Amal Kanti Bera

ORCID: 0000-0003-0362-5578
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About
Contact & Profiles
Research Areas
  • Ion channel regulation and function
  • Receptor Mechanisms and Signaling
  • Ion Transport and Channel Regulation
  • Connexins and lens biology
  • Neuroscience and Neuropharmacology Research
  • Nicotinic Acetylcholine Receptors Study
  • Neuroscience of respiration and sleep
  • Mitochondrial Function and Pathology
  • Lipid Membrane Structure and Behavior
  • Hormonal Regulation and Hypertension
  • Molecular Sensors and Ion Detection
  • MicroRNA in disease regulation
  • Fatty Acid Research and Health
  • Alzheimer's disease research and treatments
  • Nitric Oxide and Endothelin Effects
  • Protein Kinase Regulation and GTPase Signaling
  • Biochemical effects in animals
  • Cardiac electrophysiology and arrhythmias
  • Cancer-related molecular mechanisms research
  • Antimicrobial Peptides and Activities
  • Crystallization and Solubility Studies
  • X-ray Diffraction in Crystallography
  • Biochemical Analysis and Sensing Techniques
  • Ion Channels and Receptors
  • Neuropeptides and Animal Physiology

Indian Institute of Technology Madras
2015-2024

University of Würzburg
2017

University B.T. & Evening College
2017

Indian Institute of Technology Indore
2016

Indian Institute of Technology Dhanbad
2007

Yeshiva University
2005

Stahl-Zentrum (Germany)
2005

Albert Einstein College of Medicine
2002-2005

Tel Aviv University
2000-2001

The University of Texas Southwestern Medical Center
2000-2001

Artificial anion selective ion channels with single-file multiple anion-recognition sites are rare. Here, we have designed, by hypothesis, a small molecule that self-organizes to form barrel rosette channel in the lipid membrane environment. Being amphiphilic nature, this forms nanotubes through intermolecular hydrogen bond formation, while its hydrophobic counterpart is stabilized interactions membrane. The selectivity of was investigated fluorescence-based vesicle assay and planar bilayer...

10.1021/ja506278z article EN Journal of the American Chemical Society 2014-09-23

Stable expression of pannexin 1 (Panx1) and 3 (Panx3) resulted in functional gap junctions (GJs) HeLa cells, but not Neuro-2a (N2a) or PC-12 cells. The glycosylation pattern expressed Panx1 varied greatly among different cell lines. In contrast to connexin (Cx) containing GJs (Cx-GJs), junctional conductance (Gj) (Panx-GJs) is very less sensitive voltage. Both Panx3 favoured anionic dyes over cations permeate. Though, carbenoxolone (CBX) probenecid blocked hemichannel activity, they had no...

10.1038/srep04955 article EN cc-by-nc-nd Scientific Reports 2014-05-14

Many neurodegenerative diseases, such as Alzheimer's disease (AD) and frontotemporal dementia with Parkinsonism linked to chromosome 17, are characterized by tau pathology. Numerous motor proteins, many of which involved in synaptic transmission, mediate transport neurons. Dysfunction protein-mediated neuronal mechanisms occurs several disorders but remains understudied AD. Kinesins the most important molecular proteins required for microtubule-dependent neurons, kinesin-1 is crucial among...

10.3389/fmolb.2022.1050768 article EN cc-by Frontiers in Molecular Biosciences 2022-10-25

The γ-aminobutyric acid type A (GABA<sub>A</sub>) receptor M2–M3 loop structure and its role in gating were investigated using the substituted cysteine accessibility method. Residues from α<sub>1</sub>Arg-273 to α<sub>1</sub>Ile-289 mutated cysteine, one at a time. MTSET<sup>+</sup> or MTSES<sup>−</sup> reacted with all mutants α<sub>1</sub>R273C α<sub>1</sub>Y281C, except α<sub>1</sub>P277C, absence presence of GABA. closed-state reaction rate was >1000 liters/mol-s α<sub>1</sub>N274C,...

