Author

S. K.-E. Gan

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 Microbiology· 1

Signature Assays, Organisms & Methods

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Assay:proteomics· 3 Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Approach:deep learning· 1 Assay:DNA methylation· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Organism:virus· 1

Frequent Co-Authors

J. Y. Yeo· 3 shared C. T.-T. Su· 1 shared D. W.-S. Koh· 1 shared F. Samsudin· 1 shared G.-R. Goh· 1 shared J.-J. Poh· 1 shared P. Bond· 1 shared P. Yap· 1 shared

Activity by Year

2019-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersImmunology

J. Y. Yeo

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Author profile →

3 papers

Recent·Most cited

Spontaneous Mutations in HIV-1 Gag, protease, RT p66 in the first replication cycle and how they appear: Insights from an in vitro BSL2 assay on mutation rates and types.

J. Y. Yeo, D. W.-S. Koh, P. Yap, G.-R. Goh, S. K.-E. Gan

This study investigates mutation rates and types in HIV-1 Gag, protease, and RT p66 genes in an in vitro system, revealing host deaminase contributions to mutations.

bioRxiv · Jul 27, 2020Microbiology

Molecular insight into Nickel(II) binding by Her2-specific IgE: a possible mechanistic insight into the pathogenesis of Type I nickel hypersensitivity

C. T.-T. Su, W.-H. Lua, J.-J. Poh, W.-L. Ling, J. Y. Yeo, S. K.-E. Gan

The paper investigates how Her2-specific IgE binds Nickel(II) and suggests this mechanism may explain Type I nickel hypersensitivity and its potential applications in therapeutics and biotechnology.

bioRxiv · Jul 14, 2020 · PreprintImmunology

The structural basis for distinct binding avidity of Pertuzumab and Trastuzumab IgM towards HER2

F. Samsudin, J. Y. Yeo, S. K.-E. Gan, P. Bond

This paper investigates the structural basis for the differing binding avidity of Pertuzumab and Trastuzumab IgM to HER2, showing that Pertuzumab IgM binds more effectively due to stable engagement via all V-regions.

bioRxiv · Jul 21, 2019 · PreprintImmunology