172 research outputs found
Be Unconditionally Happy!
No full textJournal #39 from Media Rise's Quarantined Across Borders Collection by Anupkumar Shetty. From India. Quarantined in Texas.Staying busy practicing gratitude, mindful breathing, meditation, prayer, reading, writing and other activities you like are ways to be unconditionally happy and stress-free in life.Media Rise Publications. Quarantined Across Borders Collection. Edited by Dr. Srividya "Srivi" Ramasubramanian
A4NT : Author Attribute Anonymity by Adversarial Training of Neural Machine Translation
No full textText-based analysis methods enable an adversary to reveal privacy relevant author attributes such as gender, age and can identify the text's author. Such methods can compromise the privacy of an anonymous author even when the author tries to remove privacy sensitive content. In this paper, we propose an automatic method, called the Adversarial Author Attribute Anonymity Neural Translation (), to combat such text-based adversaries. Unlike prior works on obfuscation, we propose a system that is fully automatic and learns to perform obfuscation entirely from the data. This allows us to easily apply the system to obfuscate different author attributes. We propose a sequence-to-sequence language model, inspired by machine translation, and an adversarial training framework to design a system which learns to transform the input text to obfuscate the author attributes without paired data. We also propose and evaluate techniques to impose constraints on our model to preserve the semantics of the input text. learns to make minimal changes to the input to successfully fool author attribute classifiers, while preserving the meaning of the input text. Our experiments on two datasets and three settings show that the proposed method is effective in fooling the attribute classifiers and thus improves the anonymity of authors
Fresh-pack potatoes: handling, packaging and transportation in refrigerated railcars
No full textBulletin no. 804 Moscow, Idaho :University of Idaho, College of Agriculture, Agriculture Experiment Station, 1998-07-01. Author(s): Shetty, Kiran; Casada, Mark; Zhu, Hua; Thornton, Mike; Nolte, Phili
Differential involvement of Ca2+/calmodulin-dependent protein kinases and mitogen-activated protein kinases in the dopamine D1/D5 receptor-mediated potentiation in hippocampal CA1 pyramidal neurons
No full textAbstractDopaminergic neurotransmission modulates and influences hippocampal CA1 synaptic plasticity, learning and long-term memory mechanisms. Investigating the mechanisms involved in the slow-onset potentiation induced by the dopamine D1/D5 receptor agonists in hippocampal CA1 region, we have reported recently that it could play a role in regulating synaptic cooperation and competition. We have also shown that a sustained activation of MEK/MAP kinase pathway was involved in the maintenance of this long-lasting potentiation (Shivarama Shetty, Gopinadhan, & Sajikumar, 2016). However, the molecular aspects of the induction of dopaminergic slow-onset potentiation are not known. Here, we investigated the involvement of MEK/MAPK pathway and Ca2+-calmodulin-dependent protein kinases (CaMKII and CaMKIV) in the induction and maintenance phases of the D1/D5 receptor-mediated slow-onset potentiation. We report differential involvement of these kinases in a dose-dependent manner wherein at weaker levels of dopaminergic activation, both CaMKII and MEK1/2 activation is necessary for the establishment of potentiation and with sufficiently stronger dopaminergic activation, the role of CaMKII becomes dispensable whereas MEK activation remains crucial for the long-lasting potentiation. The results are interesting in view of the involvement of the hippocampal dopaminergic system in a variety of cognitive abilities including memory formation and also in neurological diseases such as Alzheimer’s disease and Parkinson’s disease
Detection of Rotavirus and Adenovirus diarrhea in children below five years, in Dakshina Kannada District, a coastal region of Karnataka State, India
No full textContext: Diarrheal disease is the second largest cause of death of children under 5 years. Viral diarrhea is most common which is usually caused by Rotavirus followed by enteric Adenovirus. Rotaviruses are responsible for approximately 527,000 deaths mainly in low-income countries of Africa and Asia. There is limited number of studies done on viral diarrhea in this coastal belt. Aim: To determine the prevalence of Rotavirus and Adenovirus diarrhea among children below 5 years of age and its epidemiological importance in this coastal region of Karnataka State, India. The impact of factors like socio-economic status, drinking water, and Rotavirus immunization status that can contribute to the disease were also evaluated and recommendations are formulated for disease prevention. Materials and Methods: Children below 5 years of age with history of diarrhea, vomiting and fever of less than 3 days were included in this study. The sample size was 35. General physical examination, clinical findings and other details like socio-economic status, personal hygiene, growth milestones and family income were also recorded. A commercial Rotavirus and Adenovirus antigen detection kit was used to detect the presence of Rotavirus and Adenovirus antigen from the stool sample. Results: Out of 35 patients screened, 25 (71.43%) patients were negative for both Adenovirus and Rotavirus, 10 children (28.57%) were positive for Rotavirus and no patients were positive for Adenovirus. Severe dehydration, fever, loose stools and vomiting were the commonest symptoms seen in Rotavirus positive children. The highest incidence of infection with Rotavirus was seen among 7-12 months age group. Children whose stool was positive for Rotavirus used public water supply. Conclusions: Rotavirus is an important cause of diarrhea in children below 5 years in this coastal region. A simple, rapid immunochromatography test is useful and economical tool to simultaneously detect and screen Adenovirus and Rotavirus. Low socioeconomic state and unsafe water supply contributes to diarrheal disease
Structure Analysis Of Plant Lectin Domains
No full textLectins are multivalent carbohydrate binding proteins that specifically recognise diverse sugar structures and mediate a variety of biological processes, such as cell-cell and host-pathogen interactions, serum glycoprotein turnover and innate immune responses. Lectins have received considerable attention in recent years on account of their properties leading to wide use in research and biomedical applications. Seeds of leguminous plants are mainly rich sources of lectins, but lectins are also found in all classes and families of organisms. Legume lectins have similar tertiary structures, but exhibit a large variety of quaternary structures. The carbohydrate binding site in them is made up of four loops, the first three of which are highly conserved in all legume lectins. The fourth loop, which is variable, is implicated in conferring specificity. Legume lectins which share the same monosaccharide specificity often exhibit markedly different oligosaccharide specificities. This thesis primarily concerns with structure solution and analysis of lectins from the legume and β-prism II fold families using X-ray crystallography. Apart from having the property of specifically and reversibly binding to carbohydrates, lectins are also interesting models to study sequence-structure relationships, especially of how minor change in the sequence may bring about major changes in oligomerization and binding.
