Selected publications from the Li Lab
Total citations: >38,000 (Google Scholar; as of December 2025)
Highly cited publications: Five publications, on which Dr. Li is the primary author (first or last author), have each received >2,000 citations (four > 3,000 each). These publications are linked below to Google Scholar.
Authorship note: Dr. Li is the primary author (first or last author) on all publications listed below.
Featured publications
Coronaviruses
Structural basis of receptor recognition by SARS-CoV-2.
Shang, J. et al., Nature, 2020, [PDF], [Web], [PubMed], [Google Scholar], [News1], [News2]
Structure of SARS coronavirus spike receptor-binding domain complexed with receptor.
Li, F. et al., Science, 2005, [PDF], [Web], [PubMed], [Google Scholar], [News]
Cell entry mechanisms of SARS-CoV-2.
Shang, J. et al., PNAS, 2020, [PDF], [Web], [PubMed], [Google Scholar], [News]
Receptor recognition by the novel coronavirus from Wuhan: an analysis based on decade-Long structural studies of SARS coronavirus.
Wan, Y. et al., Journal of Virology, 2020, [PDF], [Web], [PubMed], [Google Scholar], [News]
- Most cited in journal history (Crossref, 2026)
Structure, function, and evolution of coronavirus spike proteins.
Li, F., Annual Review of Virology, 2016, [PDF], [Web], [PubMed], [Google Scholar]
- Most cited in journal history (Crossref, 2026)
Filoviruses
Structures of Marburgvirus glycoprotein and its complex with NPC1 receptor.
Ye, G. et al., Nature, 2026, [PDF], [Web], [Pubmed], [News1], [News2]
Other research areas
Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP.
Li, F. et al., Cell, 2002, [PDF], [Web], [PubMed]
Representative publications
SARS-CoV-2 and SARS-CoV-1: mechanisms
Structural basis for mouse receptor recognition by SARS-CoV-2 omicron variant.
Zhang, W. et al., PNAS, 2022, [PDF], [Web], [PubMed], [News]
Structural basis for mouse receptor recognition by bat SARS2-like coronaviruses.
Zhang, W. et al., PNAS, 2024, [PDF], [Web], [PubMed]
Structural basis for bat receptor recognition by SARS-CoV-2 and bat SARS2-like coronaviruses.
Hsueh, FC. et al., Communications Biology, 2026, [PDF], [Web], [PubMed]
Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain.
Ye, G. et al., Nature Communications, 2022, [PDF], [Web], [PubMed], [News]
Lys417 acts as a molecular switch that regulates the conformation of SARS-CoV-2 spike protein.
Geng, Q. et al., eLife, 2023, [PDF], [Web], [PubMed], [News]
Structural analysis of major species barriers between humans and palm civets for severe acute respiratory syndrome coronavirus infections.
Li, F., Journal of Virology, 2008, [PDF], [Web], [PubMed]
Conformational states of the severe acute respiratory syndrome coronavirus spike protein ectodomain.
Li, F. et al., Journal of Virology, 2006, [PDF], [Web], [PubMed]
Non-SARS coronaviruses: mechanisms
Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor.
Wu, K. et al., PNAS, 2009, [PDF], [Web], [PubMed]
Crystal structure of mouse coronavirus receptor-binding domain complexed with its murine receptor.
Peng, G. et al., PNAS, 2011, [PDF], [Web], [PubMed]
Receptor usage and cell entry of bat coronavirus HKU4 provide insight into bat-to-human transmission of MERS coronavirus.
Yang, Y. et al., PNAS, 2014, [PDF], [Web], [PubMed]
Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.
Shang, J. et al., PLOS Pathogens, 2020, [PDF], [Web], [PubMed]
Cryo-EM structure of infectious bronchitis coronavirus spike protein reveals structural and functional evolution of coronavirus spike proteins.
Shang, J. et al., PLOS Pathogens, 2018, [PDF], [Web], [PubMed]
Molecular mechanism for antibody-dependent enhancement of coronavirus entry.
Wan, Y. et al., Journal of Virology, 2020, [PDF], [Web], [PubMed]
Receptor recognition mechanisms of coronaviruses: a decade of structural studies.
Li, F., Journal of Virology, 2015, [PDF], [Web], [PubMed]
Coronaviruses: interventions
Discovery of Nanosota-9 as anti-Omicron nanobody therapeutic candidate.
Ye, G. et al., PLOS Pathogens, 2024, [PDF], [Web], [PubMed], [News]
Dual-role epitope on SARS-CoV-2 spike enhances and neutralizes viral entry across different variants.
Ye, G. et al., PLOS Pathogens, 2024, [PDF], [Web], [PubMed], [News]
Discovery of Nanosota-2, -3, and -4 as super potent and broad-spectrum therapeutic nanobody candidates against COVID-19.
Ye, G. et al., Journal of Virology, 2023, [PDF], [Web], [PubMed]
The Development of Nanosota-1 as anti-SARS-CoV-2 nanobody drug candidates.
Ye, G. et al., eLife, 2021, [PDF], [Web], [PubMed], [News]
Introduction of neutralizing immunogenicity index to the rational design of MERS coronavirus subunit vaccines.
Du, L. et al., Nature Communications, 2016, [PDF], [Web], [PubMed]
Novel virus-like nanoparticle vaccine effectively protects animal model from SARS-CoV-2 infection.
Geng, Q. et al., PLOS Pathogens, 2021, [PDF], [Web], [PubMed], [News]
Filoviruses: mechanisms and interventions
A highly potent and broadly accessible bispecific nanobody for the treatment of ebola virus infections.
Bu, F. et al., PLOS Pathogens, 2026, [PDF], [Web], [PubMed]
Discovery of Nanosota-EB1 and -EB2 as Novel Nanobody Inhibitors Against Ebola Virus Infection.
Bu, F. et al., PLOS Pathogens, 2024, [PDF], [Web], [PubMed], [News]
Cryo-EM structure of Sudan ebolavirus glycoprotein complexed with its human endosomal receptor NPC1.
Bu, F. et al., Communications Biology, 2025, [PDF], [Web], [PubMed], [News]
Cancer and hypertension: mechanisms and interventions
Structural basis for multifunctional roles of mammalian aminopeptidase N.
Chen, L. et al., PNAS, 2012, [PDF], [Web], [PubMed]
A unified mechanism for aminopeptidase N-based tumor cell motility and tumor-homing therapy.
Liu, C. et al., Journal of Biological Chemistry, 2014, [PDF], [Web], [PubMed]
Structural insights into central hypertension regulation by human aminopeptidase A.
Yang, Y. et al. Journal of Biological Chemistry, 2013, [PDF], [Web], [PubMed]
Structural biology methods
Update and Reuse: Structure-Guided Nanobody Evolution Against SARS-CoV-2 Escape.
Bu, F. et al., PLOS Pathogens, 2026, [PDF], [Web], [Pubmed]
Structure-guided in vitro evolution of nanobodies targeting new viral variants.
Ye, G. et al., PLOS Pathogens, 2024, [PDF], [Web], [PubMed], [News]
Cross-crystal averaging with search models to improve molecular replacement phases.
Li, W., Li, F. Structure, 2011, [PDF], [Web], [PubMed]