Identification, classification, and analysis of beta-bulges in proteins
10.1002/pro.5560021004 · doi-reference
Bat coronaviruses related to SARS-CoV-2 and infectious for human cells
10.1038/s41586-022-04532-4 · doi-reference
Expanded ACE2 dependencies of diverse SARS-like coronavirus receptor binding domains
10.1371/journal.pbio.3001738 · doi-reference
GISAID’s role in pandemic response
10.46234/ccdcw2021.255 · doi-reference
MolProbity: more and better reference data for improved all-atom structure validation
10.1002/pro.3330 · doi-reference
Improvement of cryo-EM maps by density modification
10.1038/s41592-020-0914-9 · doi-reference
Real-space refinement in PHENIX for cryo-EM and crystallography
10.1107/s2059798318006551 · doi-reference
Features and development of Coot
10.1107/s0907444910007493 · doi-reference
UCSF Chimera–a visualization system for exploratory research and analysis
10.1002/jcc.20084 · doi-reference
Accurate structure prediction of biomolecular interactions with AlphaFold 3
10.1038/s41586-024-07487-w · doi-reference
Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
10.1016/j.jmb.2003.07.013 · doi-reference
An image processing pipeline for electron cryo-tomography in RELION-5
10.1002/2211-5463.13873 · doi-reference
Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs
10.1038/s41592-019-0575-8 · doi-reference
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
10.1038/nmeth.4169 · doi-reference
SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM
10.1038/s42003-019-0437-z · doi-reference
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
10.1038/nmeth.4193 · doi-reference
A neutralizing epitope on the SD1 domain of SARS-CoV-2 spike targeted following infection and vaccination
10.1016/j.celrep.2022.111276 · doi-reference
Longitudinal observation and decline of neutralizing antibody responses in the three months following SARS-CoV-2 infection in humans
10.1038/s41564-020-00813-8 · doi-reference
Safety and immunogenicity of one versus two doses of the COVID-19 vaccine BNT162b2 for patients with cancer: interim analysis of a prospective observational study
10.1016/s1470-2045(21)00213-8 · doi-reference
Peripheral immunophenotypes in children with multisystem inflammatory syndrome associated with SARS-CoV-2 infection
10.1038/s41591-020-1054-6 · doi-reference
Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo
10.1038/nbt0997-871 · doi-reference
A time- and cost-efficient system for high-level protein production in mammalian cells
10.1107/s0907444906029799 · doi-reference
SARS-CoV-2 can recruit a heme metabolite to evade antibody immunity
10.1126/sciadv.abg7607 · doi-reference
Mosaic RBD nanoparticle elicits immunodominant antibody responses across sarbecoviruses
10.1016/j.celrep.2024.114235 · doi-reference
Structural determinants of spike infectivity in bat SARS-like coronaviruses RsSHC014 and WIV1
10.1128/jvi.00342-24 · doi-reference
Broad cross-reactivity across sarbecoviruses exhibited by a subset of COVID-19 donor-derived neutralizing antibodies
10.1016/j.celrep.2021.109760 · doi-reference
Mechanisms of SARS-CoV-2 entry into cells
10.1038/s41580-021-00418-x · doi-reference
Membrane-bound mRNA immunogens lower the threshold to activate HIV Env V2 apex-directed broadly neutralizing B cell precursors in humanized mice
10.1016/j.immuni.2022.09.003 · doi-reference
Human immunoglobulin repertoire analysis guides design of vaccine priming immunogens targeting HIV V2-apex broadly neutralizing antibody precursors
10.1016/j.immuni.2022.09.001 · doi-reference
Ontogeny-based immunogens for the induction of V2-directed HIV broadly neutralizing antibodies
10.1111/imr.12501 · doi-reference
Identification of common features in prototype broadly neutralizing antibodies to HIV envelope V2 apex to facilitate vaccine design
10.1016/j.immuni.2015.10.014 · doi-reference
Two classes of broadly neutralizing antibodies within a single lineage directed to the high-mannose patch of HIV envelope
10.1128/jvi.02905-14 · doi-reference
Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability
10.1126/science.abc5902 · doi-reference
Potent and broadly neutralizing antibodies against sarbecoviruses elicited by single ancestral SARS-CoV-2 infection
10.1038/s42003-025-07769-7 · doi-reference
Rational identification of potent and broad sarbecovirus-neutralizing antibody cocktails from SARS convalescents
10.1016/j.celrep.2022.111845 · doi-reference
Three SARS-CoV-2 antibodies provide broad and synergistic neutralization against variants of concern, including Omicron
10.1016/j.celrep.2022.110862 · doi-reference
Beyond neutralization: Fc-dependent antibody effector functions in SARS-CoV-2 infection
10.1038/s41577-022-00813-1 · doi-reference
