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RISS 인기검색어
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- 저자 : Maddukuri, Leena (검색결과 3 건)
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Vasudevarao Pasala,Satyanarayana Maddukuri,V. Sethuraman,Rekha Lankipalli,Devi Gajula,Venkateswarlu Manne The Korean Electrochemical Society 2023 Journal of electrochemical science and technology Vol.14 No.3
For electrode stability and the electrochemical performance of the Li-ion cell, it is essential that the active ingredients and unique additives in the polymer binder be well dispersed with the solvent-based slurry. The efficient procedure used to create the slurry affects the rheological characteristics of the electrode slurry. When successively adding different steps of Nmethyl-2-pyrrolidone (NMP) solvent to the cathode composition, it is evenly disseminated. The electrochemical performance of the Li-ion cells and the electrodes made with slurry formed by single step and multiple steps of addition of NMP solvent are examined. To preform rheological properties of cathode electrode slurry on Ni-rich Lithium Nickel-Cobalt-Aluminum Oxide (LiNi<sub>0.80</sub>Co<sub>0.15</sub>Al<sub>0.05</sub>) (NCA). Also, we investigate different step addition of electrode formation and mechanical strength characterization like peel strength. According to the EIS study, a multi-step electrode slurry has lower internal resistance than a single-step electrode slurry, which results in better electrical characteristics and efficiency. Further, microstructure of electrodes is obtained electrochemical performance in the 18650 cylindrical cells with targeted capacity of 1.5 Ah. The slurry of electrodes prepared by single step and multiple steps of addition of NMP solvent and its effect on the fabrication of 1.5 Ah cells. A three-step solvent addition on slurry has been found to be a lower internal resistance than a single-step electrode slurry as confirmed by the EIS analysis, yielding improved electrical properties and efficiency.
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Human Rev1 polymerase disrupts G-quadruplex DNA
Eddy, Sarah,Ketkar, Amit,Zafar, Maroof K.,Maddukuri, Leena,Choi, Jeong-Yun,Eoff, Robert L. Oxford University Press 2014 Nucleic acids research Vol.42 No.5
<P>The Y-family DNA polymerase Rev1 is required for successful replication of G-quadruplex DNA (G4 DNA) in higher eukaryotes. Here we show that human Rev1 (hRev1) disrupts G4 DNA structures and prevents refolding <I>in vitro</I>. Nucleotidyl transfer by hRev1 is not necessary for mechanical unfolding to occur. hRev1 binds G4 DNA substrates with <I>K</I><SUB>d,DNA</SUB> values that are 4–15-fold lower than those of non-G4 DNA substrates. The pre-steady-state rate constant of deoxycytidine monophosphate (dCMP) insertion opposite the first tetrad-guanine by hRev1 is ∼56% as fast as that observed for non-G4 DNA substrates. Thus, hRev1 can promote fork progression by either dislodging tetrad guanines to unfold the G4 DNA, which could assist in extension by other DNA polymerases, or hRev1 can prevent refolding of G4 DNA structures. The hRev1 mechanism of action against G-quadruplexes helps explain why replication progress is impeded at G4 DNA sites in Rev1-deficient cells and illustrates another unique feature of this enzyme with important implications for genome maintenance.</P>
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Leukotriene Biosynthesis Inhibitor MK886 Impedes DNA Polymerase Activity
Ketkar, Amit,Zafar, Maroof K.,Maddukuri, Leena,Yamanaka, Kinrin,Banerjee, Surajit,Egli, Martin,Choi, Jeong-Yun,Lloyd, R. Stephen,Eoff, Robert L. American Chemical Society 2013 Chemical research in toxicology Vol.26 No.2
<P>Specialized DNA polymerases participate in replication stress responses and in DNA repair pathways that function as barriers against cellular senescence and genomic instability. These events can be co-opted by tumor cells as a mechanism to survive chemotherapeutic and ionizing radiation treatments and as such, represent potential targets for adjuvant therapies. Previously, a high-throughput screen of ∼16,000 compounds identified several first generation proof-of-principle inhibitors of human DNA polymerase kappa (hpol κ). The indole-derived inhibitor of 5-lipoxygenase activating protein (FLAP), MK886, was one of the most potent inhibitors of hpol κ discovered in that screen. However, the specificity and mechanism of inhibition remained largely undefined. In the current study, the specificity of MK886 against human Y-family DNA polymerases and a model B-family DNA polymerase was investigated. MK886 was found to inhibit the activity of all DNA polymerases tested with similar IC<SUB>50</SUB> values, the exception being a 6- to 8-fold increase in the potency of inhibition against human DNA polymerase iota (hpol ι), a highly error-prone enzyme that uses Hoogsteen base-pairing modes during catalysis. The specificity against hpol ι was partially abrogated by inclusion of the recently annotated 25 a.a. N-terminal extension. On the basis of Michaelis–Menten kinetic analyses and DNA binding assays, the mechanism of inhibition by MK886 appears to be mixed. <I>In silico</I> docking studies were used to produce a series of models for MK886 binding to Y-family members. The docking results indicate that two binding pockets are conserved between Y-family polymerases, while a third pocket near the thumb domain appears to be unique to hpol ι. Overall, these results provide insight into the general mechanism of DNA polymerase inhibition by MK886.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/crtoec/2013/crtoec.2013.26.issue-2/tx300392m/production/images/medium/tx-2012-00392m_0005.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/tx300392m'>ACS Electronic Supporting Info</A></P>
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