995 research outputs found
An Enhanced Least Significant Bit Steganography to Improve the Effectiveness of Graphical Password Authentication
Authentication means acknowledging a user’s identity. It is the way of associating a request with a set of identity. The identification provided is an authorized user’s information on a personal computer system or within an authentication server. A graphical password is a validation system in which user has to select from images, in a particular order, presented in a graphical user + interface (GUI). Graphical passwords can be easily remembered, as users remember images better than words. Also, the system should be more unaffected by brute-force attacks, because there is practically an infinite search space. Complex text passwords are hard to remember and simple textual passwords are easy to guess. Graphical passwords provide more robustness and memorability. It is a secure mechanism to provide authenticated sign up to a system
Myo2p is the major motor involved in actomyosin ring contraction in fission yeast
Cytokinesis in many eukaryotes requires an actomyosin-based contractile ring [1]. In fission yeast, cytokinesis involves the type II myosins Myo2p and Myp2p and the type V myosin Myo51p [2]. A recent study by Laplante et al. [3], using deletion mutants of myp2 and myo51 and the mis-sense mutant myo2-E1 [4], concluded that each myosin has distinct functions and proposed that Myp2p plays the dominant role in actomyosin ring contraction. Here we present evidence that Myo2p, not Myp2p, is likely to be the major motor driving actomyosin ring contractility. Since the previous work [3] was performed at 25°C, the permissive temperature for myo2-E1, we compared cytokinesis timings in myo2-E1 and myo2Δ at 25°C and found that myo2-E1 is only partially compromised at 25°C. Furthermore, we find that myp2Δ and myp2Δ myo51Δ double mutants contract actomyosin rings at ∼90% of the rate of wild-type cells at 30°C and 36°C, suggesting that Myp2p plays a minimal role in ring contraction at these temperatures. Finally, ring contraction in our myo2-E1 strain took longer at 25°C than previously reported [3]. Although faster-acting alleles of myo2 will be required to evaluate its contribution at 25°C, our work establishes that Myo2p is the major motor involved in ring contraction, under most, if not all, conditions
Identification of Phytochemical Constituents of Aegle marmelos Responsible for Antimicrobial Activity against Selected Pathogenic Organisms
Antimicrobial activity and phytochemical constituents of an ethanolic extract of Aegle marmelos were investigated. The phytochemical screening of the crude extract revealed the presence of Alkaloids, Cardiac glycosides, Terpenoids, Saponins, Tannis, Flavonoids, and Steroids. The crude ethanolic extract was tested for antimicrobial activity against gram positive organisms of Bacillus subtilis (NCIM: 3471), Staphylococcus aureus (NCIM: 2079), gram negative Escherichia coli (NCIM: 2065) and Pseudomonas aeruginosa (NCIM: 2200) at different concentrations levels of 0.5, 1.0, 1.5, 2.0 and 2.5 mg/ml. At the 2.5 mg/ml concentration, gram negative Escherichia coli exhibits a zone of inhibition about 25.7mm; Pseudomonas aeruginosa 19.9mm; gram positive Staphylococcus aureus 29.0 mm; and Bacillus subtilis, a maximum zone of inhibition about 28.1 mm as compared to the control drug penicillin. Escherichia coli, Pseudomonas aeruginosa and Bacillus subtilis exhibit a maximum zone of inhibition, hence they were considered as susceptible to the plant extracts but Staphylococcus aureus doesn’t exhibit such a zone of inhibition and is therefore considered as resistant
Motor activity dependent and independent functions for Myosin II in cytokinesis contribute to actomyosin ring assembly and contraction in Schizosaccharomyces pombe
Cytokinesis depends on a contractile actomyosin ring in many eukaryotes [1, 2, 3]. Myosin II is a key component of the actomyosin ring, although whether it functions as a motor or as an actin cross-linker to exert its essential role is disputed [1, 4, 5]. In Schizosaccharomyces pombe, the myo2-E1 mutation affects the upper 50 kDa sub-domain of the myosin II heavy chain, and cells carrying this lethal mutation are defective in actomyosin ring assembly at the non-permissive temperature [6, 7]. myo2-E1 also affects actomyosin ring contraction when rings isolated from permissive temperature-grown cells are incubated with ATP [8]. Here we report isolation of a compensatory suppressor mutation in the lower 50 kDa sub-domain (myo2-E1-Sup1) that reverses the inability of myo2-E1 to form colonies at the restrictive temperature. myo2-E1-Sup1 is capable of assembling normal actomyosin rings, although rings isolated from myo2-E1-Sup1 are defective in ATP-dependent contraction in vitro. Furthermore, the product of myo2-E1-Sup1 does not translocate actin filaments in motility assays in vitro. Superimposition of myo2-E1 and myo2-E1-Sup1 on available rigor and blebbistatin-bound myosin II structures suggests that myo2-E1-Sup1 may represent a novel actin translocation-defective allele. Actomyosin ring contraction and viability of myo2-E1-Sup1 cells depend on the late cytokinetic S. pombe myosin II isoform, Myp2p, a non-essential protein that is normally dispensable for actomyosin ring assembly and contraction. Our work reveals that Myo2p may function in two different and essential modes during cytokinesis: a motor activity-independent form that can promote actomyosin ring assembly and a motor activity-dependent form that supports ring contraction
