标题
Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement
作者
关键词
-
出版物
SCIENCE
Volume 375, Issue 6583, Pages 864-868
出版商
American Association for the Advancement of Science (AAAS)
发表日期
2022-02-25
DOI
10.1126/science.abn8652
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。- Considerable escape of SARS-CoV-2 Omicron to antibody neutralization
- (2022) Delphine Planas et al. NATURE
- Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift
- (2022) Elisabetta Cameroni et al. NATURE
- Rapid epidemic expansion of the SARS-CoV-2 Omicron variant in southern Africa
- (2022) Raquel Viana et al. NATURE
- Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
- (2022) Yunlong Cao et al. NATURE
- Striking antibody evasion manifested by the Omicron variant of SARS-CoV-2
- (2022) Lihong Liu et al. NATURE
- Antibody-mediated broad sarbecovirus neutralization through ACE2 molecular mimicry
- (2022) Young-Jun Park et al. SCIENCE
- Broad and potent activity against SARS-like viruses by an engineered human monoclonal antibody
- (2021) C. Garrett Rappazzo et al. SCIENCE
- Prospective mapping of viral mutations that escape antibodies used to treat COVID-19
- (2021) Tyler N. Starr et al. SCIENCE
- Circulating SARS-CoV-2 spike N439K variants maintain fitness while evading antibody-mediated immunity
- (2021) Emma C. Thomson et al. CELL
- Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies
- (2021) Dami A. Collier et al. NATURE
- Antibody Resistance of SARS-CoV-2 Variants B.1.351 and B.1.1.7
- (2021) Pengfei Wang et al. NATURE
- N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
- (2021) Matthew McCallum et al. CELL
- Adjuvanting a subunit COVID-19 vaccine to induce protective immunity
- (2021) Prabhu S. Arunachalam et al. NATURE
- 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
- Tackling COVID-19 with neutralizing monoclonal antibodies
- (2021) Davide Corti et al. CELL
- Elicitation of broadly protective sarbecovirus immunity by receptor-binding domain nanoparticle vaccines
- (2021) Alexandra C. Walls et al. CELL
- Broad sarbecovirus neutralization by a human monoclonal antibody
- (2021) M. Alejandra Tortorici et al. NATURE
- SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
- (2021) Tyler N. Starr et al. NATURE
- Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants
- (2021) Meng Yuan et al. SCIENCE
- SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
- (2021) Matthew McCallum et al. SCIENCE
- Chimeric spike mRNA vaccines protect against Sarbecovirus challenge in mice
- (2021) David R. Martinez et al. SCIENCE
- Antibodies elicited by mRNA-1273 vaccination bind more broadly to the receptor binding domain than do those from SARS-CoV-2 infection
- (2021) Allison J. Greaney et al. Science Translational Medicine
- Convalescent-Phase Sera and Vaccine-Elicited Antibodies Largely Maintain Neutralizing Titer against Global SARS-CoV-2 Variant Spikes
- (2021) Takuya Tada et al. mBio
- Broad cross-reactivity across sarbecoviruses exhibited by a subset of COVID-19 donor-derived neutralizing antibodies
- (2021) Claudia A. Jette et al. Cell Reports
- Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail
- (2021) Jinhui Dong et al. Nature Microbiology
- Molecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants
- (2021) Matthew McCallum et al. SCIENCE
- A broadly cross-reactive antibody neutralizes and protects against sarbecovirus challenge in mice
- (2021) David R. Martinez et al. Science Translational Medicine
- Emerging SARS-CoV-2 variants expand species tropism to murines
- (2021) Huiping Shuai et al. EBioMedicine
- Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
- (2020) Daniel Wrapp et al. SCIENCE
- Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
- (2020) Alexandra C. Walls et al. CELL
- Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
- (2020) Dora Pinto et al. NATURE
- Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
- (2020) Jun Lan et al. NATURE
- Deep mutational scanning of SARS-CoV-2 receptor binding domain reveals constraints on folding and ACE2 binding
- (2020) Tyler N. Starr et al. CELL
- Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies
- (2020) Christopher O. Barnes et al. CELL
- Potently neutralizing and protective human antibodies against SARS-CoV-2
- (2020) Seth J. Zost et al. NATURE
- Structure-based design of prefusion-stabilized SARS-CoV-2 spikes
- (2020) Ching-Lin Hsieh et al. SCIENCE
- Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail
- (2020) Johanna Hansen et al. SCIENCE
- Broad neutralization of SARS-related viruses by human monoclonal antibodies
- (2020) Anna Z. Wec et al. SCIENCE
- A Mouse-Adapted SARS-CoV-2 Induces Acute Lung Injury and Mortality in Standard Laboratory Mice
- (2020) Sarah R. Leist et al. CELL
- 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
- SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
- (2020) Christopher O. Barnes et al. NATURE
- Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein
- (2020) Christine Toelzer et al. SCIENCE
- Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction
- (2020) Ali Punjani et al. NATURE METHODS
- Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix
- (2019) Dorothee Liebschner et al. Acta Crystallographica Section D-Structural Biology
- Real-time cryo-electron microscopy data preprocessing with Warp
- (2019) Dimitry Tegunov et al. NATURE METHODS
- ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps
- (2018) Tristan Ian Croll Acta Crystallographica Section D-Structural Biology
- Automatically Fixing Errors in Glycoprotein Structures with Rosetta
- (2018) Brandon Frenz et al. STRUCTURE
- New tools for automated high-resolution cryo-EM structure determination in RELION-3
- (2018) Jasenko Zivanov et al. eLife
- A Bayesian approach to beam-induced motion correction in cryo-EM single-particle analysis
- (2018) Jasenko Zivanov et al. IUCrJ
- cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
- (2017) Ali Punjani et al. NATURE METHODS
- UCSF ChimeraX: Meeting modern challenges in visualization and analysis
- (2017) Thomas D. Goddard et al. PROTEIN SCIENCE
- Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer
- (2016) Alexandra C. Walls et al. NATURE
- Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta
- (2016) Ray Yu-Ruei Wang et al. eLife
- EMRinger: side chain–directed model and map validation for 3D cryo-electron microscopy
- (2015) Benjamin A Barad et al. NATURE METHODS
- Privateer: software for the conformational validation of carbohydrate structures
- (2015) Jon Agirre et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Privateer: software for the conformational validation of carbohydrate structures
- (2015) Jon Agirre et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
- (2013) Shaoxia Chen et al. ULTRAMICROSCOPY
- RELION: Implementation of a Bayesian approach to cryo-EM structure determination
- (2012) Sjors H.W. Scheres JOURNAL OF STRUCTURAL BIOLOGY
- REFMAC5 for the refinement of macromolecular crystal structures
- (2011) Garib N. Murshudov et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Features and development ofCoot
- (2010) P. Emsley 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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