Author

K.-H. Liang

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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Immunology· 2 Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 3 Research Focus:drug response / drug discovery· 2 Organism:mouse· 2 Assay:proteomics· 2 Organism:virus· 2 Assay:cryo-EM· 1 Assay:structural biology· 1

Frequent Co-Authors

H.-C. Wu· 4 shared F.-F. Hsu· 2 shared H.-T. Lin· 2 shared M. Kumari· 2 shared P.-Y. Yu· 2 shared S.-T. D. Hsu· 2 shared T.-J. Yang· 2 shared W.-Y. Chen· 2 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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4 shared papersImmunology

H.-C. Wu

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

An Efficient Approach for SARS-CoV-2 Monoclonal Antibody Production via Modified mRNA-LNP Immunization

F.-F. Hsu, K.-H. Liang, M. Kumari, W. Y. Chen, H. T. Lin, C. M. Cheng, M.-H. Tao, H.-C. Wu

This study combines mRNA-LNP immunization with hybridoma fusion to produce SARS-CoV-2 monoclonal antibodies, showing improved antibody titers and cross-variant neutralization.

bioRxiv · Apr 20, 2022Immunology

Broadly neutralizing antibodies against Omicron variants of SARS-CoV-2 derived from mRNA-lipid nanoparticle-immunized mice

R.-M. Lu, K.-H. Liang, H.-L. Chiang, F.-F. Hsu, H.-T. Lin, W.-Y. Chen, F.-Y. Ke, M. Kumari, Y.-C. Chou, H.-C. Wu

This paper develops broadly neutralizing antibodies against Omicron variants of SARS-CoV-2 using mRNA-lipid nanoparticle immunization in mice, showing effectiveness against multiple variants.

bioRxiv · Apr 19, 2022Immunology

Structure-activity relationships of B.1.617 and other SARS-CoV-2 spike variants

T.-J. Yang, P.-Y. Yu, Y.-C. Chang, N.-E. Chang, Y.-X. Tsai, K.-H. Liang, P. Draczkowski, B. Lin, Y.-S. Wang, Y.-C. Chien, K.-H. Khoo, H.-C. Wu, S.-T. D. Hsu

This study reports cryo-EM structures of SARS-CoV-2 spike variants and finds mutations alter conformation and glycan shield, enhance ACE2 binding, but are neutralized by three antibodies.

bioRxiv · Sep 12, 2021 · PreprintBiophysics

Impacts on the structure-function relationship of SARS-CoV-2 spike by B.1.1.7 mutations

T.-J. Yang, P.-Y. Yu, Y.-C. Chang, K.-H. Liang, H.-C. Tso, M.-R. Ho, W.-Y. Chen, H.-T. Lin, H.-C. Wu, S.-T. D. Hsu

This study examines how B.1.1.7 mutations affect the structure and function of SARS-CoV-2 spike protein, showing changes in receptor binding and antibody neutralization.

bioRxiv · May 11, 2021 · PreprintBiochemistry