Search Tracker: Human-derived object tracking in-the-wild through large-scale search and retrieval

Humans use context and scene knowledge to easily localize moving objects in conditions of complex illumination changes, scene clutter and occlusions. In this paper, we present a method to leverage human knowledge in the form of annotated video libraries in a novel search and retrieval based setting to track objects in unseen video sequences. For every video sequence, a document that represents motion information is generated. Documents of the unseen video are queried against the library at multiple scales to find videos with similar motion characteristics. This provides us with coarse localization of objects in the unseen video. We further adapt these retrieved object locations to the new video using an efficient warping scheme. The proposed method is validated on in-the-wild video surveillance datasets where we outperform state-of-the-art appearance-based trackers. We also introduce a new challenging dataset with complex object appearance changes.Comment: Under review with the IEEE Transactions on Circuits and Systems for Video Technolog

Synthesis of zinc oxide nanoparticles using plant leaf extract against urinary tract infection pathogen

In modern science, Nanotechnology is an ablaze field for the researchers. Zinc oxide nanoparticles (ZnO NPs) are known to be one of the most multifunctional inorganic nanoparticles with its application in treatment of urinary tract infection. Nanoparticles were synthesized using Passiflora caerulea fresh leaf extract and were characterized by UV-visible spectroscopy (UV-vis), X-ray diffractometer (XRD), Fourier transform infrared spectroscopy (FT-IR), Scanning electron microscopy (SEM), Energy dispersive analysis of x-ray (EDAX), Atomic force microscopy (AFM). Therefore, the study reveals an efficient, eco-friendly and simple method for the green synthesis of multifunctional ZnO NPs using P. caerulea. Urinary tract infection causing microbes were isolated from the disease affected patient urine sample. The synthesized nanoparticles have been tested against the pathogenic culture showed a very good zone of inhibition compared with plant extract. It indicates the biomedical capability of ZnO NPs

Heterogeneous polymer supported and soluble tantalum metal complex catalysts for acylation reaction: A kinetic study

495-505New soluble and insoluble Tantalum pentachloride complex catalysts are prepared by simple procedures using pyridine and polymer-supported cross-linked (poly-4-vinyl pyridine) beads (PSCPVP) respectively as supports and Tantalum pentachloride as a catalytic moiety (TaCl5). The prepared soluble Py-TaCl5 and insoluble bead-shaped PSCPVP-TaCl5 catalysts have been characterized with FT-IR, UV-Vis, SEM, TGA and elemental analysis techniques. The catalytic efficiency of these catalysts has been examined through acylation of ethanol as a model reaction under identical pseudo first order reaction condition. From the calculated kobs values, it has been noticed that both the catalysts are active and however, Py-TaCl5shown 1.65 fold has increased activity (kobs =11.42x103 min-1) than insoluble PSCPVP-TaCl5 catalyst (kobs= 6.98x103, min-1). Although, PSCPVP-TaCl5 has shown lesser activity than soluble due to its lower cost, recyclability and reusable nature up to third cycle, it has received greater recognition. Hence, in order to utilize this insoluble bead-shaped PSCPVP-TaCl5 catalyst to pack in column reactor and to carry out the same reaction for continuous mode operation at industrial level, detailed kinetics study for acylation of ethanol has been conducted under pseudo first order condition by varying the different experimental parameters and has observed that each parameter has influenced the reaction. The obtained kobs value reveals that reaction rates increase with the increase in the stirring speed, [substrate], [catalyst] and temperature. The thermodynamic parameters viz., activation energy (Ea), entropy (∆S), enthalpy (∆H) and free energy (∆G#) for the reaction are also calculated for the first time and their observed values are 35.2 kJmol-1, -64.6 kJ-1mol-1, 37.7 kJmol-1and 57.3 kJmol-1 respectively. The prepared insoluble catalyst is stable even after its use for three times in acylation without losing its efficiency, thus it is better suited for industrial applications

