Related references
Note: Only part of the references are listed.Considerable escape of SARS-CoV-2 Omicron to antibody neutralization
Delphine Planas et al.
NATURE (2022)
Mechanisms of SARS-CoV-2 entry into cells
Cody B. Jackson et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2022)
COULD NEW COVID VARIANTS UNDERMINE VACCINES? LABS SCRAMBLE TO FIND OUT
Ewen Callaway
NATURE (2021)
Evolution of antibody immunity to SARS-CoV-2
Christian Gaebler et al.
NATURE (2021)
Prospective mapping of viral mutations that escape antibodies used to treat COVID-19
Tyler N. Starr et al.
SCIENCE (2021)
Neutralizing antibodies targeting SARS-CoV-2 spike protein
Shi Xiaojie et al.
STEM CELL RESEARCH (2021)
Molecular determinants and mechanism for antibody cocktail preventing SARS-CoV-2 escape
Zhiqiang Ku et al.
NATURE COMMUNICATIONS (2021)
SARS-CoV-2 501Y.V2 variants lack higher infectivity but do have immune escape
Qianqian Li et al.
CELL (2021)
Circulating SARS-CoV-2 spike N439K variants maintain fitness while evading antibody-mediated immunity
Emma C. Thomson et al.
CELL (2021)
Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7
Pengfei Wang et al.
NATURE (2021)
Memory B cell repertoire for recognition of evolving SARS-CoV-2 spike
Pei Tong et al.
CELL (2021)
SARS-CoV-2 variants, spike mutations and immune escape
William T. Harvey et al.
NATURE REVIEWS MICROBIOLOGY (2021)
Multivalency transforms SARS-CoV-2 antibodies into ultrapotent neutralizers
Edurne Rujas et al.
NATURE COMMUNICATIONS (2021)
Mapping mutations to the SARS-CoV-2 RBD that escape binding by different classes of antibodies
Allison J. Greaney et al.
NATURE COMMUNICATIONS (2021)
Effects of common mutations in the SARS-CoV-2 Spike RBD and its ligand, the human ACE2 receptor on binding affinity and kinetics
Michael Barton et al.
ELIFE (2021)
COVIDium: a COVID-19 resource compendium
Rohit Satyam et al.
DATABASE-THE JOURNAL OF BIOLOGICAL DATABASES AND CURATION (2021)
Bioinformatics resources facilitate understanding and harnessing clinical research of SARS-CoV-2
Md Asif Ahsan et al.
BRIEFINGS IN BIOINFORMATICS (2021)
OverCOVID: an integrative web portal for SARS-CoV-2 bioinformatics resources
Md Asif Ahsan et al.
JOURNAL OF INTEGRATIVE BIOINFORMATICS (2021)
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Renhong Yan et al.
SCIENCE (2020)
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Daniel Wrapp et al.
SCIENCE (2020)
Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
Alexandra C. Walls et al.
CELL (2020)
Key residues of the receptor binding motif in the spike protein of SARS-CoV-2 that interact with ACE2 and neutralizing antibodies
Chunyan Yi et al.
CELLULAR & MOLECULAR IMMUNOLOGY (2020)
Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody
Xiaolong Tian et al.
EMERGING MICROBES & INFECTIONS (2020)
A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2
Yan Wu et al.
SCIENCE (2020)
A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV
Meng Yuan et al.
SCIENCE (2020)
A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2
Rui Shi et al.
NATURE (2020)
Human neutralizing antibodies elicited by SARS-CoV-2 infection
Bin Ju et al.
NATURE (2020)
Structural basis of receptor recognition by SARS-CoV-2
Jian Shang et al.
NATURE (2020)
The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity
Qianqian Li et al.
CELL (2020)
Developing a Fully Glycosylated Full-Length SARS-CoV-2 Spike Protein Model in a Viral Membrane
Hyeonuk Woo et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2020)
A Therapeutic Non-self-reactive SARS-CoV-2 Antibody Protects from Lung Pathology in a COVID-19 Hamster Model
Jakob Kreye et al.
CELL (2020)
Structurally Resolved SARS-CoV-2 Antibody Shows High Efficacy in Severely Infected Hamsters and Provides a Potent Cocktail Pairing Strategy
Shuo Du et al.
