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1
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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2
Probable Pangolin Origin of SARS-CoV-2 Associated with the COVID-19 Outbreak
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Probable Pangolin Origin of SARS-CoV-2 Associated with the COVID-19 Outbreak

Current Biology, 2020-04, Vol.30 (7), p.1346-1351.e2 [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: 0960-9822 ;EISSN: 1879-0445 ;DOI: 10.1016/j.cub.2020.03.022 ;PMID: 32197085

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3
The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade
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The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade

Antiviral research, 2020-04, Vol.176 [Peer Reviewed Journal]

Attribution - NonCommercial - NoDerivatives ;ISSN: 0166-3542 ;EISSN: 1872-9096 ;DOI: 10.1016/j.antiviral.2020.104742 ;PMID: 32057769

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4
Receptor Recognition by the Novel Coronavirus from Wuhan: an Analysis Based on Decade-Long Structural Studies of SARS Coronavirus
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Receptor Recognition by the Novel Coronavirus from Wuhan: an Analysis Based on Decade-Long Structural Studies of SARS Coronavirus

Journal of virology, 2020-03, Vol.94 (7) [Peer Reviewed Journal]

Copyright © 2020 American Society for Microbiology. ;Copyright © 2020 American Society for Microbiology. 2020 American Society for Microbiology ;ISSN: 0022-538X ;EISSN: 1098-5514 ;DOI: 10.1128/jvi.00127-20 ;PMID: 31996437

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5
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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6
Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization
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Article
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Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization

Cell host & microbe, 2021-05, Vol.29 (5), p.747-751.e4 [Peer Reviewed Journal]

2021 Elsevier Inc. ;Copyright © 2021 Elsevier Inc. All rights reserved. ;2021 Elsevier Inc. 2021 Elsevier Inc. ;ISSN: 1931-3128 ;EISSN: 1934-6069 ;DOI: 10.1016/j.chom.2021.04.007 ;PMID: 33887205

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7
A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells
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A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells

Molecular Cell, 2020-05, Vol.78 (4), p.779-784.e5 [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: 1097-2765 ;EISSN: 1097-4164 ;DOI: 10.1016/j.molcel.2020.04.022 ;PMID: 32362314

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8
Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite
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Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite

Cell host & microbe, 2021-05, Vol.29 (5), p.819-833.e7 [Peer Reviewed Journal]

2021 Elsevier Inc. ;Copyright © 2021 Elsevier Inc. All rights reserved. ;2021 Elsevier Inc. 2021 Elsevier Inc. ;ISSN: 1931-3128 ;EISSN: 1934-6069 ;DOI: 10.1016/j.chom.2021.03.005 ;PMID: 33789084

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9
Structural diversity of the SARS-CoV-2 Omicron spike
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Structural diversity of the SARS-CoV-2 Omicron spike

Molecular cell, 2022-06, Vol.82 (11), p.2050-2068.e6 [Peer Reviewed Journal]

2022 Elsevier Inc. ;Copyright © 2022 Elsevier Inc. All rights reserved. ;2022 Elsevier Inc. 2022 Elsevier Inc. ;ISSN: 1097-2765 ;EISSN: 1097-4164 ;DOI: 10.1016/j.molcel.2022.03.028 ;PMID: 35447081

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10
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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11
Antibody evasion by the P.1 strain of SARS-CoV-2
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Article
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Antibody evasion by the P.1 strain of SARS-CoV-2

Cell, 2021-05, Vol.184 (11), p.2939-2954.e9 [Peer Reviewed Journal]

2021 The Author(s) ;Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved. ;2021 The Author(s) 2021 ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2021.03.055 ;PMID: 33852911

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12
Circulating SARS-CoV-2 spike N439K variants maintain fitness while evading antibody-mediated immunity
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Article
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Circulating SARS-CoV-2 spike N439K variants maintain fitness while evading antibody-mediated immunity

Cell, 2021-03, Vol.184 (5), p.1171-1187.e20 [Peer Reviewed Journal]

2021 The Authors ;Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved. ;2021 The Authors 2021 ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2021.01.037 ;PMID: 33621484

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13
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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14
Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2
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Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2

Cell, 2022-02, Vol.185 (4), p.630-640.e10 [Peer Reviewed Journal]

2022 Elsevier Inc. ;Copyright © 2022 Elsevier Inc. All rights reserved. ;2022 Elsevier Inc. 2022 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2022.01.001 ;PMID: 35093192

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15
Striking antibody evasion manifested by the Omicron variant of SARS-CoV-2
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Striking antibody evasion manifested by the Omicron variant of SARS-CoV-2

Nature (London), 2022-02, Vol.602 (7898), p.676-681 [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/s41586-021-04388-0 ;PMID: 35016198

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16
Detection of a SARS-CoV-2 variant of concern in South Africa
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Detection of a SARS-CoV-2 variant of concern in South Africa

Nature (London), 2021-04, Vol.592 (7854), p.438-443 [Peer Reviewed Journal]

COPYRIGHT 2021 Nature Publishing Group ;Copyright Nature Publishing Group Apr 15, 2021 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-021-03402-9 ;PMID: 33690265

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17
Cell entry mechanisms of SARS-CoV-2
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Cell entry mechanisms of SARS-CoV-2

Proceedings of the National Academy of Sciences - PNAS, 2020-05, Vol.117 (21), p.11727-11734 [Peer Reviewed Journal]

Copyright © 2020 the Author(s). Published by PNAS. ;Copyright National Academy of Sciences May 26, 2020 ;Copyright © 2020 the Author(s). Published by PNAS. 2020 ;ISSN: 0027-8424 ;EISSN: 1091-6490 ;DOI: 10.1073/pnas.2003138117 ;PMID: 32376634

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18
Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
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Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2

Cell, 2020-05, Vol.181 (4), p.894-904.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.2020.03.045 ;PMID: 32275855

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19
The Omicron variant is highly resistant against antibody-mediated neutralization: Implications for control of the COVID-19 pandemic
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Article
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The Omicron variant is highly resistant against antibody-mediated neutralization: Implications for control of the COVID-19 pandemic

Cell, 2022-02, Vol.185 (3), p.447-456.e11 [Peer Reviewed Journal]

2021 Elsevier Inc. ;Copyright © 2021 Elsevier Inc. All rights reserved. ;2021 Elsevier Inc. 2021 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2021.12.032 ;PMID: 35026151

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20
The variant gambit: COVID-19’s next move
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The variant gambit: COVID-19’s next move

Cell host & microbe, 2021-04, Vol.29 (4), p.508-515 [Peer Reviewed Journal]

2021 ;Copyright © 2021. Published by Elsevier Inc. ;COPYRIGHT 2021 Elsevier B.V. ;2021 Published by Elsevier Inc. 2021 ;ISSN: 1931-3128 ;EISSN: 1934-6069 ;DOI: 10.1016/j.chom.2021.02.020 ;PMID: 33789086

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