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Generalized switched-capacitor multilevel inverter topology with self-balancing capacitors
Jena, Kasinath,Panigrahi, Chinmoy Kumar,Gupta, Krishna Kumar,Kumar, Dhananjay,Dewangan, Niraj Kumar The Korean Institute of Power Electronics 2022 JOURNAL OF POWER ELECTRONICS Vol.22 No.9
This paper presents a switched-capacitor topology with fewer switching components and reduced voltage stresses. The circuit contains eight switches and two capacitors to generate a five-level voltage waveform. This paper provides in-depth descriptions of the structural design, operation, and loss analysis. Inherently self-balanced capacitors are utilized in the proposed topology, which eliminates the need for additional charge balancing circuits and sensors. The control action was implemented using a simple logic-based multicarrier pulse width modulation (PWM) strategy. A brief comparative analysis with state-of-the-art topologies has been presented to demonstrate the merits of the developed topology. Finally, the feasibility and efficacy of the suggested topology have been evaluated using simulation and experimental testing to ensure that it is both feasible and effective.
흰쥐에서 Glomerular Basement Membrane Heparan Sulfate Proteoglycan(GBM HSPG)의 클론
고철우,Kasinath, B . S . 대한신장학회 1996 Kidney Research and Clinical Practice Vol.15 No.3
Although full length cDNA sequences of murine and human basement membrane HSPG are known, rat basement membrane HSPG has not been cloned. Oligonucleotide primers were synthesized from the published sequences of domainI of mouse and human basement membrane HSPG, perlecan, where the homology is 9996. The primers were employed in RT-PCR using polyARNA from rat glomerular epithelial cells (GEC) in culture to obtain a 497-bp product, rat perlecan domain-I (RPD-I). RPD-I was sequenced by dideoxy chain termination method using either the M-13 primers or the perlecan domain-I specific primers. The deduced amino acid sequence of the rat product showed 85 % and 88 % homology to the published sequences of domain-I of mouse and human perlecan, respectively. In RPD-I, the three sites for heparan sulfate glycosaminoglycan attachment with the consensus sequence SGD and the sequence NFT for N-linked oligosaccharide attachment are fully conserved, similar to mouse and human species. By northem analysis, employing total and polyA'RNA of rat GEC, RPD-I detected a single large (-12 kb) transcript, similar in size to rat glomerular perlecan reported previously. Our data demonstrate that GBM HSPG synthesized by rat GEC shares similarity with murine and human perlecan basement membrane HSPG.
배양한 백서의 사구체 상피세포에 대한 당과 후기당화합물에 의한 heparan sulfate proteoglycan의 변화
하태선(Tae Sun Ha),(Balakuntalam S Kasinath),김헌식(Hun Sik Kim) 대한신장학회 2000 Kidney Research and Clinical Practice Vol.19 No.1
N/A HSPG, a component of size-and charge-selective barrier of glomerular basement membrane, is one of important matrix proteins which has been known to be reduced in the kidney of diabetic patients or animals. To examine the effects of glucose and AGE on the HSPG production by cultured GEC, we cultured rat GEC on the AGE- or BSA-coated plate under normal(5mM) and high glucose.(30mM) conditions and measured the change of HSPG production by sandwich-ELISA assay and northern blot analysis at 2 days and one week incubation periods. There was no difference in proliferation between 2 different conditions of culture plate surface. We measured the relative amount of the extracted HSPC and observed significant decreases in high glucose condition at one week incubation, and particularly on the AGE-coated surface as compared to the results of BSA-coated condition, by 22% and 5%, respectively. The expression of mRNA for perlecan promoter was decreased in condition of high glucose and AGE-coated surface by 20Yo at 2 days and 61i at one week. Even in normal glucose condition, the expression of mRNA was reduced by 30Yo at one week if the plate was coated with AGE. In conclusion, both high glucose and AGE have reducing effects on the production of HSPG by GEC in vitro. Their effects seem to be additive, however, the role of AGE is greater than that of glucose, This means that the effort to inhibit AGE formation is more important than short-term glucose control for the prevention of diabetic proteinuria.