CELL (2020)
Mapping Neutralizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution Serology
Luca Piccoli et al.
CELL (2020)
Neutralization of SARS-CoV-2 by Destruction of the Prefusion Spike (vol 28, pg 445, 2020)
Jiandong Huo et al.
CELL HOST & MICROBE (2020)
Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient
Daming Zhou et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2020)
A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2
Xiangyang Chi et al.
SCIENCE (2020)
Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail
Johanna Hansen et al.
SCIENCE (2020)
Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody
Zhe Lv et al.
SCIENCE (2020)
Structural basis of a shared antibody response to SARS-CoV-2
Meng Yuan et al.
SCIENCE (2020)
SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Christopher O. Barnes et al.
NATURE (2020)
Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms
M. Alejandra Tortorici et al.
SCIENCE (2020)
Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein
Antoni G. Wrobel et al.
NATURE COMMUNICATIONS (2020)
Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition
Oliver C. Grant et al.
SCIENTIFIC REPORTS (2020)
An Alternative Binding Mode of IGHV3-53 Antibodies to the SARS-CoV-2 Receptor Binding Domain
Nicholas C. Wu et al.
CELL REPORTS (2020)
Comparative Review of SARS-CoV-2, SARS-CoV, MERS-CoV, and Influenza A Respiratory Viruses
Zeinab Abdelrahman et al.
FRONTIERS IN IMMUNOLOGY (2020)
Cross-Neutralization of a SARS-CoV-2 Antibody to a Functionally Conserved Site Is Mediated by Avidity
Hejun Liu et al.
IMMUNITY (2020)
CovMT: an interactive SARS-CoV-2 mutation tracker, with a focus on critical variants
Intikhab Alam et al.
LANCET INFECTIOUS DISEASES (2020)
Escape from neutralizing antibodies by SARS-CoV-2 spike protein variants
Yiska Weisblum et al.
ELIFE (2020)
Mutated COVID-19 may foretell a great risk for mankind in the future
A. A. Dawood
NEW MICROBES AND NEW INFECTIONS (2020)
The role of coevolutionary signatures in protein interaction dynamics, complex inference, molecular recognition, and mutational landscapes
Faruck Morcos et al.
CURRENT OPINION IN STRUCTURAL BIOLOGY (2019)
Origin and evolution of pathogenic coronaviruses
Jie Cui et al.
NATURE REVIEWS MICROBIOLOGY (2019)
Finding the ΔΔG spot: Are predictors of binding affinity changes upon mutations in protein-protein interactions ready for it?
Cunliang Geng et al.
WILEY INTERDISCIPLINARY REVIEWS-COMPUTATIONAL MOLECULAR SCIENCE (2019)
GISAID: Global initiative on sharing all influenza data - from vision to reality
Yuelong Shu et al.
EUROSURVEILLANCE (2017)
Diversity of Functionally Permissive Sequences in the Receptor-Binding Site of Influenza Hemagglutinin (vol 21, pg 742, 2017)
Nicholas C. Wu et al.
CELL HOST & MICROBE (2017)
PRODIGY: a web server for predicting the binding affinity of protein-protein complexes
Li C. Xue et al.
BIOINFORMATICS (2016)
Contacts-based prediction of binding affinity in protein-protein complexes
Anna Vangone et al.
ELIFE (2015)
Evol and ProDy for bridging protein sequence evolution and structural dynamics
Ahmet Bakan et al.
BIOINFORMATICS (2014)
MAFFT Multiple Sequence Alignment Software Version 7: Improvements in Performance and Usability
Kazutaka Katoh et al.
MOLECULAR BIOLOGY AND EVOLUTION (2013)
BeAtMuSiC: prediction of changes in protein-protein binding affinity on mutations
Yves Dehouck et al.
NUCLEIC ACIDS RESEARCH (2013)
Epistasis - the essential role of gene interactions in the structure and evolution of genetic systems
Patrick C. Phillips
NATURE REVIEWS GENETICS (2008)
Mutual information without the influence of phylogeny or entropy dramatically improves residue contact prediction
S. D. Dunn et al.
BIOINFORMATICS (2008)
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
WH Li et al.
NATURE (2003)