Author

P.-Y. Yu

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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Biochemistry· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

S.-T. D. Hsu· 4 shared T.-J. Yang· 4 shared K.-H. Khoo· 3 shared Y.-C. Chang· 3 shared C.-W. Kuo· 2 shared H.-C. Wu· 2 shared K.-H. Liang· 2 shared Y.-C. Chien· 2 shared

Activity by Year

2021-2021 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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4 shared papersBiochemistry

S.-T. D. Hsu

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

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

Distinct shifts in site-specific glycosylation pattern of SARS-CoV-2 spike proteins associated with arising mutations in the D614G and Alpha variants

C.-W. Kuo, T.-J. Yang, Y.-C. Chien, P.-Y. Yu, S.-T. D. Hsu, K.-H. Khoo

The paper analyzes site-specific glycosylation changes in SARS-CoV-2 spike proteins of D614G and Alpha variants, revealing altered N-glycan processing and potential impacts on transmissibility.

bioRxiv · Jul 21, 2021Biochemistry

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

COVID-19 dominant D614G mutation in the SARS-CoV-2 spike protein desensitizes its temperature-dependent denaturation

T.-J. Yang, P.-Y. Yu, Y.-C. Chang, C.-W. Kuo, K.-H. Khoo, S.-T. D. Hsu

The paper shows the D614G mutation in SARS-CoV-2 spike protein increases thermal stability and reduces cold-induced unfolding, enhancing viral infectivity.

bioRxiv · Mar 28, 2021Biochemistry