Author

A. Bhattacherjee

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 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 3 Organism:human· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Organism:mouse· 1 Assay:proteomics· 1

Frequent Co-Authors

C. D. St. Laurent· 2 shared M. S. Macauley· 2 shared A. Bains· 1 shared A. E. S. Watson· 1 shared A. Voronova· 1 shared C.-W. Kuo· 1 shared D. T. Bui· 1 shared E. Rodrigues· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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2 shared papersImmunology

C. D. St. Laurent

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Author profile →

3 papers

Recent·Most cited

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

Increasing phagocytosis of microglia through targeting CD33 with liposomes displaying glycan ligands

A. Bhattacherjee, G. Daskhan, A. Bains, A. E. S. Watson, G. Eskandari-Sedighi, C. D. St. Laurent, A. Voronova, M. S. Macauley

This study shows that CD33L liposomes enhance microglia phagocytosis by multivalently engaging CD33, with effects dependent on CD33's glycan-binding and signaling properties.

bioRxiv · May 8, 2021Immunology

Interaction of 14-3-3I and CDPK1 mediates the growth of human malaria parasite

R. Jain, P. Dey, S. Gupta, S. Pati, A. Bhattacherjee, M. Munde, S. Singh

This study identifies 14-3-3I as a scaffold protein in Plasmodium falciparum and reveals its interaction with CDPK1, a key kinase, through phosphorylation-dependent binding, suggesting a potential target for antimalarial drug development.

bioRxiv · Jan 14, 2020 · PreprintCell Biology