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Arnab Datta

Researcher at National Institutes of Health

Publications -  19
Citations -  1170

Arnab Datta is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Phosphorylation & Protein kinase A. The author has an hindex of 13, co-authored 19 publications receiving 987 citations. Previous affiliations of Arnab Datta include Yenepoya University & National University of Singapore.

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Hypoxic Tumor Cell Modulates Its Microenvironment to Enhance Angiogenic and Metastatic Potential by Secretion of Proteins and Exosomes

TL;DR: In this article, the authors observed that tumor cells produce a secretion that modifies their microenvironment to facilitate tumor angiogenesis and metastasis under hypoxia, and the secreted proteins were predominantly cytoplasmic and membrane proteins.
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Simultaneous Characterization of Glyco- and Phosphoproteomes of Mouse Brain Membrane Proteome with Electrostatic Repulsion Hydrophilic Interaction Chromatography

TL;DR: An optimized protocol using electrostatic repulsion hydrophilic interaction chromatography for the simultaneous enrichment of glyco- and phosphopeptides from mouse brain membrane protein digest is reported here to study the complex interaction of two different post-translational modifications in health and disease without being affected by interexperimental variations.
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SF3B1 Association with Chromatin Determines Splicing Outcomes

TL;DR: These findings suggest that the association of SF3B1 with nucleosomes is functionally important for splice-site recognition and that SF3 B1 conveys splicing-relevant information embedded in chromatin structure.
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Phenotyping of an in vitro model of ischemic penumbra by iTRAQ-based shotgun quantitative proteomics.

TL;DR: This study shows the potential application of iTRAQ-based quantitative proteomics for the elucidation of pathophysiology and the discovery of novel therapeutic targets in the field of neuroproteomics.
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Elucidating in Vivo Structural Dynamics in Integral Membrane Protein by Hydroxyl Radical Footprinting

TL;DR: The data showed the voltage gating of porin OmpF in vivo for the first time and supported the proposed mechanism that the local electrostatic field changes in the eyelet region may alter the porin channels to switch.