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1
Site-specific glycan analysis of the SARS-CoV-2 spike
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Site-specific glycan analysis of the SARS-CoV-2 spike

Science, 2020-07, Vol.369 (6501) [Peer Reviewed Journal]

2020. 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.abb9983

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2
The 3.1-Angstrom Cryo-electron Microscopy Structure of the Porcine Epidemic Diarrhea Virus Spike Protein in the Prefusion Conformation
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The 3.1-Angstrom Cryo-electron Microscopy Structure of the Porcine Epidemic Diarrhea Virus Spike Protein in the Prefusion Conformation

Journal of virology, 2019-12, Vol.93 (23) [Peer Reviewed Journal]

Copyright © 2019 Wrapp and McLellan. ;Copyright © 2019 Wrapp and McLellan. 2019 Wrapp and McLellan ;ISSN: 0022-538X ;EISSN: 1098-5514 ;DOI: 10.1128/jvi.00923-19 ;PMID: 31534041

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3
Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies
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Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies

Cell, 2020-05, Vol.181 (5), p.1004-1015.e15 [Peer Reviewed Journal]

2020 Elsevier Inc. ;Copyright © 2020 Elsevier Inc. All rights reserved. ;2020 Elsevier Inc. 2020 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2020.04.031 ;PMID: 32375025

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4
Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis
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Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis

Scientific Reports, 2018-10, Vol.8 (1), p.15701-11, Article 15701 [Peer Reviewed Journal]

2018. This work is published under http://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. ;2018. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at http://creativecommons.org/licenses/by/4.0 ;The Author(s) 2018 ;ISSN: 2045-2322 ;EISSN: 2045-2322 ;DOI: 10.1038/s41598-018-34171-7 ;PMID: 30356097

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5
SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma
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SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma

Proceedings of the National Academy of Sciences - PNAS, 2021-09, Vol.118 (36) [Peer Reviewed Journal]

Copyright National Academy of Sciences Sep 7, 2021 ;Copyright © 2021 the Author(s). Published by PNAS. 2021 ;ISSN: 0027-8424 ;EISSN: 1091-6490 ;DOI: 10.1073/pnas.2103154118 ;PMID: 34417349

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6
Vulnerabilities in coronavirus glycan shields despite extensive glycosylation
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Vulnerabilities in coronavirus glycan shields despite extensive glycosylation

Nature communications, 2020-05, Vol.11 (1), p.2688-2688, Article 2688 [Peer Reviewed Journal]

The Author(s) 2020. This work is published under http://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. ;The Author(s) 2020 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-020-16567-0 ;PMID: 32461612

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7
Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
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Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen

Proceedings of the National Academy of Sciences - PNAS, 2017-08, Vol.114 (35), p.E7348-E7357 [Peer Reviewed Journal]

Volumes 1–89 and 106–114, copyright as a collective work only; author(s) retains copyright to individual articles ;Copyright National Academy of Sciences Aug 29, 2017 ;ISSN: 0027-8424 ;EISSN: 1091-6490 ;DOI: 10.1073/pnas.1707304114 ;PMID: 28807998

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8
A glycan gate controls opening of the SARS-CoV-2 spike protein
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A glycan gate controls opening of the SARS-CoV-2 spike protein

Nature chemistry, 2021-10, Vol.13 (10), p.963-968 [Peer Reviewed Journal]

2021. The Author(s), under exclusive licence to Springer Nature Limited. ;The Author(s), under exclusive licence to Springer Nature Limited 2021. ;ISSN: 1755-4330 ;EISSN: 1755-4349 ;DOI: 10.1038/s41557-021-00758-3 ;PMID: 34413500

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9
Beyond Shielding: The Roles of Glycans in the SARS-CoV‑2 Spike Protein
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Beyond Shielding: The Roles of Glycans in the SARS-CoV‑2 Spike Protein

ACS central science, 2020-10, Vol.6 (10), p.1722-1734

2020 American Chemical Society ;ISSN: 2374-7943 ;EISSN: 2374-7951 ;DOI: 10.1021/acscentsci.0c01056 ;PMID: 33140034

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10
Structure of Respiratory Syncytial Virus Fusion Glycoprotein in the Postfusion Conformation Reveals Preservation of Neutralizing Epitopes
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Structure of Respiratory Syncytial Virus Fusion Glycoprotein in the Postfusion Conformation Reveals Preservation of Neutralizing Epitopes

Journal of Virology, 2011-08, Vol.85 (15), p.7788-7796 [Peer Reviewed Journal]

2015 INIST-CNRS ;Copyright © 2011, American Society for Microbiology 2011 American Society for Microbiology ;ISSN: 0022-538X ;EISSN: 1098-5514 ;DOI: 10.1128/JVI.00555-11 ;PMID: 21613394

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11
Host species restriction of Middle East respiratory syndrome coronavirus through its receptor, dipeptidyl peptidase 4
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Host species restriction of Middle East respiratory syndrome coronavirus through its receptor, dipeptidyl peptidase 4