Simulation and Performance Evaluation of Shunt Hybrid Power Filter for Power Quality Improvement Using PQ Theory
This work proposes the design of shunt hybrid filter using instantaneous power theory to improve the power quality and simulation has been carried out for 3 phase distribution system feeding different types of non linear loads. The proposed filter consists of parallel combination of 5th and 7th tuned selective harmonic elimination passive filters, which is connected in series with a small rating IGBTs based voltage source inverter. In this work, principle of compensation and filtering behavior of the system has been discussed in detail. Instantaneous real and reactive power theory based controller has been designed to estimate the reference current from the distorted current. In order to reduce the harmonics, generated reference currents are tracked by voltage source inverter using hysteresis band current controller. The performance of the hybrid scheme is evaluated for various nonlinear loads using Matlab/ Simulink tool. The detailed analysis has been carried out on harmonics reduction and DC bus voltage regulation and the simulation result ensures the feasibility of suggested control strategy. The proposed topology improves the filtering performance of the passive filter in hybrid scheme
C-STrap Sample Preparation Method—In-Situ Cysteinyl Peptide Capture for Bottom-Up Proteomics Analysis in the STrap Format
Recently we introduced the concept of Suspension Trapping (STrap) for bottom-up proteomics sample processing that is based upon SDS-mediated protein extraction, swift detergent removal and rapid reactor-type protein digestion in a quartz depth filter trap. As the depth filter surface is made of silica, it is readily modifiable with various functional groups using the silane coupling chemistries. Thus, during the digest, peptides possessing specific features could be targeted for enrichment by the functionalized depth filter material while non-targeted peptides could be collected as an unbound distinct fraction after the digest. In the example presented here the quartz depth filter surface is functionalized with the pyridyldithiol group therefore enabling reversible in-situ capture of the cysteine-containing peptides generated during the STrap-based digest. The described C-STrap method retains all advantages of the original STrap methodology and provides robust foundation for the conception of the targeted in-situ peptide fractionation in the STrap format for bottom-up proteomics. The presented data support the method’s use in qualitative and semi-quantitative proteomics experiments
Stochastic Cytokine Expression Induces Mixed T Helper Cell States
During eukaryotic development, the induction of a lineage-specific transcription factor typically drives differentiation of multipotent progenitor cells, while repressing that of alternative lineages. This process is often mediated by some extracellular signaling molecules, such as cytokines that can bind to cell surface receptors, leading to activation and/or repression of transcription factors. We explored the early differentiation of naive CD4 T helper (Th) cells into Th1 versus Th2 states by counting single transcripts and quantifying immunofluorescence in individual cells. Contrary to mutually exclusive expression of antagonistic transcription factors, we observed their ubiquitous co-expression in individual cells at high levels that are distinct from basal-level co-expression during lineage priming. We observed that cytokines are expressed only in a small subpopulation of cells, independent from the expression of transcription factors in these single cells. This cell-to-cell variation in the cytokine expression during the early phase of T helper cell differentiation is significantly larger than in the fully differentiated state. Upon inhibition of cytokine signaling, we observed the classic mutual exclusion of antagonistic transcription factors, thus revealing a weak intracellular network otherwise overruled by the strong signals that emanate from extracellular cytokines. These results suggest that during the early differentiation process CD4 T cells acquire a mixed Th1/Th2 state, instructed by extracellular cytokines. The interplay between extracellular and intracellular signaling components unveiled in Th1/Th2 differentiation may be a common strategy for mammalian cells to buffer against noisy cytokine expression.National Cancer Institute (U.S.). Physical Sciences-Oncology Center (U54CA143874)National Institutes of Health (U.S.) (Pioneer Award)National Institutes of Health (U.S.) (Grant R01-GM068957
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