Search

Byline: M. Bhar, S. Khargharia, A. Chakraborty, T. Mandal Objective: To study the variation of disposition kinetic values of sparfloxacin in healthy, hepatopathic, and nephropathic chickens after a single intravenous [...]

Byline: M. Bhar, S. Das, A. Chakraborty, T. Mandal, S. Roy Enliv ® is a poly-herbal formulation that exists in a powder form. It contains the aqueous extract of eight [...]

The ubiquitous manufacturing of lithium-ion batteries (LIBs) due to high consumer demand produces inevitable e-waste that imposes severe environmental and resource sustainability challenges. In this work, the charge storage capability and Li-ion kinetics of the recovered water-leached graphite (WG) anode from spent LIBs are enhanced by using an optimized amount of recycled graphene nanoflakes (GNFs) as an additive. The WG@GNF anode exhibits an initial discharge capacity of 400 mAh g -1 at 0.5C with 88.5% capacity retention over 300 cycles. Besides, it delivers an average discharge capacity of 320 mAh g -1 at 500 mA g -1 over 1000 cycles, which is 1.5-2 times higher than that of WG. The sharp increase in electrochemical performance is due to the synergistic effects of Li-ion intercalation into the graphite layers and Li-ion adsorption into the surface functionalities of GNF. Density functional theory calculations reveal the role of functionalization behind the superior voltage profile of WG@GNF. Besides, the unique morphology of spherical graphite particles trapping into graphene nanoflakes provides mechanical stability over long-term cycling. This work explains an efficient strategy to upgrade the electrochemical compatibility of recovered graphite anode from spent LIBs toward next-generation high-energy-density LIBs.

Scd6 is a conserved RGG-motif protein which represses translation by binding eIF4G through its RGG-motif. Lsm and FDF are two other conserved domains present in the protein, however the role of both these domains is unclear. We provide evidence in this report that the Lsm domain is important for the role of Scd6 in translation. Mutant of Scd6 lacking the Lsm domain does not cause overexpression growth defect in a manner comparable to the wild type. Similar results were observed with two distinct point mutants of Scd6 wherein putative RNA-binding motifs DxEKxTV and YVG were mutated. Upon overexpression, the three mutants were defective in inducing formation of P-bodies and stress granules which are conserved sites of translation repression. Importantly localization to granules in response to glucose deprivation and sodium azide stress was defective for Lsm domain mutants indicating that the inability to localize to granules could be a reason for their defective role in translation. Deletion of scd6 impairs Lsm1 foci formation upon glucose deprivation stress which could not be rescued by complementation with Lsm-domain deletion mutant of Scd6 when compared to the full-length protein. Put together, our results highlight the role of Lsm domain and its specific motifs in Scd6 activity and provide crucial insight into its function., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2020 Elsevier B.V. All rights reserved.)