scholarly article | Q13442814 |
P819 | ADS bibcode | 2020NatCo..11.5413H |
P356 | DOI | 10.1038/S41467-020-19231-9 |
P698 | PubMed publication ID | 33110068 |
P50 | author | Andrew McGuire | Q56454340 |
Nicholas Hurlburt | Q57468178 | ||
Mehul S. Suthar | Q90167763 | ||
Marie Pancera | Q101038499 | ||
Venkata Viswanadh Edara | Q101561612 | ||
P2093 | author name string | Junli Feng | |
Leonidas Stamatatos | |||
Andrew B Stuart | |||
Emilie Seydoux | |||
Yu-Hsin Wan | |||
P2860 | cites work | XDS | Q27860472 |
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GlycoDelete engineering of mammalian cells simplifies N-glycosylation of recombinant proteins. | Q42825895 | ||
Viridot: An automated virus plaque (immunofocus) counter for the measurement of serological neutralizing responses with application to dengue virus | Q57794103 | ||
Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion | Q84315378 | ||
An interactive web-based dashboard to track COVID-19 in real time | Q87456354 | ||
Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2 | Q87726414 | ||
Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein | Q87973551 | ||
SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor | Q88292103 | ||
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation | Q89108866 | ||
Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses | Q89866691 | ||
SARS-CoV-2 is an appropriate name for the new coronavirus | Q90164541 | ||
Covid-19: WHO declares pandemic because of "alarming levels" of spread, severity, and inaction | Q90280296 | ||
Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV | Q90713511 | ||
Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2 | Q91807337 | ||
An Infectious cDNA Clone of SARS-CoV-2 | Q91914454 | ||
A human monoclonal antibody blocking SARS-CoV-2 infection | Q94440473 | ||
Protocol and Reagents for Pseudotyping Lentiviral Particles with SARS-CoV-2 Spike Protein for Neutralization Assays | Q94567274 | ||
A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2 | Q94670272 | ||
A human neutralizing antibody targets the receptor binding site of SARS-CoV-2 | Q95851276 | ||
Human neutralizing antibodies elicited by SARS-CoV-2 infection | Q95851279 | ||
Broad neutralization of SARS-related viruses by human monoclonal antibodies | Q96429124 | ||
Analysis of a SARS-CoV-2-Infected Individual Reveals Development of Potent Neutralizing Antibodies with Limited Somatic Mutation | Q96607975 | ||
Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies | Q97519832 | ||
Structural basis of a shared antibody response to SARS-CoV-2 | Q97526726 | ||
P433 | issue | 1 | |
P921 | main subject | SARS-CoV-2 | Q82069695 |
P304 | page(s) | 5413 | |
P577 | publication date | 2020-10-27 | |
P1433 | published in | Nature Communications | Q573880 |
P1476 | title | Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation | |
P478 | volume | 11 |
Q107980765 | SARS-CoV-2 Unrevealed: Ultrastructural and Nanomechanical Analysis |
Q99707961 | Structurally Resolved SARS-CoV-2 Antibody Shows High Efficacy in Severely Infected Hamsters and Provides a Potent Cocktail Pairing Strategy |
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