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Amal Kanti Bera
Researcher at Indian Institute of Technology Madras
Publications - 58
Citations - 1357
Amal Kanti Bera is an academic researcher from Indian Institute of Technology Madras. The author has contributed to research in topics: G protein-coupled inwardly-rectifying potassium channel & Pannexin. The author has an hindex of 20, co-authored 50 publications receiving 1139 citations. Previous affiliations of Amal Kanti Bera include Albert Einstein College of Medicine & Tel Aviv University.
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GABAA Receptor M2–M3 Loop Secondary Structure and Changes in Accessibility during Channel Gating
TL;DR: The γ-aminobutyric acid type A receptor M2–M3 loop structure and its role in gating were investigated using the substituted cysteine accessibility method and it is suggested that the M2 segment α-helix extends beyond the predicted extracellular end of the M1 segment and that gating induces a conformational change in and/or around the N-terminal half of the GABAA loop.
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RGS Proteins Provide Biochemical Control of Agonist-Evoked [Ca2+]i Oscillations
TL;DR: It is proposed that RGS proteins within the G protein-coupled receptor complexes provide a biochemical control of [Ca2+]i oscillations.
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Hopping-mediated anion transport through a mannitol-based rosette ion channel.
Tanmoy Saha,Sathish Dasari,Debanjan Tewari,Annamalai Prathap,Kana M. Sureshan,Amal Kanti Bera,Arnab Mukherjee,Pinaki Talukdar +7 more
TL;DR: A small molecule that self-organizes to form a barrel rosette ion channel in the lipid membrane environment is designed, by hypothesis, being amphiphilic in nature, which forms nanotubes through intermolecular hydrogen bond formation, while its hydrophobic counterpart is stabilized by hydrophilic interactions in the membrane.
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Mitochondrial VDAC Can Be Phosphorylated by Cyclic AMP-Dependent Protein Kinase
TL;DR: It is demonstrated that VDAC purified from rat liver mitochondria can be phosphorylated by the catalytic subunit of cAMP dependent protein kinase (PKA).
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P2X7 receptor-pannexin 1 hemichannel association: effect of extracellular calcium on membrane permeabilization.
V. Poornima,M. Madhupriya,M. Madhupriya,Scherazad Kootar,G. Sujatha,Arvind Kumar,Amal Kanti Bera +6 more
TL;DR: It is hypothesized that extracellular calcium ([Ca2+]o) plays an important role in the coupling of P2X7R–panx1 and subsequent membrane permeabilization and activation and association, triggered by the removal of [Ca2+.