Author

Srinivasaraghavan Kannan

Agency for Science, Technology and ResearchORCID 0000-0002-9539-5249Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Bioengineering· 1 Bioinformatics· 1

Signature Assays, Organisms & Methods

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Assay:protein structure· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1 Approach:experimental assay· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Approach:simulation· 1

Frequent Co-Authors

Chandra Shekhar VermaiD· 2 shared Abdurrahman AdamiD· 1 shared Alexander B. BaeriD· 1 shared Alexandre PoulhazaniD· 1 shared Ali MisereziD· 1 shared Ann‐Marie ChackoiD· 1 shared Barindra SanaiD· 1 shared Carel Min Jie TaniD· 1 shared

Activity by Year

2024-2025 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersBiochemistry

Chandra Shekhar VermaORCID

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3 papers

Recent·Most cited

In silico discovery of pathogenic PD-L1 nsSNVs with altered glycosylation and immunotherapy binding

Kai Wei Tan, Shruti Vijay Khare, Joanne Ong, Carel Min Jie Tan, Sven Hans Petersen, Srinivasaraghavan Kannan, Chandrabhan Verma, Ann‐Marie Chacko

The paper identifies pathogenic PD-L1 nsSNVs that alter glycosylation and ICI binding through bioinformatics and experimental methods.

bioRxiv · Jun 17, 2025 · PreprintBioinformatics

Receptor-based protein binding in the supramolecular network of velvet worm slime

Zhaolong Hu, Alexander B. Baer, Lars Hering, Ivo de Sena Oliveira, Alexandre Poulhazan, Darren C. Browne, Xue Guo, Quentin Moana Perrin, Radoslaw Mikolaj Sobota, Shawn S. Hoon, Georg Mayer, Srinivasaraghavan Kannan, Chandra Shekhar Verma, Matthew J. Harrington, Ali Miserez

This paper identifies evolutionarily conserved LRR proteins in velvet worm slime that form receptor-like structures, enabling reversible supramolecular network formation in bioadhesive fibers.

Proceedings of the National Academy of Sciences · Mar 18, 2025Peer-reviewedBiochemistry

Modulation of Ideonella sakaiensis PETase active site flexibility and activity on morphologically distinct substrates by surface charge engineering

Ke Ding, Zarina Levitskaya, Barindra Sana, Rupali Reddy Pasula, Srinivasaraghavan Kannan, Abdurrahman Adam, Sundaravadanam Vishnu Vadanan, Chandra Shekhar Verma, Sierin Lim, John F. Ghadessy

The paper investigates how surface charge mutations affect PETase activity on different PET substrates and identifies an engineered variant with improved degradation efficiency.

Biochemical Engineering Journal · Jul 2, 2024Peer-reviewedBioengineering