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- 저자 : Chavda, Alap P. (검색결과 5 건)
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Nanostructured SnS with inherent anisotropic optical properties for high photoactivity
Patel, Malkeshkumar,Chavda, Arvind,Mukhopadhyay, Indrajit,Kim, Joondong,Ray, Abhijit The Royal Society of Chemistry 2016 Nanoscale Vol.8 No.4
<P>In view of the worldwide energy challenge in the 21<SUP>st</SUP>century, the technology of semiconductor-based photoelectrochemical (PEC) water splitting has received considerable attention as an alternative approach for solar energy harvesting and storage. Two-dimensional (2D) structures such as nanosheets have the potential to tap the solar energy by unlocking the functional properties at the nanoscale. Tin(ii) sulfide is a fascinating solar energy material due to its anisotropic material properties. In this manuscript, we report on exploiting the 2D structure modulated optical properties of nanocrystalline SnS thin film synthesized by chemical spray pyrolysis using ambient transport in the harvesting of solar energy. We obtained the nanostructured SnS with well-preserved dimensions and morphologies with one step processing. The work demonstrates that the intrinsically ordered SnS nanostructure on FTO coated glass can tap the incident radiation in an efficient manner. The structure-property relationship to explain the photo-response in nanocrystalline-SnS is verified experimentally and theoretically. The novel design scheme for antireflection coating along with the anisotropic properties of SnS is conceived for realizing a PEC cell. The developed PEC cell consists of a SnS photoanode which shows considerably high photocurrent density of 7 mA cm<SUP>−2</SUP>with aqueous media under AM 1.5G, 100 mW cm<SUP>−2</SUP>exposure with notably stable operation. Electrochemical impedance spectroscopy revealed that a non-ideal capacitive behavior as well as drift assisted transport across the solid-state interface is responsible for such a high photo-current density in the nanocrystalline-SnS photoanode.</P>
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Jerry C. Ku,Vishal Chavda,Paolo Palmisciano,Christopher R. Pasarikovski,Victor X.D. Yang,Ruba Kiwan,Stefano M. Priola,Bipin Chaurasia 대한뇌혈관외과학회 2023 Journal of Cerebrovascular and Endovascular Neuros Vol.25 No.4
The Anterior Inferior Cerebellar Artery-Posterior Inferior Cerebellar Artery (AICA-PICA) common trunk is a rare variant of cerebral posterior circulation in which a single vessel originating from either the basilar or vertebral arteries supplies both cerebellum and brainstem territories. We present the first case of an unruptured right AICA-PICA aneurysm treated with flow diversion using a Shield-enhanced pipeline endovascular device (PED, VANTAGE Embolization Device with Shield Technology, Medtronic, Canada). We expand on this anatomic variant and review the relevant literature.A 39-year-old man presented to our treatment center with vertigo and right hypoacusis. The initial head CT/CTA was negative, but a 4-month follow-up MRI revealed a 9 mm fusiform dissecting aneurysm of the right AICA. The patient underwent a repeat head CTA and cerebral angiogram, which demonstrated the presence of an aneurysm on the proximal portion of an AICA-PICA anatomical variant. This was treated with an endovascular approach that included flow diversion via a PED equipped with Shield Technology. The patient’s post-procedure period was uneventful, and he was discharged home after two days with an intact neurological status. The patient is still asymptomatic after a 7-month follow-up, with MR angiogram evidence of stable aneurysm obliteration and no ischemic lesions.Aneurysms of the AICA-PICA common trunk variants have a high morbidity risk due to the importance and extent of the territory vascularized by a single vessel. Endovascular treatment with flow diversion proved to be both safe and effective in obliterating unruptured cases.
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Kothiya Madhvi,Kuldeep Mehta,K. R. Vadalia,Chavda Jay,Kapadiya Sandip 한국약제학회 2015 Journal of Pharmaceutical Investigation Vol.45 No.2
The co-processing is most widely exploredmethod for development of directly compressible excipients. The present research was focused on development ofco-processed excipients for fast dissolving tablets of Irbesartanby melt agglomeration technique. From the preliminarytrials Lactose monohydrate and mannitol wasselected as a diluent and Poly ethylene glycol 4000 asbinder. To improve functionality of co-processed excipients8 % crospovidone was incorporated. Diluent blendratio and concentration of binder (%) were selected asindependent variables in central composite design. Theagglomerates were evaluated in terms of % fines, angle ofrepose, Carr’s index, Hausner ratio. The tablets weremanufactured on a rotary press and their friability, tensilestrength and disintegration time were evaluated. Thisoptimized batch was characterized by means of the granularfriability index, Heckel analysis, Kawakita, Kuno’sanalysis, lubricant sensitivity ratio and a dilution potentialstudy. Result of dilution potential showed that up to 40 %drug can be incorporated. In addition to these, bitter taste ofdrug was masked by forming drug—β-cyclodextrin inclusioncomplex and by adding aspartame as a Sweetener. Compared to conventional tablet it showed faster dissolution. Instrumental studies like Fourier transform-infraredspectroscopy, differential scanning calorimetry, X-raydiffraction showed that the compatibility of various excipientswith drug. The present study underlines the factthat melt granulation technique may be adopted for thedevelopment of directly compressible adjuvant for use inpharmaceuticals.
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Badyal, Sandip K.,Basran, Jaswir,Bhanji, Nina,Kim, Ju Hwan,Chavda, Alap P.,Jung, Hyun Suk,Craig, Roger,Elliott, Paul R.,Irvine, Andrew F.,Barsukov, Igor L.,Kriajevska, Marina,Bagshaw, Clive R. Elsevier 2011 Journal of molecular biology Vol.405 No.4
<P>The interaction between the calcium-binding protein S100A4 and the C-terminal fragments of nonmuscle myosin heavy chain IIA has been studied by equilibrium and kinetic methods. Using site-directed mutants, we conclude that Ca<SUP>2+</SUP> binds to the EF2 domain of S100A4 with micromolar affinity and that the <I>K</I><SUB>d</SUB> value for Ca<SUP>2+</SUP> is reduced by several orders of magnitude in the presence of myosin target fragments. The reduction in <I>K</I><SUB>d</SUB> results from a reduced dissociation rate constant (from 16 s<SUP>− 1</SUP> to 0.3 s<SUP>− 1</SUP> in the presence of coiled-coil fragments) and an increased association rate constant. Using peptide competition assays and NMR spectroscopy, we conclude that the minimal binding site on myosin heavy chain IIA corresponds to A1907-G1938; therefore, the site extends beyond the end of the coiled-coil region of myosin. Electron microscopy and turbidity assays were used to assess myosin fragment filament disassembly by S100A4. The latter assay demonstrated that S100A4 binds to the filaments and actively promotes disassembly rather than just binding to the myosin monomer and displacing the equilibrium. Quantitative modelling of these <I>in vitro</I> data suggests that S100A4 concentrations in the micromolar region could disassemble myosin filaments even at resting levels of cytoplasmic [Ca<SUP>2+</SUP>]. However, for Ca<SUP>2+</SUP> transients to be effective in further promoting dissociation, the elevated Ca<SUP>2+</SUP> signal must persist for tens of seconds. Fluorescence recovery after photobleaching of A431/SIP1 cells expressing green fluorescent protein–myosin IIA, immobilised on fibronectin micropatterns to control stress fibre location, yielded a recovery time constant of around 20 s, consistent with <I>in vitro</I> data.</P>
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