Chapter 1 gives an overview of different structural types of plant lectins and describes in detail, their carbohydrate binding features. The details of the various experimental procedures employed during the course of this research, are explained in Chapter 2.
Chapter 3 describes the crystal structure of a β-prism II fold lectin (RVL), from Remusatia vivipara, an epiphytic plant of traditional medicinal value, and analysis of its binding properties. This lectin was established to have distinct binding properties and has nematicidal activity against a root-knot nematode with the localization site identified as the high-mannose displaying gut-lining in the nematode. The crystal structure of RVL revealed a new quaternary association of this homodimeric lectin, different from those of reported β-prism II lectins. Functional studies on RVL showed that it fails to bind to simple mannose moieties yet showed agglutination with rabbit blood cells (which have mannose moieties on the surface) and some high mannose containing glycoproteins like mucin and asialofetuin. Further, ELISA and glycan array experiments indicated that RVL has high affinity to N-glycans like trimannose pentasaccharide such as in gp120, a capsid glycoprotein of HIV virus, necessary in virus-association with the host cell. The structural basis for this N-glycan binding was revealed through structure analysis and molecular modelling, and it was demonstrated that there are two distinct binding sites per monomer, making RVL a truly multivalent lectin. Evolutionary phylogeny revealed the divergence in the β-prism II fold proteins with regards to the number of sugar-binding regions per domain, oligomerization and specificity.
Chapter 4 deals with the structural studies on a galactose-specific legume lectin (DLL-II) from Dolichos lablab, a leguminous plant. The lectin was found to be a planar tetramer in the crystal structures of the native and ligand bound forms, as expected from our solution studies and phylogenetic analysis. The protein is a heterotetramer with subunits differing only in the presence or absence of a C-terminal helical region at the core of the tetramer. Due to the static disorder in all the crystals, the central helix could be oriented in either direction. Structure analysis of DLL-II proved to be an interesting endeavour as static disorder compounded with twinning in the crystal made the data processing and structure solution a challenging process. Subsequent structure and sequence alignments led to the identification of an adenine-binding pocket in the hydrophobic core of the tetramer. Based on this, DLL-II lectin was co-crystallized with adenine and the structure revealed the presence of adenine at the predicted binding site.
Chapter 5 describes the identification and analysis of potential plant lectins/lectin-like domains in the genome of Oryza sativa, using bioinformatics approaches. This project was initiated to study the occurrence of legume-lectin like domains (a predominant dicot feature) in O. sativa, which is a monocot. Later, a large scale genome analysis for all types of lectin domains was carried out through exhaustive PSI-BLAST, profile matching by HMMer, CDD and MulPSSM. The final validation was carried out by assessing the carbohydrate binding potential of the domain by examining the sugar binding sites. The primary interest in undertaking this work was to find the occurrence of association of these domains with other domains as in protein receptor kinases, where lectin is the receptor domain. Though primarily initiated as a bioinformatics project, further structural characterization was attempted by cloning, expression and purification of some of the annotated lectin proteins using prokaryotic expression systems. The protein expression was attained in reasonable amounts for a few of the annotated legume lectin homologs, however purification is yet to be achieved as the expressed proteins are insoluble.
A part of the results described in this thesis and the other related projects that the author was involved are reported in the following publications.
1) Purification, characterization and molecular cloning of a monocot mannose-binding lectin from Remusatia vivipara with nematicidal activity Bhat GG, Shetty KN, Nagre NN, Neekhra VV, Lingaraju S, Bhat RS, Inamdar SR, Suguna K, Swamy BM. 2010. Glycoconjugate J. 27(3):309-320
2) Modification of the sugar specificity of a plant lectin: structural studies on a point mutant of Erythrina corallodendron lectin Thamotharan S, Karthikeyan T, Kulkarni KA, Shetty KN, Surolia A, Vijayan M & Suguna K. 2011. Acta Crystallographica D 67(3):218-227
3) Crystal structure of a β-prism II lectin from Remusatia vivipara Shetty KN, Bhat GG, Inamdar SR, Swamy BM, Suguna K. 2012. Glycobiology 22(1): 56-69.
4) Structure of a galactose binding lectin from Dolichos lablab
Shetty KN, Lavanyalatha V, Rao RN, SivaKumar N & Suguna K (Under review)
5) Occurrence of lectin-like domains: Oryza sativa genome analysis. Shetty KN & Suguna K. (Manuscript in preparation
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