SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
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Title
SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
Authors
Keywords
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Journal
Nature Communications
Volume 11, Issue 1, Pages -
Publisher
Springer Science and Business Media LLC
Online
2020-11-26
DOI
10.1038/s41467-020-19808-4
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Note: Only part of the references are listed.- A pneumonia outbreak associated with a new coronavirus of probable bat origin
- (2020) Peng Zhou et al. NATURE
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- (2020) Daniel Wrapp et al. SCIENCE
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- SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor
- (2020) Markus Hoffmann et al. CELL
- A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells
- (2020) Markus Hoffmann et al. MOLECULAR CELL
- Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
- (2020) Jun Lan et al. NATURE
- Structural basis of receptor recognition by SARS-CoV-2
- (2020) Jian Shang et al. NATURE
- Cell entry mechanisms of SARS-CoV-2
- (2020) Jian Shang et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV
- (2020) Xiuyuan Ou et al. Nature Communications
- Host cell proteases: Critical determinants of coronavirus tropism and pathogenesis
- (2015) Jean Kaoru Millet et al. VIRUS RESEARCH
- Evidence that TMPRSS2 Activates the Severe Acute Respiratory Syndrome Coronavirus Spike Protein for Membrane Fusion and Reduces Viral Control by the Humoral Immune Response
- (2011) I. Glowacka et al. JOURNAL OF VIROLOGY
- Structure and Properties of a Complex of α-Synuclein and a Single-Domain Camelid Antibody
- (2010) Erwin J. De Genst et al. JOURNAL OF MOLECULAR BIOLOGY
- A Transmembrane Serine Protease Is Linked to the Severe Acute Respiratory Syndrome Coronavirus Receptor and Activates Virus Entry
- (2010) A. Shulla et al. JOURNAL OF VIROLOGY
- Efficient Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by the Transmembrane Protease TMPRSS2
- (2010) S. Matsuyama et al. JOURNAL OF VIROLOGY
- Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites
- (2009) S. Belouzard et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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