6 results on '"Padmanabhan, Prasad"'
Search Results
2. Tests of integration, mild segmentation and segmentation hypotheses
- Author
-
Errunza, Vihang, Losq, Etienne, and Padmanabhan, Prasad
- Subjects
Capital market -- Economic aspects ,Market segmentation -- Research ,Banking, finance and accounting industries ,Business - Abstract
Eight emerging markets are tested for complete integration, mild segmentation and complete segmentation for a group of securities based on an international asset pricing model using the maximum likelihood estimation procedure. The empirical evidence regarding the structure of world capital marhets strongly indicate a leaning of the markets towards a nonpolar streucture. This implies that the world market is neither fully integrated nor completely segmented.
- Published
- 1992
3. Firm level offshoring activities, pollution regulation, triple bottom line, and market structure: What do they have in common?
- Author
-
Zhang, Wenqing, Padmanabhan, Prasad, and Huang, Chia-Hsing
- Subjects
- *
MARKET design & structure (Economics) , *BUSINESS enterprises , *ECONOMIC competition , *GROSS domestic product , *POLLUTION laws - Abstract
Facing global competition, multinational corporations (MNCs) have considered offshoring as a viable alternative to domestic production. By offshoring production, MNCs have generally enjoyed lower labor costs and higher production efficiencies, in addition to other benefits. Unfortunately, target countries chosen for such activities tend to be pollution friendly countries. To make matter worse, strong environmental pollution regulations in host countries (for example, through carbon taxes, focus on the triple bottom line, incentives to select green technology investment options) have incentivized MNCs to offshore more activities. In this study, an optimization model is presented where a domestic firms' propensity to offshore is shown to be function of the market structure in the industry. The findings suggest that a domestic firms' propensity to offshore pollution via production in pollution friendly host countries is directly related to the degree of competition in the industry. In this context, the paper presents specific scenarios where governments could effectively force firms operating in less competitive industry environments to pay an “offshoring penalty”. These proceeds could then be used to subsidize firms in competitive industries who could then be incentivized to adopt green technology instead of offshoring production and pollution. [ABSTRACT FROM AUTHOR]
- Published
- 2018
- Full Text
- View/download PDF
4. Transient transfection and expression of foreign and endogenous genes in the intracellular stages of Trypanosoma cruzi.
- Author
-
Padmanabhan, Prasad K., Polidoro, Rafael B., Barteneva, Natasha S., Gazzinelli, Ricardo T., and Burleigh, Barbara A.
- Subjects
- *
TRYPANOSOMA cruzi , *CHAGAS' disease , *PARASITIC diseases , *GENE transfection , *GENE expression , *EPITOPES , *CHIMERIC proteins - Abstract
The capacity for rapid localization of epitope-tagged or fluorescent fusion proteins in cells is an important tool for biological discovery and functional analysis. For Trypanosoma cruzi , the protozoan parasite that causes human Chagas disease, visualization of ectopically-expressed proteins in the clinically-relevant mammalian stages is hindered by the necessity to first perform transfection and lengthy selection procedures in the insect vector form of the parasite. Here, we demonstrate the ability to by-pass the insect stage with the delivery of plasmid DNA to non-dividing, tissue culture trypomastigotes such that upon host cell infection, transgenes are expressed and rapidly localized in intracellular T. cruzi amastigotes. The inclusion of a sorting step prior to host cell infection by trypomastigotes greatly enriches (>90%) the number of transgene-expressing amastigotes observed in mammalian host cells. This is a significant methodological advance that has the potential to accelerate the pace of discovery in the Chagas disease field. [ABSTRACT FROM AUTHOR]
- Published
- 2014
- Full Text
- View/download PDF
5. Roles for mitochondria in pentamidine susceptibility and resistance in Leishmania donovani
- Author
-
Mukherjee, Angana, Padmanabhan, Prasad K., Sahani, Mayurbhai H., Barrett, Michael Peter, and Madhubala, Rentala
- Subjects
- *
DEHYDROGENASES , *DRUG resistance , *SUCCINATE dehydrogenase , *PARASITES - Abstract