αA-Crystallin Peptide 66SDRDKFVIFLDVKHF80 Accumulating in Aging Lens Impairs the Function of α-Crystallin and Induces Lens Protein Aggregation

The eye lens is composed of fiber cells that are filled with α-, β- and γ-crystallins. The primary function of crystallins is to maintain the clarity of the lens through ordered interactions as well as through the chaperone-like function of α-crystallin. With aging, the chaperone function of α-crystallin decreases, with the concomitant accumulation of water-insoluble, light-scattering oligomers and crystallin-derived peptides. The role of crystallin-derived peptides in age-related lens protein aggregation and insolubilization is not understood.We found that αA-crystallin-derived peptide, (66)SDRDKFVIFLDVKHF(80), which accumulates in the aging lens, can inhibit the chaperone activity of α-crystallin and cause aggregation and precipitation of lens crystallins. Age-related change in the concentration of αA-(66-80) peptide was estimated by mass spectrometry. The interaction of the peptide with native crystallin was studied by multi-angle light scattering and fluorescence methods. High molar ratios of peptide-to-crystallin were favourable for aggregation and precipitation. Time-lapse recordings showed that, in the presence of αA-(66-80) peptide, α-crystallin aggregates and functions as a nucleus for protein aggregation, attracting aggregation of additional α-, β- and γ-crystallins. Additionally, the αA-(66-80) peptide shares the principal properties of amyloid peptides, such as β-sheet structure and fibril formation.These results suggest that crystallin-derived peptides such as αA-(66-80), generated in vivo, can induce age-related lens changes by disrupting the structure and organization of crystallins, leading to their insolubilization. The accumulation of such peptides in aging lenses may explain a novel mechanism for age-related crystallin aggregation and cataractogenesis

Identification of the Rheumatoid Arthritis Shared Epitope Binding Site on Calreticulin

Background: The rheumatoid arthritis (RA) shared epitope (SE), a major risk factor for severe disease, is a five amino acid motif in the third allelic hypervariable region of the HLA-DRb chain. The molecular mechanisms by which the SE affects susceptibility to – and severity of- RA are unknown. We have recently demonstrated that the SE acts as a ligand that interacts with cell surface calreticulin (CRT) and activates innate immune signaling. In order to better understand the molecular basis of SE-RA association, here we have undertaken to map the SE binding site on CRT. Principal Findings: Surface plasmon resonance (SPR) experiments with domain deletion mutants suggested that the SE binding site is located in the P-domain of CRT. The role of this domain as a SE-binding region was further confirmed by a sulfosuccinimidyl-2-[6-(biotinamido)-2-(p-azido-benzamido) hexanoamido] ethyl-1,3-dithiopropionate (sulfo-SBED) photoactive cross-linking method. In silico analysis of docking interactions between a conformationally intact SE ligand and the CRT P-domain predicted the region within amino acid residues 217–224 as a potential SE binding site. Site-directed mutagenesis demonstrated involvement of residues Glu 217 and Glu 223- and to a lesser extent residue Asp 220- in cell-free SPR-based binding and signal transduction assays. Significance: We have characterized here the molecular basis of a novel ligand-receptor interaction between the SE and CRT. The interaction represents a structurally and functionally well-defined example of cross talk between the adaptive an

High Throughput Ratio Imaging to Profile Caspase Activity: Potential Application in Multiparameter High Content Apoptosis Analysis and Drug Screening

