Bidyut Sarkar
Affiliations: | RIKEN |
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Parents
Sign in to add mentor| Sudipta Maiti | grad student | 2008-2014 | Tata Insitute of Fundamental Research |
| Tahei Tahara | post-doc | 2014-2021 | RIKEN |
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Publications
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| Dey A, Verma A, Bhaskar U, et al. (2024) A Toxicogenic Interaction between Intracellular Amyloid-β and Apolipoprotein-E. Acs Chemical Neuroscience |
| Safar M, Saurabh A, Sarkar B, et al. (2022) Single-photon smFRET. III. Application to pulsed illumination. Biophysical Reports. 2: 100088 |
| Sarkar B, Ishii K, Tahara T. (2021) Microsecond Folding of preQ Riboswitch and Its Biological Significance Revealed by Two-Dimensional Fluorescence Lifetime Correlation Spectroscopy. Journal of the American Chemical Society. 143: 7968-7978 |
| Sarkar B, Ishii K, Tahara T. (2019) Microsecond Conformational Dynamics of Biopolymers Revealed by Dynamic-Quenching Two-Dimensional Fluorescence Lifetime Correlation Spectroscopy with Single Dye Labeling. The Journal of Physical Chemistry Letters |
| Sarkar B, Ishii K, Tahara T. (2018) Microsecond Conformational Dynamics and Distinct Folding Mechanisms of PreQ1 Riboswitch Studied by Two-Dimensional Fluorescence Lifetime Correlation Spectroscopy Biophysical Journal. 114: 434a |
| Bera K, Das AK, Rakshit A, et al. (2017) Fluorogenic Detection of Monoamine Neurotransmitters in Live Cells. Acs Chemical Neuroscience |
| Chandrakesan M, Bhowmik D, Sarkar B, et al. (2015) Steric Crowding of the Turn Region Alters the Tertiary Fold of Amyloid-β18-35 and Makes it Soluble. The Journal of Biological Chemistry |
| Sarkar B, Mithu VS, Chandra B, et al. (2014) Significant structural differences between transient amyloid-β oligomers and less-toxic fibrils in regions known to harbor familial Alzheimer's mutations. Angewandte Chemie (International Ed. in English). 53: 6888-92 |
| Sarkar B, Banerjee A, Das AK, et al. (2014) Label-free dopamine imaging in live rat brain slices. Acs Chemical Neuroscience. 5: 329-34 |
| Mithu VS, Sarkar B, Bhowmik D, et al. (2014) Curcumin alters the salt bridge-containing turn region in amyloid β(1-42) aggregates. The Journal of Biological Chemistry. 289: 11122-31 |