标题
How the coronavirus infects cells — and why Delta is so dangerous
作者
关键词
-
出版物
NATURE
Volume 595, Issue 7869, Pages 640-644
出版商
Springer Science and Business Media LLC
发表日期
2021-07-28
DOI
10.1038/d41586-021-02039-y
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- SARS-CoV-2 entry into human airway organoids is serine protease-mediated and facilitated by the multibasic cleavage site
- (2021) Anna Z Mykytyn et al. eLife
- Nsp1 protein of SARS-CoV-2 disrupts the mRNA export machinery to inhibit host gene expression
- (2021) Ke Zhang et al. Science Advances
- SARS-CoV-2 spike protein dictates syncytium-mediated lymphocyte elimination
- (2021) Zhengrong Zhang et al. CELL DEATH AND DIFFERENTIATION
- Drugs that inhibit TMEM16 proteins block SARS-CoV-2 spike-induced syncytia
- (2021) Luca Braga et al. NATURE
- SARS-CoV-2 uses a multipronged strategy to impede host protein synthesis
- (2021) Yaara Finkel et al. NATURE
- The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets
- (2021) Thomas P. Peacock et al. Nature Microbiology
- Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity
- (2021) Sophie M.-C. Gobeil et al. SCIENCE
- TMEM41B is a host factor required for the replication of diverse coronaviruses including SARS-CoV-2
- (2021) Joseph D. Trimarco et al. PLoS Pathogens
- Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro
- (2020) Manli Wang et al. CELL RESEARCH
- Imbalanced Host Response to SARS-CoV-2 Drives Development of COVID-19
- (2020) Daniel Blanco-Melo et al. CELL
- 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
- A SARS-CoV-2 protein interaction map reveals targets for drug repurposing
- (2020) David E. Gordon et al. NATURE
- Structural basis of receptor recognition by SARS-CoV-2
- (2020) Jian Shang et al. NATURE
- Does SARS-CoV-2 Bind to Human ACE2 Stronger Than SARS-CoV?
- (2020) Hoang Linh Nguyen et al. JOURNAL OF PHYSICAL CHEMISTRY B
- Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2
- (2020) Matthias Thoms et al. SCIENCE
- A molecular pore spans the double membrane of the coronavirus replication organelle
- (2020) Georg Wolff et al. SCIENCE
- Structures and distributions of SARS-CoV-2 spike proteins on intact virions
- (2020) Zunlong Ke et al. NATURE
- SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation
- (2020) Katharina Schubert et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges
- (2020) Beata Turoňová et al. SCIENCE
- Beyond Shielding: The Roles of Glycans in the SARS-CoV-2 Spike Protein
- (2020) Lorenzo Casalino et al. ACS Central Science
- β-Coronaviruses Use Lysosomes for Egress Instead of the Biosynthetic Secretory Pathway
- (2020) Sourish Ghosh et al. CELL
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