Abstract: Pentamidine resistant Leishmania donovani was raised in the laboratory by stepwise exposure to increasing drug pressure until a line capable of growth in 8μM pentamidine (R8) had been selected. An IC50 value of 40μM was determined for this line, some 50-fold higher than that recorded for the parental wild-type line. The pentamidine resistant promastigotes were cross-resistant to other toxic diamidine derivatives but not to antimonials or substrates of multidrug resistance pumps. Decreased mitochondrial transmembrane potential was observed in pentamidine resistant promastigotes. A substantial net decrease in accumulation of [3H]-pentamidine accompanied the resistance phenotype. Inhibitors of P-glycoprotein pumps, including prochlorperazine and trifluoperazine, did not reverse this decreased drug uptake, which distinguishes the L. donovani resistant line studied here from L. mexicana promastigotes previously studied for pentamidine resistance. Kinetic analysis identified a carrier with an apparent K m value of 6μM for pentamidine. No significant difference between wild-type and resistant parasites could be detected with respect to this transporter in rapid uptake experiments. However, in longer-term uptake experiments and also using concentrations of pentamidine up to 1mM, it was demonstrated that wild-type cells, but not resistant cells, could continue to accumulate pentamidine after apparent saturation via the measured transporter had been reached. Agents that diminish the mitochondrial membrane potential inhibited this secondary route. A fluorescent analogue of pentamidine, 2,5-bis-(4-amidophenyl)-3,4-dimethylfuran (DB99), accumulated in the kinetoplast of wild-type but not resistant parasites indicating that uptake of this cationic compound into mitochondria of wild-type cells was more pronounced than in the resistant line. These data together indicate that resistance to pentamidine in L. donovani is associated with alterations to the mitochondria of the parasites, which lead to reduced accumulation of drug. [Copyright &y& Elsevier]
- Published
- 2006
- Full Text
- View/download PDF
6. A glutathione-specific aldose reductase of Leishmania donovani and its potential implications for methylglyoxal detoxification pathway
- Author
-
Rath, Jyoti, Gowri, V.S., Chauhan, Swati C., Padmanabhan, Prasad K., Srinivasan, N., and Madhubala, Rentala
- Subjects
- *
ALDOSE reductase , *METABOLIC detoxification , *GLUTATHIONE , *LEISHMANIA , *ENZYMES , *NUCLEOTIDE sequence , *PROTEIN analysis - Abstract
Abstract: Methylglyoxal is mainly catabolized by two major enzymatic pathways. The first is the ubiquitous detoxification pathway, the glyoxalase pathway. In addition to the glyoxalase pathway, aldose reductase pathway also plays a crucial role in lowering the levels of methylglyoxal. The gene encoding aldose reductase (ALR) has been cloned from Leishmania donovani, a protozoan parasite causing visceral leishmaniasis. DNA sequence analysis revealed an open reading frame (ORF) of ~855 bp encoding a putative protein of 284 amino acids with a calculated molecular mass of 31.7 kDa and a predicted isoelectric point of 5.85. The sequence identity between L. donovani ALR (LdALR) and mammals and plants is only 36–44%. The ORF is a single copy gene. A protein with a molecular mass that matched the estimated ~74 kDa according to the amino acid composition of LdALR with a maltose binding tag present at its N-terminal end was induced by heterologous expression of LdALR in Escherichia coli. In the presence of glutathione, recombinant LdALR reduced methylglyoxal with a K m of ∼112 μM. Comparative structural analysis of the human ALR structure with LdALR model suggests that the active site anchoring the N-terminal end of the glutathione is highly conserved. However, the C-terminal end of the glutathione backbone is expected to be exposed in LdALR, as the residues anchoring the C-terminal end of the glutathione backbone come from the three loop regions in human, which are apparently shortened in the LdALR structure. Thus, the computational analysis provides clues about the expected mode of glutathione binding and its interactions with the protein. This is the first report of the role of an ALR in the metabolic disposal of methylglyoxal in L. donovani and of thiol binding to a kinetoplastid aldose reductase. [Copyright &y& Elsevier]
- Published
- 2009
- Full Text
- View/download PDF
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.