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Avik Biswas on Muck Rack

Avik Biswas

Southern Asia
As seen in: Nature, MDPI, Science Magazine, BioRxiv, Lexology, Mondaq, The Journal of Biological Chemistry, People Matters, Legal Era Online
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Articles

The RNA-binding protein hnRNP E1 regulates p53 and p21 translation via KH1 and KH2 domain interactions with 3′ UTR C-rich motifs

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By Sandipan Mukherjee, Avik Biswas, Abhisekh Samanta, Arpita Kar
| The Journal of Biological Chemistry Verified
Keywords hnRNP E1 KH domains p53 p21 3’UTR protein-RNA interaction Abbreviations EMT (Epithelial-to-mesenchymal transition) KH (K-homology) NLS (Nuclear localization signal) RBP (RNA-binding proteins) RIP (RNA immuno-precipitation) RRM (RNA recognition motif) Introduction Dynamic alterations in the post-transcriptional regulation of various transcript species are a characteristic feature of numerous human diseases, including cancer (1, 2).
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Using phage display for rational engineering of a higher-affinity humanized 3’ phosphohistidine-specific antibody - Communications Chemistry

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By Gianluca Veggiani, Margaux Sala, Avik Biswas, Ronald Levy, Dmitry Lyumkis, Ian Wilson, Tony Hunter
| Nature Verified
Abstract Histidine phosphorylation is a non-canonical post-translational modification (PTM), with 1-phosphohistidine (1-pHis) and 3-phosphohistidine (3-pHis) isoforms, that is understudied due to a lack of robust reagents, including high-affinity pHis-specific antibodies. Engineering pHis antibodies is challenging due to the labile nature of its phosphoramidate (P-N) bond.
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Oligomeric HIV-1 integrase structures reveal functional plasticity for intasome assembly and RNA binding - Nature Communications

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By Tao Jing, Zelin Shan, Tung Dinh, Avik Biswas, Dario O. Passos, Sriram Aiyer, Leonardo Andrade, Yuxuan Zhang, Alan N. Engelman, Mamuka Kvaratskhelia
| Nature Verified
Abstract Integrase (IN) performs dual essential roles during HIV-1 replication. During ingress, IN functions within an oligomeric “intasome” assembly to catalyze viral DNA integration into host chromatin. During late stages of infection, tetrameric IN binds viral RNA and orchestrates the condensation of ribonucleoprotein complexes into the capsid core. The molecular architectures of HIV-1 IN assemblies that mediate these distinct events remain unknown.
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