Author

X. F. Zhang

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 6 Immunology· 2 Bioengineering· 1

Signature Assays, Organisms & Methods

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Organism:human· 5 Research Focus:protein folding & dynamics· 5 Approach:statistical model· 5 Approach:experimental assay· 4 Assay:proteomics· 4 Approach:deep learning· 3 Research Focus:drug response / drug discovery· 3 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

S. Kim· 3 shared W. Im· 3 shared A. Jagota· 2 shared A. Oztekin· 2 shared C. Dong· 2 shared E. Webb· 2 shared F. J. Shen· 2 shared G. Z. Wu· 2 shared

Activity by Year

2018-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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3 shared papersBiophysics

S. Kim

Mutual co-authors in cluster

Author profile →

9 papers

Recent·Most cited

A mosaic-type trimeric RBD-based COVID-19 vaccine candidate induces potent neutralization against Omicron and other SARS-CoV-2 variants

J. Zhang, Z. B. Han, Y. Liang, X. F. Zhang, Y. Q. Jin, L. F. Du, S. Shao, H. Wang, J. W. Hou, K. Xu, Z. H. Lei, Z. M. Liu, J. Zhang, Y. N. Hou, N. Liu, , Q. M. Li

This study develops a mosaic-type trimeric RBD vaccine that induces strong neutralizing antibodies against Omicron and other SARS-CoV-2 variants in rats.

bioRxiv · Mar 29, 2022Immunology

Binding of Human ACE2 and RBD of Omicron Enhanced by Unique Interaction Patterns Among SARS-CoV-2 Variants of Concern

S. Kim, Y. Liu, M. Ziarnik, Y. Cao, X. F. Zhang, W. Im

This study quantifies how Omicron variant's RBD mutations enhance binding affinity to ACE2 compared to the original SARS-CoV-2 strain.

bioRxiv · Jan 24, 2022Biophysics

Differential Interactions Between Human ACE2 and Spike RBD of SARS-CoV-2 Variants of Concern

S. Kim, Y. Liu, Z. Lei, J. Dicker, Y. Cao, X. F. Zhang, W. Im

This study uses molecular dynamics and experiments to analyze how mutations in SARS-CoV-2 variants affect their binding to ACE2, identifying which variants are more contagious.

bioRxiv · Jul 23, 2021Biophysics

Structure and computation-guided design of a mutation-integrated trimeric RBD candidate vaccine with broad neutralization against SARS-CoV-2

Y. Liang, J. Zhang, R. Y. Yuan, M. Y. Wang, P. He, J. G. Su, Z. B. Han, Y. Q. Jin, J. W. Hou, H. Zhang, X. F. Zhang, S. Shao, Y. N. Hou, Z. M. Liu, L. F. Du, , Q. M. Li

This paper designs a trimeric RBD vaccine candidate with mutations from multiple SARS-CoV-2 strains, showing broad neutralization against variants including Beta and Kappa.

bioRxiv · Jun 18, 2021 · PreprintImmunology

Long time-scale study of von Willebrand factor multimers in extensional flow

E. Webb, S. Kania, A. Oztekin, X. Cheng, X. F. Zhang

This study uses WEBD simulations to analyze vWF multimer unfolding in extensional flow, showing that pathological unfolding is unlikely below 2000 s-1 strain rate.

bioRxiv · Sep 9, 2020 · PreprintBiophysics

Biomechanical Characterization of SARS-CoV-2 Spike RBD and Human ACE2 Protein-Protein Interaction

W. Cao, C. Dong, S. Kim, D. Hou, W. Tai, L. Du, W. Im, X. F. Zhang

This study quantifies the biophysical differences in SARS-CoV-2 and SARS-CoV-1 RBD-ACE2 interactions using single-molecule force spectroscopy and SMD simulations, revealing a key N-glycan interaction in SARS-CoV-2 that enhances binding affinity.

bioRxiv · Jul 31, 2020Biophysics

Length of Mucin-Like Domains Enhance Cell-Ebola Virus Adhesion by Increasing Binding Probability

X. Cui, N. Lapinski, X. F. Zhang, A. Jagota

This study models TIM-PS adhesion to show longer MLDs increase binding probability, enhancing Ebola virus adhesion through increased surface sampling.

bioRxiv · Jul 2, 2020Biophysics

Adhesive Contact Between Cylindrical (Ebola) and Spherical (SARS-CoV-2) Viral Particles and a Cell Membrane

J. Wang, N. Fortoul, X. F. Zhang, A. Jagota

This paper models adhesive interactions between cylindrical and spherical viral particles and a cell membrane, showing conditions under which adhesion occurs or is prevented without external force.

bioRxiv · Jun 26, 2020Bioengineering

Internal Tensile Force and A2 Domain Unfolding of von Willebrand Factor Multimers in Shear Flow

M. J. Morabito, C. Dong, W. Wei, X. F. Zhang, X. Cheng, A. Oztekin, E. Webb

This study uses simulations to show that A2 domain unfolding in vWF multimers under shear flow occurs preferentially near the center of unraveled multimers, with threshold shear rates inversely related to multimer length.

bioRxiv · May 2, 2018Biophysics