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Srinivasaraghavan Kannan on Muck Rack

Srinivasaraghavan Kannan

As seen in: Nature, MDPI, Science Magazine, BioRxiv, Cancer Discovery, The Journal of Biological Chemistry
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Articles

Genomic landscape of drug binding and pharmacogenetic variation across diverse populations using SNPdrug3D

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By Ashar Malik, Dimitar Kenanov, Cheng-Shoong Chong, Mert Öztürk, Qiqi Wang, Maxime Hebrard, Ying Swan Ho, Zhenxun Wang, Srinivasaraghavan Kannan, Roberto Magallanes, Xueling Sim, Jin Chai, Sonia Davila, Khung Keong Yeo, Khai Pang Leong, Liuh Ling Goh, Neerja Karnani, Johan Eriksson, Ching-Yu Cheng, Marie Loh, Rinkoo Dalan, Chiea Chuen Khor, Guo-Liang Chew, Weng Khong Lim, Joanne Ngeow, John Chambers, E. Shyong Tai, Nicolas Bertin, Patrick Tan, Chandra Verma, Sebastian Maurer-Stroh, Hong-Yun Chang, Vachiranee Limviphuvadh, Jhoann M. T. Miyajima, Judice Koh
| Nature Verified
Abstract One of the promises of precision medicine is to understand and act on inter-individual genetic differences in drug responses. SNPdrug3D contains the complete genomic landscape of missense single nucleotide variants (SNV) across the human proteome and at a population-wide level that could affect drug binding.
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TP53 mutation at codon 179 metabolically reprograms cancer cells to promote invasion

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By Debina Sarkar, Aaron Jeffs, Adele G. Woolley, Selena Wang, Maryam Sardari, Apeksha Arun Bhandarkar, Halima Siddiqui, Magdalena Ratajska, Makhdoom Sarwar, Srinivasaraghavan Kannan, Chandra Verma, Catherine J. Drummond, Cushla McKinney, Jisha Antony, Antony W. Braithwaite, Sunali Mehta, Gaurav C. Gyanwali, Jaishree Patel, Polina Shevchuk, Sally P. McCormick
| Nature Verified
Abstract Mutations in the tumour suppressor, TP53, are prevalent in human cancers yet their functional implications remain unclear. Through comprehensive pan-cancer database analysis, we identified H179 mutations in TP53 as significantly associated with poor disease-free survival across multiple cancer types.
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Design-rules for stapled peptides with in vivo activity and their application to Mdm2/X antagonists - Nature Communications

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By Diana Spiegelberg, Chandra Verma, Brian Henry, Srinivasaraghavan Kannan, Charles W. Johannes, Pietro G. Aronica, Marika Nestor
| Nature Verified
Abstract Although stapled α-helical peptides can address challenging targets, their advancement is impeded by poor understandings for making them cell permeable while avoiding off-target toxicities. By synthesizing >350 molecules, we present workflows for identifying stapled peptides against Mdm2(X) with in vivo activity and no off-target effects.
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