10.1074/jbc.m206321200 article EN cc-by Journal of Biological Chemistry 2002-11-01

10.1006/bbrc.1995.1491 article EN Biochemical and Biophysical Research Communications 1995-04-01

Aspirin induces apoptotic cell death in various cancer lines. Here we showed that silencing of VDAC1 protected HeLa cells from aspirin-induced death. Compared to the wild type cells, knocked down lesser change mitochondrial membrane potential (Δψm), upon aspirin treatment. augmented ATP and ionomycin-induced Ca2+ uptake which was abolished cells. dissociated bound hexokinase II (HK-II) mitochondria. Further, promoted closure recombinant human VDAC1, reconstituted planar lipid bilayer. Taken...

10.1038/srep45184 article EN cc-by Scientific Reports 2017-03-22

To investigate possible effects of adrenergic stimulation on G protein–activated inwardly rectifying K+ channels (GIRK), acetylcholine (ACh)-evoked current, IKACh, was recorded from adult rat atrial cardiomyocytes using the whole cell patch clamp method and a fast perfusion system. The rise time IKACh 0.4 ± 0.1 s. When isoproterenol (Iso) applied simultaneously with ACh, an additional slow component (11.4 3.0 s) appeared, amplitude elicited increased by 22.9 5.4%. Both activation current...

10.1085/jgp.115.5.547 article EN The Journal of General Physiology 2000-05-01

ABSTRACT Leucine-rich repeat-containing 8 (LRRC8) proteins have been proposed to evolutionarily originate from the combination of channel protein pannexin, and a leucine-rich repeat (LRR) domain. Five paralogs LRRC8, namely LRRC8A, LRRC8B, LRRC8C, LRRC8D LRRC8E reported. LRRC8A has shown be instrumental in cell swelling. Here, we identify LRRC8B as key player cellular Ca2+ signaling network. Overexpression human HEK293 cells reduced level endoplasmic reticulum (ER). LRRC8B-overexpressing...

10.1242/jcs.203646 article EN Journal of Cell Science 2017-11-15

G protein-activated K+ channel (GIRK), which is activated by the Gβγ subunit of heterotrimeric proteins, and muscarinic m2 receptor (m2R) were coexpressed in Xenopus oocytes. Acetylcholine evoked a current, I ACh, via endogenous pertussis toxin (PTX)-sensitive Gi/o proteins. Activation ACh was accelerated increasing expression m2R, suggesting collision coupling mechanism one catalytically activates several Coexpression α PTX-insensitive protein Gz, Gαz, induced slowly activating whose...

10.1074/jbc.275.6.4166 article EN cc-by Journal of Biological Chemistry 2000-02-01

Catestatin (CST), a chromogranin A-derived peptide, is potent endogenous inhibitor of the neuronal nicotinic acetylcholine receptor (nAChR). It exerts anti-hypertensive effect by acting as “physiological brake” on transmitter release into circulation. However, mechanism interaction CST with nAChR only partially understood. To unravel molecular interactions common/wild type human (CST-WT) well its naturally-occurring variants (viz. CST-364S and CST-370L having Gly→Ser Pro→Leu substitutions,...

10.1242/jcs.103176 article EN Journal of Cell Science 2012-01-01

Essentials•Mechanism of thrombin–induced inflammation is not fully understood.•Thrombin induced monocyte adhesion and barrier loss require Angiopoietin‐2 (Ang‐2).•Ang‐2 mediates vessel leakage through SHP‐2/p38MAPK pathway.•Calcium dependent SHP2/p38MAPK activation regulates Ang‐2 expression a feedback loop.Summary: BackgroundThrombin imparts an inflammatory phenotype to the endothelium by promoting increased vascular permeability. However, molecular players that govern these events are...

10.1111/jth.13376 article EN publisher-specific-oa Journal of Thrombosis and Haemostasis 2016-05-31

Catestatin (CST), a chromogranin A (CHGA)-derived peptide, is potent inhibitor of catecholamine release from adrenal chromaffin cells and postganglionic sympathetic axons. We re-sequenced the CST region CHGA in an Indian population (n = 1010) detected two amino acid substitution variants: G364S G367V. Synthesized variant peptides (viz. CST-Ser-364 CST-Val-367) were significantly less than wild type peptide (CST-WT) to inhibit nicotine-stimulated secretion PC12 cells. Consistently, rank-order...

10.1074/jbc.m112.407916 article EN cc-by Journal of Biological Chemistry 2012-10-29
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