70 research outputs found

    Moral Rights: International Framework and Indian Approach

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    In the wake of increasing globalization and technical advancements in the digital field, the dissemination of creative work has become easier than ever. However, this development has come with its own set of challenges, particularly for Intellectual Property Law, as most of online transfer of information is unregulated. Digitalization has lead to the imminent need for standardized and stringent protection of an author‟s work. While this protection is mainly conceived as commercial right of the author on his work, there is another fundamental element to it, which is equally important and cannot be neglected, i.e., moral rights. These rights include right of attribution and integrity and are so inextricably related, that they stay with the author, even after transfer of economic rights on the work. In order to ensure effective globalized protection, there is a requirement for minimum standards of protection in all domestic laws, as was provided in the TRIPS agreement. This paper analyzes the Moral Rights regime as envisaged by the TRIPS agreement, and the monoist and dualist approaches that have been adopted by different countries. It also analyzes the evolution of moral rights in India

    Assessment of foot trajectories and ground reaction force in a trans-femoral amputee with Jaipur Knee and 3R20 knee joints

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    In developing countries like India, unilateral transfemoral amputees encounter with the challenge to select and evaluate the knee joint performance. This study aims to evaluate the response of knee joint on vertical ground reaction forces (vGRFs), walking speed, range of motion (ROM) of joints like hip, knee and ankle joints in first two weeks and enhanced response. Movements of different joints were recorded through VICON motion analysis system. Vertical ground reaction forces were captured through AMTI strain gauzed force plate. It has been observed that in two weeks normalized speed increases 0.41 to 0.49 with 3R20. Range of motion of joints was observed with interesting fact that in general with 3R20, joints angle their respective ROM were more than Jaipur Knee but in same cases in second half of gait cycle Jaipur Knee responded better than 3R20 knee joint

    A rare case of term viable abdominal pregnancy with review of literature

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    Abdominal pregnancies are rare types of ectopic pregnancies with high rates of maternal and perinatal morbidity and mortality. Abdominal pregnancy accounts for up to 1.4% of ectopic pregnancies. We report a case of term live abdominal pregnancy without malformation with implantation of the placenta into the uterus and anterior abdominal wall, discovered during a planned obstetric hysterectomy indicated for placenta accreta. Abdominal pregnancy is a serious and potential life-threatening condition. Diagnosis and management can be difficult especially in developing countries. A high index of suspicion is key for timely diagnosis and intervention to prevent life-threatening complications

    Shock Tube as an Impulsive Application Device

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    Current investigations solely focus on application of an impulse facility in diverse area of high-speed aerodynamics and structural mechanics. Shock tube, the fundamental impulse facility, is specially designed and calibrated for present objectives. Force measurement experiments are performed on a hemispherical test model integrated with the stress wave force balance. Similar test model is considered for heat transfer measurements using coaxial thermocouple. Force and heat transfer experiments demonstrated that the strain gauge and thermocouple have lag time of 11.5 and 9 microseconds, respectively. Response time of these sensors in measuring the peak load is also measured successfully using shock tube facility. As an outcome, these sensors are found to be suitable for impulse testing. Lastly, the response of aluminum plates subjected to impulsive loading is analyzed by measuring the in-plane strain produced during deformation. Thus, possibility of forming tests in shock is also confirmed

    Biosynthesis of coral settlement cue tetrabromopyrrole in marine bacteria by a uniquely adapted brominase-thioesterase enzyme pair

