4.0 International License ;2020 Elsevier Inc. 2020 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2020.02.058 ;PMID: 32155444

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4
The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity
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The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity

Cell, 2020-09, Vol.182 (5), p.1284-1294.e9 [Peer Reviewed Journal]

2020 Elsevier Inc. ;Copyright © 2020 Elsevier Inc. All rights reserved. ;2020. Not withstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.elsevier.com/legal/elsevier-website-terms-and-conditions ;2020 Elsevier Inc. 2020 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2020.07.012 ;PMID: 32730807

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5
SARS-CoV-2 variants, spike mutations and immune escape
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SARS-CoV-2 variants, spike mutations and immune escape

Nature reviews. Microbiology, 2021-07, Vol.19 (7), p.409-424 [Peer Reviewed Journal]

COPYRIGHT 2021 Nature Publishing Group ;Springer Nature Limited 2021. ;Springer Nature Limited 2021 ;ISSN: 1740-1526 ;EISSN: 1740-1534 ;DOI: 10.1038/s41579-021-00573-0 ;PMID: 34075212

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6
Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
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Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies

Nature (London), 2022-02, Vol.602 (7898), p.657-663 [Peer Reviewed Journal]

2021. The Author(s). ;Copyright Nature Publishing Group Feb 24, 2022 ;The Author(s) 2021 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-021-04385-3 ;PMID: 35016194

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7
Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift
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Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift

Nature (London), 2022-02, Vol.602 (7898), p.664-670 [Peer Reviewed Journal]

2021. The Author(s), under exclusive licence to Springer Nature Limited. ;Copyright Nature Publishing Group Feb 24, 2022 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-021-04386-2 ;PMID: 35016195

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8
SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
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SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies

Nature (London), 2020-12, Vol.588 (7839), p.682-687 [Peer Reviewed Journal]

COPYRIGHT 2020 Nature Publishing Group ;Copyright Nature Publishing Group Dec 24-Dec 31, 2020 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-020-2852-1 ;PMID: 33045718

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9
Mapping Neutralizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution Serology
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Mapping Neutralizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution Serology

Cell, 2020-11, Vol.183 (4), p.1024-1042.e21 [Peer Reviewed Journal]

2020 Elsevier Inc. ;Copyright © 2020 Elsevier Inc. All rights reserved. ;2020. Not withstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.elsevier.com/legal/elsevier-website-terms-and-conditions ;Distributed under a Creative Commons Attribution 4.0 International License ;2020 Elsevier Inc. 2020 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2020.09.037 ;PMID: 32991844

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10
A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2
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A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2

Nature, 2020-08, Vol.584 (7819), p.120-124 [Peer Reviewed Journal]

2020. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.springernature.com/gp/researchers/campaigns/coronavirus ;Copyright Nature Publishing Group Aug 6, 2020 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-020-2381-y ;PMID: 32454512

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11
Structures and distributions of SARS-CoV-2 spike proteins on intact virions
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Article
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Structures and distributions of SARS-CoV-2 spike proteins on intact virions

Nature (London), 2020-12, Vol.588 (7838), p.498-502 [Peer Reviewed Journal]

COPYRIGHT 2020 Nature Publishing Group ;Copyright Nature Publishing Group Dec 17, 2020 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-020-2665-2 ;PMID: 32805734

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12
Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies
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Article
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Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies

Nature (London), 2021-05, Vol.593 (7857), p.136-141 [Peer Reviewed Journal]

Copyright Nature Publishing Group May 6, 2021 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-021-03412-7 ;PMID: 33706364

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13
Prospective mapping of viral mutations that escape antibodies used to treat COVID-19
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Article
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Prospective mapping of viral mutations that escape antibodies used to treat COVID-19

Science, 2021-02, Vol.371 (6531) [Peer Reviewed Journal]

2021. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;DOI: 10.1126/science.abf9302

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14
A thermostable, closed SARS-CoV-2 spike protein trimer
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A thermostable, closed SARS-CoV-2 spike protein trimer

Nature structural & molecular biology, 2020-10, Vol.27 (10), p.934-941 [Peer Reviewed Journal]

COPYRIGHT 2020 Nature Publishing Group ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-020-0478-5 ;PMID: 32737467

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15
Controlling the SARS-CoV-2 spike glycoprotein conformation
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Controlling the SARS-CoV-2 spike glycoprotein conformation

Nature structural & molecular biology, 2020-10, Vol.27 (10), p.925-933 [Peer Reviewed Journal]

ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-020-0479-4 ;PMID: 32699321

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16
Structural impact on SARS-CoV-2 spike protein by D614G substitution
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Structural impact on SARS-CoV-2 spike protein by D614G substitution

Science, 2021-04, Vol.372 (6541) [Peer Reviewed Journal]

2021. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;DOI: 10.1126/science.abf2303

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17
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
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Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants

Science, 2021-08, Vol.373 (6555) [Peer Reviewed Journal]

2021. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;DOI: 10.1126/science.abi9745

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18
Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants
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Article
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Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants

Science, 2021-08, Vol.373 (6556) [Peer Reviewed Journal]

2021. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;DOI: 10.1126/science.abh1139

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19
Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity
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Article
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Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity

Science, 2021-08, Vol.373 (6555) [Peer Reviewed Journal]

2021. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;DOI: 10.1126/science.abi6226

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20
Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion
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Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion

Cell, 2019-02, Vol.176 (5), p.1026-1039.e15 [Peer Reviewed Journal]

2018 Elsevier Inc. ;Copyright © 2018 Elsevier Inc. All rights reserved. ;2019. Not withstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.elsevier.com/legal/elsevier-website-terms-and-conditions ;Distributed under a Creative Commons Attribution 4.0 International License ;2018 Elsevier Inc. 2018 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2018.12.028 ;PMID: 30712865

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