Related references
Note: Only part of the references are listed.Bi-paratopic and multivalent VH domains block ACE2 binding and neutralize SARS-CoV-2
Colton J. Bracken et al.
NATURE CHEMICAL BIOLOGY (2021)
Rational development of a human antibody cocktail that deploys multiple functions to confer Pan-SARS-CoVs protection
Hangping Yao et al.
CELL RESEARCH (2021)
Structure-based development of human antibody cocktails against SARS-CoV-2
Nan Wang et al.
CELL RESEARCH (2021)
REGN-COV2, a Neutralizing Antibody Cocktail, in Outpatients with Covid-19
D. M. Weinreich et al.
NEW ENGLAND JOURNAL OF MEDICINE (2021)
Monoclonal Antibodies to Disrupt Progression of Early Covid-19 Infection
Myron S. Cohen
NEW ENGLAND JOURNAL OF MEDICINE (2021)
SARS-CoV-2 Neutralizing Antibody LY-CoV555 in Outpatients with Covid-19
Peter Chen et al.
NEW ENGLAND JOURNAL OF MEDICINE (2021)
Prospective mapping of viral mutations that escape antibodies used to treat COVID-19
Tyler N. Starr et al.
SCIENCE (2021)
Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape
Paul-Albert Koenig et al.
SCIENCE (2021)
Robust SARS-CoV-2 infection in nasal turbinates after treatment with systemic neutralizing antibodies
Dongyan Zhou et al.
CELL HOST & MICROBE (2021)
Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7
Pengfei Wang et al.
NATURE (2021)
mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants
Zijun Wang et al.
NATURE (2021)
SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Constantinos Kurt Wibmer et al.
NATURE MEDICINE (2021)
Estimated transmissibility and impact of SARS-CoV-2 lineage B.1.1.7 in England
Nicholas G. Davies et al.
SCIENCE (2021)
Structure-based development of three- and four-antibody cocktails against SARS-CoV-2 via multiple mechanisms
Yao Sun et al.
CELL RESEARCH (2021)
Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma
Sandile Cele et al.
NATURE (2021)
Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice
Phillip Pymm et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2021)
Nanobodies from camelid mice and llamas neutralize SARS-CoV-2 variants
Jianliang Xu et al.
NATURE (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)
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Renhong Yan et al.
SCIENCE (2020)
Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
Qihui Wang et al.
CELL (2020)
Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies
Daniel Wrapp et al.
CELL (2020)
Potent Neutralizing Antibodies against SARS-CoV-2 Identified by High-Throughput Single-Cell Sequencing of Convalescent Patients' B Cells
Yunlong Cao 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)
Convergent antibody responses to SARS-CoV-2 in convalescent individuals
Davide F. Robbiani et al.
NATURE (2020)
Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike
Lihong Liu et al.
NATURE (2020)
Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2
Jiangdong Huo 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)
Distinct conformational states of SARS-CoV-2 spike protein
Yongfei Cai et al.
SCIENCE (2020)
Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability
Philip J. M. Brouwer et al.
SCIENCE (2020)
Broad neutralization of SARS-related viruses by human monoclonal antibodies
Anna Z. Wec et al.
SCIENCE (2020)
Structures and distributions of SARS-CoV-2 spike proteins on intact virions
Zunlong Ke et al.
NATURE (2020)
In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges
Beata Turonova et al.
SCIENCE (2020)
An ultrapotent synthetic nanobody neutralizes SARS-CoV-2 by stabilizing inactive Spike
Michael Schoof et al.
SCIENCE (2020)
Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2
Yufei Xiang et al.
SCIENCE (2020)
The protein complex crystallography beamline (BL19U1) at the Shanghai Synchrotron Radiation Facility
Wei-Zhe Zhang et al.
NUCLEAR SCIENCE AND TECHNIQUES (2019)
Nanobodies: Natural Single-Domain Antibodies
Serge Muyldermans
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 82 (2013)
MolProbity: all-atom structure validation for macromolecular crystallography
Vincent B. Chen et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2010)
Coot:: model-building tools for molecular graphics
P Emsley et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2004)
PHENIX:: building new software for automated crystallographic structure determination
PD Adams et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2002)