S
Saikat Bhattacharya
Researcher at Stowers Institute for Medical Research
Publications - 26
Citations - 147
Saikat Bhattacharya is an academic researcher from Stowers Institute for Medical Research. The author has contributed to research in topics: Histone & Chromatin. The author has an hindex of 5, co-authored 22 publications receiving 72 citations. Previous affiliations of Saikat Bhattacharya include Homi Bhabha National Institute & Tata Memorial Hospital.
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Journal ArticleDOI
The methyltransferase SETD2 couples transcription and splicing by engaging mRNA processing factors through its SHI domain.
Saikat Bhattacharya,Michaella J. Levy,Ning Zhang,Hua Li,Laurence Florens,Michael P. Washburn,Jerry L. Workman +6 more
TL;DR: In this article, the histone methyltransferase SETD2 interacts with hnRNP L in vitro and in vivo to regulate alternative splicing (AS) by binding to pre-mRNA transcripts.
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Dynamic alteration in H3 serine 10 phosphorylation is G1-phase specific during ionization radiation induced DNA damage response in human cells.
TL;DR: It is proposed that the drop in the levels of histone H3S10 phosphorylation is a universal phenomenon in response to DNA damage and is a trigger to induce transcription repressive state to facilitate repair.
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Histone isoform H2A1H promotes attainment of distinct physiological states by altering chromatin dynamics
Saikat Bhattacharya,Saikat Bhattacharya,Divya Reddy,Vinod Jani,Nikhil Gadewal,Sanket Shah,Raja Reddy,Kakoli Bose,Uddhavesh Sonavane,Rajendra Joshi,Sanjay Gupta +10 more
TL;DR: Insight is provided into the molecular basis of the non-redundancy of the histone H2A isoforms that are being increasingly reported to be functionally important in varied physiological contexts, suggesting that the nucleosome stability is intimately linked with the physiological effects observed.
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Regulation of SETD2 stability is important for the fidelity of H3K36me3 deposition
TL;DR: It is shown that the poorly characterized N-terminal region of SETD2 plays a determining role in regulating the stability ofSETD2 and leads to a marked increase in global H3K36me3 which, uncharacteristically, happens in a Pol II-independent manner.
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Brief Communication: Featured Article: Histone H2A mono-ubiquitination and cellular transformation are inversely related in N-nitrosodiethylamine-induced hepatocellular carcinoma.
TL;DR: This work for the first time suggests the in vivo association of H3S10p, H4ac, and H2A119ub with cellular transformation and shows that treatment of cells with histone deacetylase inhibitor trichostatin A results in increase of H1Aub and decrease in H3s10p.