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    Author Posting. © The Author(s), 2016. This is the author's version of the work. It is posted here by permission of National Academy of Sciences for personal use, not for redistribution. The definitive version was published in Proceedings of the National Academy of Sciences of United States of America 113 (2016): 3797-3802, doi: 10.1073/pnas.1519695113.Halogenated pyrroles (halopyrroles) are common chemical moieties found in bioactive bacterial natural products. The halopyrrole moieties of mono- and di- halopyrrole-containing compounds arise from a conserved mechanism in which a proline-derived pyrrolyl group bound to a carrier protein is first halogenated then elaborated by peptidic or polyketide extensions. This paradigm is broken during the marine pseudoalteromonad bacterial biosynthesis of the coral larval settlement cue tetrabromopyrrole (1), which arises from the substitution of the proline-derived carboxylate by a bromine atom. To understand the molecular basis for decarboxylative bromination in the biosynthesis of 1, we sequenced two Pseudoalteromonas genomes and identified a conserved four-gene locus encoding the enzymes involved its complete biosynthesis. Through total in vitro reconstitution of the biosynthesis of 1 using purified enzymes and biochemical interrogation of individual biochemical steps, we show that all four bromine atoms in 1 are installed by the action of a single flavin-dependent halogenase- Bmp2. Tetrabromination of the pyrrole induces a thioesterase-mediated offloading reaction from the carrier protein and activates the biosynthetic intermediate for decarboxylation. Insights into the tetrabrominating activity of Bmp2 were obtained from the high-resolution crystal structure of the halogenase contrasted against structurally homologous halogenase Mpy16 that forms only a dihalogenated pyrrole in marinopyrrole biosynthesis. Structure-guided mutagenesis of the proposed substrate-binding pocket of Bmp2 led to a reduction in the degree of halogenation catalyzed. Our study provides a biogenetic basis for the biosynthesis of 1, and sets a firm foundation for querying the biosynthetic potential for the production of 1 in marine (meta)genomes.This work was jointly supported by the US National Science Foundation (OCE-1313747) and the US National Institute of Environmental Health Sciences (P01-ES021921) through the Ocean and Human Health Program to B.S.M., and the US National Institute of Allergy and Infectious Disease R01-AI47818 to B.S.M. and R21- AI119311 to K.E.W. and T.J.M., the Mote Protect Our Reef Grant Program (POR-2012-3), the Dart Foundation, the Smithsonian Competitive Grants Program for Science to V.J.P., the Howard Hughes Medical Institute to J.P.N., the US National Institutes of Health (NIH) Marine Biotechnology Training Grant predoctoral fellowship to A.E. (T32-GM067550), the Helen Hay Whitney Foundation postdoctoral fellowship to V.A., and a Swiss National Science Foundation (SNF) postdoctoral Fellowship to S.D.2016-09-2

    Sharing and community curation of mass spectrometry data with Global Natural Products Social Molecular Networking

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    The potential of the diverse chemistries present in natural products (NP) for biotechnology and medicine remains untapped because NP databases are not searchable with raw data and the NP community has no way to share data other than in published papers. Although mass spectrometry techniques are well-suited to high-throughput characterization of natural products, there is a pressing need for an infrastructure to enable sharing and curation of data. We present Global Natural Products Social molecular networking (GNPS, http://gnps.ucsd.edu), an open-access knowledge base for community wide organization and sharing of raw, processed or identified tandem mass (MS/MS) spectrometry data. In GNPS crowdsourced curation of freely available community-wide reference MS libraries will underpin improved annotations. Data-driven social-networking should facilitate identification of spectra and foster collaborations. We also introduce the concept of ‘living data’ through continuous reanalysis of deposited data

    Structural studies of enzymes involved in antibiotic resistance and phosphonate degradation

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    Biological chemistry revolves around the abiogenetic interplay of high energy labile chemical linkages which shuttle energy and chemical potential, and stable and degradation resistant bonds that make up the biological polymers which offer structural and functional support. Insights into secondary metabolism in microorganisms have shed light on fascinating arrays of genetically encoded small molecule natural products which have utilized the chemical frameworks of transient high energy compounds, and replaced key labile bonds with those borrowed from stable structural molecules. Compounds such as these can be designed as mimics of enzymatic transition states, which thus inhibit the respective enzymes by binding to them, but are not turned over to products. One such example is the Trojan horse tRNA synthetase inhibitor antibiotic microcin C7, which mimics the aminoacyl adenylate intermediate of the tRNA synthetase enzyme by replacing the high energy phosphodiester bond of the enzyme intermediate with a stable phosphoramine-amide linkage. Second examples are the phosphonate molecules which replace the high energy phosphoryl and carboxyl ester moieties of various enzyme intermediates by stable phosphonate linkages. These compounds in addition to possessing bioinhibitory activities are also thought to be store houses of carbon and phosphorous in the microbial metabolome as they cannot be easily degraded. The body of work presented in this dissertation delves into molecular mechanisms of enzymatic degradation of the stable phosphoramine-amide bond of microcin C7, as well as the hydrolysis of the phosphonate bond in a ubiquitous phosphonate molecule- phosphonoacetate. Both these studies, presented in the form of two chapters, involve the atomic resolution structure determination of the enzyme catalysts during various stages of their catalytic cycles, and in complex with different substrate molecules which delineate their specificity and selectivity. All structural investigations have been followed by extensive biochemical validation of the structural results. These results have allowed us to postulate the reaction mechanisms for these catalysts. Our proposals reveal how enzymatic architectures have been borrowed from primary metabolism, and the enzyme active sites slightly tweaked to achieve remarkable and unprecedented chemical transformations by these enzymes of microbial secondary metabolism. Our studies also have implications for the design of inhibitors of these enzymes, as similar mechanisms may be used to avert the bioinhibitory action of various antibiotics by drug resistant pathogenic microorganisms
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