Recent advancement in the area of green fluorescent protein techniques coupled with microscopic imaging has significantly contributed in defining and dissecting subcellular changes of apoptosis with high spatio-temporal resolution. Although single cell based studies using EGFP and associated techniques have provided valuable information of initiation and hierarchical changes of apoptosis, they are yet to be exploited for multiparameter cell based real time analysis for possible drug screening or pathway defining in a high throughput manner. Here we have developed multiple cancer cell lines expressing FRET sensors for active caspases and adapted them for high throughput live cell ratio imaging, enabling high content image based multiparameter analysis. Sensitivity of the system to detect live cell caspase activation was substantiated by confocal acceptor bleaching as well as wide field FRET imaging. Multiple caspase-specific activities of DEVDase, IETDase and LEHDase were analysed simultaneously with other decisive events of cell death. Through simultaneous analysis of caspase activation by FRET ratio change coupled with detection of mitochondrial membrane potential loss or superoxide generation, we identified several antitumor agents that induced caspase activation with or without membrane potential loss or superoxide generation. Also, cells that escaped the initial drug-induced caspase activation could be easily followed up for defining long term fate. Employing such a revisit imaging strategy of the same area, we have tracked the caspase surviving fractions with multiple drugs and its subsequent response to retreatment, revealing drug-dependent diverging fate of surviving cells. This thereby indicates towards a complex control of drug induced tumor resistance. The technique described here has wider application in both screening of compound libraries as well as in defining apoptotic pathways by linking multiple signaling to identify non-classical apoptosis inducing agents, the greatest advantage being that the high content information obtained are from individual cells rather than being population based

Hydroimidazolone Modification of the Conserved Arg12 in Small Heat Shock Proteins: Studies on the Structure and Chaperone Function Using Mutant Mimics

Methylglyoxal (MGO) is an α-dicarbonyl compound present ubiquitously in the human body. MGO reacts with arginine residues in proteins and forms adducts such as hydroimidazolone and argpyrimidine in vivo. Previously, we showed that MGO-mediated modification of αA-crystallin increased its chaperone function. We identified MGO-modified arginine residues in αA-crystallin and found that replacing such arginine residues with alanine residues mimicked the effects of MGO on the chaperone function. Arginine 12 (R12) is a conserved amino acid residue in Hsp27 as well as αA- and αB-crystallin. When treated with MGO at or near physiological concentrations (2–10 µM), R12 was modified to hydroimidazolone in all three small heat shock proteins. In this study, we determined the effect of arginine substitution with alanine at position 12 (R12A to mimic MGO modification) on the structure and chaperone function of these proteins. Among the three proteins, the R12A mutation improved the chaperone function of only αA-crystallin. This enhancement in the chaperone function was accompanied by subtle changes in the tertiary structure, which increased the thermodynamic stability of αA-crystallin. This mutation induced the exposure of additional client protein binding sites on αA-crystallin. Altogether, our data suggest that MGO-modification of the conserved R12 in αA-crystallin to hydroimidazolone may play an important role in reducing protein aggregation in the lens during aging and cataract formation

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Not AvailableStudy was conducted to enhance storage life of cocoa (Theobroma cocoa L.) seeds through encapsulation and germination inhibition at College of Forestry, Kerala, India. The extracted embryonic axes of the seeds were encapsulated with calcium alginate and kept under different storage media alone as well as in combination with osmolytes under varying levels of relative humidity. Embryonic axes with quarter potion of cotyledon were ideal for preparation of synthetic seeds. Among different storage media, greater longevity and viability were observed in ½ MS media while least longevity was observed in dry cotton. Maximum longevity of 70 days was observed in synthetic seeds stored in cotton with 250 mM sorbitol. Longevity was less than 10 days in dry cotton due to absence of moisture content. The incorporation of MS media in the encapsulation reduced the longevity of synthetic seeds. In addition, MS media was found to reduce the activity of inhibitor. Addition sobitol (250 mM; 500 mM) in the encapsulation media enhanced longevity to 65 days. Duration of desiccation was positively correlated with seed longevity. Synthetic seeds stored with wet cotton and 250 mM sorbitol for 55 days and transferred to wet cotton for germination had longevity of 89 days with 80% germination. The results of present study indicate that it is possible to enhance the storage life of cocoa seeds from two weeks to three months by encapsulation and altering storage environment.Not Availabl