Journal of virology, 2014-08, Vol.88 (16), p.9220-9232 [Peer Reviewed Journal]

Copyright © 2014, American Society for Microbiology. All Rights Reserved. ;Copyright © 2014, American Society for Microbiology. All Rights Reserved. 2014 American Society for Microbiology ;ISSN: 0022-538X ;EISSN: 1098-5514 ;DOI: 10.1128/jvi.00676-14 ;PMID: 24899185

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12
Molecular determinants and mechanism for antibody cocktail preventing SARS-CoV-2 escape
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Molecular determinants and mechanism for antibody cocktail preventing SARS-CoV-2 escape

Nature communications, 2021-01, Vol.12 (1), p.469-13, Article 469 [Peer Reviewed Journal]

The Author(s) 2021. This work is published under http://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. ;The Author(s) 2021. corrected publication 2021. This work is published under http://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. ;The Author(s) 2021, corrected publication 2021 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-020-20789-7 ;PMID: 33473140

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13
Structure of the Respiratory Syncytial Virus Polymerase Complex
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Structure of the Respiratory Syncytial Virus Polymerase Complex

Cell, 2019-09, Vol.179 (1), p.193-204.e14 [Peer Reviewed Journal]

2019 Elsevier Inc. ;Copyright © 2019 Elsevier Inc. All rights reserved. ;Distributed under a Creative Commons Attribution 4.0 International License ;2019 Elsevier Inc. 2019 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2019.08.014 ;PMID: 31495574

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14
Suptavumab for the Prevention of Medically Attended Respiratory Syncytial Virus Infection in Preterm Infants
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Suptavumab for the Prevention of Medically Attended Respiratory Syncytial Virus Infection in Preterm Infants

Clinical infectious diseases, 2021-12, Vol.73 (11), p.e4400-e4408 [Peer Reviewed Journal]

The Author(s) 2020. Published by Oxford University Press for the Infectious Diseases Society of America. ;The Author(s) 2020. Published by Oxford University Press for the Infectious Diseases Society of America. 2020 ;ISSN: 1058-4838 ;EISSN: 1537-6591 ;DOI: 10.1093/cid/ciaa951 ;PMID: 32897368

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15
Local computational methods to improve the interpretability and analysis of cryo-EM maps
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Local computational methods to improve the interpretability and analysis of cryo-EM maps

Nature communications, 2021-02, Vol.12 (1), p.1240-1240, Article 1240 [Peer Reviewed Journal]

The Author(s) 2021. This work is published under http://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. ;The Author(s) 2021 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-021-21509-5 ;PMID: 33623015

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16
Alternative conformations of a major antigenic site on RSV F
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Alternative conformations of a major antigenic site on RSV F

PLoS pathogens, 2019-07, Vol.15 (7), p.e1007944-e1007944 [Peer Reviewed Journal]

COPYRIGHT 2019 Public Library of Science ;COPYRIGHT 2019 Public Library of Science ;2019 Jones et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2019 Jones et al 2019 Jones et al ;ISSN: 1553-7374 ;ISSN: 1553-7366 ;EISSN: 1553-7374 ;DOI: 10.1371/journal.ppat.1007944 ;PMID: 31306469

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17
Structure and immunogenicity of pre-fusion-stabilized human metapneumovirus F glycoprotein
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Article
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Structure and immunogenicity of pre-fusion-stabilized human metapneumovirus F glycoprotein

Nature communications, 2017-11, Vol.8 (1), p.1528-11, Article 1528 [Peer Reviewed Journal]

2017. This work is published under http://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. ;The Author(s) 2017 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-017-01708-9 ;PMID: 29142300

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18
Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins
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Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins

Nature communications, 2022-03, Vol.13 (1), p.1299-1299, Article 1299 [Peer Reviewed Journal]

2022. The Author(s). ;The Author(s) 2022. This work is published under http://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. ;The Author(s) 2022 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-022-28931-3 ;PMID: 35288548

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19
Global site-specific analysis of glycoprotein N-glycan processing
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Global site-specific analysis of glycoprotein N-glycan processing

Nature protocols, 2018-06, Vol.13 (6), p.1196-1212 [Peer Reviewed Journal]

COPYRIGHT 2018 Nature Publishing Group ;COPYRIGHT 2018 Nature Publishing Group ;Copyright Nature Publishing Group Jun 2018 ;Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. 2018 ;ISSN: 1754-2189 ;EISSN: 1750-2799 ;DOI: 10.1038/nprot.2018.024 ;PMID: 29725121

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20
Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies
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Article
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Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies

Cell, 2020-06, Vol.181 (6), p.1436-1441 [Peer Reviewed Journal]

2020 Elsevier Inc. ;2020 Elsevier Inc. 2020 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2020.05.047 ;PMID: 32531248

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