Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2
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Title
Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2
Authors
Keywords
omicron, delta, variants of concern, VOCs, receptor-binding domain, RBD, hACE2, structure
Journal
CELL
Volume 185, Issue 4, Pages 630-640.e10
Publisher
Elsevier BV
Online
2022-01-06
DOI
10.1016/j.cell.2022.01.001
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Note: Only part of the references are listed.- Prospective mapping of viral mutations that escape antibodies used to treat COVID-19
- (2021) Tyler N. Starr et al. SCIENCE
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- (2021) Qianqian Li et al. CELL
- Multiple SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity
- (2021) Wilfredo F. Garcia-Beltran et al. CELL
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- (2021) Daming Zhou et al. CELL
- SARS-CoV-2 variant B.1.1.7 is susceptible to neutralizing antibodies elicited by ancestral spike vaccines
- (2021) Xiaoying Shen et al. Cell Host & Microbe
- Neutralization of SARS-CoV-2 lineage B.1.1.7 pseudovirus by BNT162b2 vaccine–elicited human sera
- (2021) Alexander Muik et al. SCIENCE
- Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 spike protein with the human receptor ACE2
- (2021) Amit Singh et al. Scientific Reports
- SARS-CoV-2 evolution in an immunocompromised host reveals shared neutralization escape mechanisms
- (2021) Sarah A. Clark et al. CELL
- New SARS-CoV-2 Variants — Clinical, Public Health, and Vaccine Implications
- (2021) Salim S. Abdool Karim et al. NEW ENGLAND JOURNAL OF MEDICINE
- Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies
- (2021) Xing Zhu et al. PLOS BIOLOGY
- Q493K and Q498H substitutions in Spike promote adaptation of SARS-CoV-2 in mice
- (2021) Kun Huang et al. EBioMedicine
- Changes in symptomatology, reinfection, and transmissibility associated with the SARS-CoV-2 variant B.1.1.7: an ecological study
- (2021) Mark S Graham et al. Lancet Public Health
- Binding and molecular basis of the bat coronavirus RaTG13 virus to ACE2 in humans and other species
- (2021) Kefang Liu et al. CELL
- Humoral immune response to circulating SARS-CoV-2 variants elicited by inactivated and RBD-subunit vaccines
- (2021) Yunlong Cao et al. CELL RESEARCH
- Molecular basis of cross‐species ACE2 interactions with SARS‐CoV‐2‐like viruses of pangolin origin
- (2021) Sheng Niu et al. EMBO JOURNAL
- The reproductive number of the Delta variant of SARS-CoV-2 is far higher compared to the ancestral SARS-CoV-2 virus
- (2021) Ying Liu et al. JOURNAL OF TRAVEL MEDICINE
- The molecular basis for SARS-CoV-2 binding to dog ACE2
- (2021) Zengyuan Zhang et al. Nature Communications
- SARS-CoV-2 variant prediction and antiviral drug design are enabled by RBD in vitro evolution
- (2021) Jiří Zahradník et al. Nature Microbiology
- Emerging SARS-CoV-2 Variants of Concern (VOCs): An Impending Global Crisis
- (2021) Angel Yun-Kuan Thye et al. Biomedicines
- The emergence, genomic diversity and global spread of SARS-CoV-2
- (2021) Juan Li et al. NATURE
- Molecular insights into receptor binding of recent emerging SARS-CoV-2 variants
- (2021) Pengcheng Han et al. Nature Communications
- The significant immune escape of pseudotyped SARS-CoV-2 variant Omicron
- (2021) Li Zhang et al. Emerging Microbes & Infections
- The Global Epidemic of the SARS-CoV-2 Delta Variant, Key Spike Mutations and Immune Escape
- (2021) Dandan Tian et al. Frontiers in Immunology
- Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
- (2020) Qihui Wang et al. CELL
- SARS-CoV-2: Virology, epidemiology, immunology and vaccine development
- (2020) Marc Baay et al. BIOLOGICALS
- Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike
- (2020) Lihong Liu et al. NATURE
- Mapping Neutralizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution Serology
- (2020) Luca Piccoli et al. CELL
- Broad host range of SARS-CoV-2 and the molecular basis for SARS-CoV-2 binding to cat ACE2
- (2020) Lili Wu et al. Cell Discovery
- Persistence and Evolution of SARS-CoV-2 in an Immunocompromised Host
- (2020) Bina Choi et al. NEW ENGLAND JOURNAL OF MEDICINE
- New tools for automated high-resolution cryo-EM structure determination in RELION-3
- (2018) Jasenko Zivanov et al. eLife
- MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
- (2017) Shawn Q Zheng et al. NATURE METHODS
- MolProbity: More and better reference data for improved all-atom structure validation
- (2017) Christopher J. Williams et al. PROTEIN SCIENCE
- Epidemiology, Genetic Recombination, and Pathogenesis of Coronaviruses
- (2016) Shuo Su et al. TRENDS IN MICROBIOLOGY
- CTFFIND4: Fast and accurate defocus estimation from electron micrographs
- (2015) Alexis Rohou et al. JOURNAL OF STRUCTURAL BIOLOGY
- Bat-to-human: spike features determining ‘host jump’ of coronaviruses SARS-CoV, MERS-CoV, and beyond
- (2015) Guangwen Lu et al. TRENDS IN MICROBIOLOGY
- Quantifying the local resolution of cryo-EM density maps
- (2013) Alp Kucukelbir et al. NATURE METHODS
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- MolProbity: all-atom structure validation for macromolecular crystallography
- (2009) Vincent B. Chen et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
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