Author

C.-W. Kuo

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 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 3 Assay:proteomics· 3 Organism:human· 2 Research Focus:cancer & tumor microenvironment· 1 Assay:structural biology· 1 Organism:virus· 1

Frequent Co-Authors

K.-H. Khoo· 4 shared P.-Y. Yu· 2 shared S.-T. D. Hsu· 2 shared T.-J. Yang· 2 shared A. Bhattacherjee· 1 shared C. D. St. Laurent· 1 shared D. T. Bui· 1 shared E. Rodrigues· 1 shared

Activity by Year

2021-2021 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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4 shared papersBiochemistry

K.-H. Khoo

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Cancer malignancy is correlated with up-regulation of PCYT2-mediated glycerol phosphate modification of α-dystroglycan

F. Umezawa, M. Natsume, S. Fukusada, K. Nakajima, F. Yamasaki, H. Kawashima, C.-W. Kuo, K.-H. Khoo, T. Shimura, H. Yagi, K. Kato

This study shows that PCYT2-mediated glycerol phosphate modification of α-dystroglycan correlates with cancer progression and promotes cell migration in colorectal cancer.

bioRxiv · Oct 25, 2021 · PreprintBiochemistry

Carbohydrate sulfation as a mechanism for fine-tuning Siglec ligands

J. Jung, J. R. Enterina, D. T. Bui, F. Mozaneh, P.-H. Lin, H. Nitin, C.-W. Kuo, E. Rodrigues, A. Bhattacherjee, P. Raeisimakiani, G. C. Daskhan, C. D. St. Laurent, K.-H. Khoo, L. K. Mahal, W. F. Zandberg, , M. S. Macauley

This study shows that specific sulfate modifications on Siglec ligands, mediated by CHSTs, can enhance or reduce Siglec binding, with implications for cancer immune evasion.

ACS Chemical Biology · Oct 18, 2021Peer-reviewedImmunology

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

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