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Institution

Kuvempu University

EducationShimoga, India
About: Kuvempu University is a education organization based out in Shimoga, India. It is known for research contribution in the topics: Cyclic voltammetry & Carbon paste electrode. The organization has 1575 authors who have published 2210 publications receiving 39755 citations. The organization is also known as: KU.


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Journal ArticleDOI
16 Mar 2010-Vaccine
TL;DR: The cross-protective efficacy of binary ethylenimine-inactivated BTV-1 vaccine was evaluated in Indian native sheep against virulent heterologous B TV-23 serotype challenge and suggested that inactivated B television vaccine induced appreciable cell-mediated immunity (CMI) and greatly reduced the severity of heterOLOGous B television-23 infection.

47 citations

Journal ArticleDOI
TL;DR: A public resource for OSM induced signaling events is created by systematically gathered and curated molecular information from literature and integrated OSM signaling pathway into NetPath (Kandasamy et al. 2010), which is a public resource of human signaling pathways.
Abstract: Oncostatin M (OSM), belonging to the IL-6 family of cytokines (Heinrich et al. 2003), was first reported and purified from U937 monocytic cells (Zarling et al. 1986; Ensoli et al. 1999; Hasegawa et al. 1999). In normal physiological condition, OSM is associated with multiple biological processes and cellular responses including growth, differentiation, and inflammation However, anti-proliferative activity of OSM against breast cancer cell line generated the interest of biomedical community on this molecule (Douglas et al. 1997, 1998). OSM was also found associated with pathological conditions such as proliferation of ovarian cancer cells (Taga and Kishimoto 1997), prostate cancer 22Rv1 cells (Hoffman et al. 1996), up-regulation of the ER chaperone Grp78/BiP in the liver cells, atherosclerotic lesions, ischemic heart disease and rheumatoid arthritis (Linsley et al. 1990; Dunham et al. 1999). The dual role of OSM in either inducing or inhibiting the proliferation of various types of cells called upon the scientific community to investigate role of OSM in various physiological and experimental contexts in detail. However, diverse molecular level information pertaining to OSM signaling is not available in a centralized resource. Therefore, we have systematically gathered and curated molecular information from literature and created a public resource for OSM induced signaling events. We integrated OSM signaling pathway into NetPath (Kandasamy et al. 2010), which is a public resource of human signaling pathways. OSM is known to mediate its biological effects by binding to two distinct heterodimers of gp130 with either leukemia inhibiting factor receptor (LIFR) or OSM receptor-beta (OSMR-beta) (Thoma et al. 1994). Former heterodimer between gp130 and LIFR is called type I receptor complex and the latter between gp130 and OSMR-beta is called type II receptor complex. Type I receptor can bind to either OSM or leukemia inhibiting factor, whereas type II receptor has more affinity towards OSM (O’Hara et al. 2003). The binding of OSM to either gp130/OSMR-beta or gp130/LIFR induces the activation of Janus Kinase family members through tyrosine phosphorylation (Tanaka and Miyajima 2003). The activated JAK family members in turn induce the activation of Signal Transduction and Activator of Transcription (STAT) proteins (Schaefer et al. 2000). Alternatively, the activated receptors can also activate mitogen-activated protein kinase (MAPK) pathway (Van Wagoner et al. 2000) and PI3K/AKT pathways (Arita et al. 2008). It was also reported that OSM bring about ligand-induced receptor degradation of gp130, OSMR-beta, and LIFR before enhancing the synthesis of the receptor subunits (Blanchard et al. 2001).

46 citations

Journal ArticleDOI
TL;DR: In this paper, the synthesis of five novel heterocyclic azo dyes (4a-4e) through conventional diazo-coupling reaction of 4, 5, 6, 7-tetrahydro-1, 3-benzothiazole with various coupling compounds at 0-5

46 citations

Journal ArticleDOI
TL;DR: This study comprehensively reports 386 novel proteins that have important potential as biomarker candidates for future research into personalized medicine and diagnostics aimed towards improving visual health.
Abstract: The aqueous humor is a colorless, transparent fluid that fills the anterior chamber of the eye. It plays an important role in maintaining the intraocular pressure and providing nourishment to the lens and cornea. The constitution of the aqueous humor is controlled by the blood-aqueous barrier. Though this ocular fluid has been extensively studied, its role in ocular physiology is still not completely understood. In this study, aqueous humor samples were collected from 250 patients undergoing cataract surgery, subjected to multiple fractionation strategies and analyzed on a Fourier transform LTQ-Orbitrap Velos mass spectrometer. In all, we identified 763 proteins, of which 386 have been identified for the first time in this study. Sorbitol dehydrogenase (SORD), filensin (BFSP1), and phakinin (BFSP2) are some of the proteins that have not been previously reported in the aqueous humor. Gene Ontology analysis revealed 35% of the identified proteins to be extracellular, with a majority of them involved in cell communication and signal transduction. This study comprehensively reports 386 novel proteins that have important potential as biomarker candidates for future research into personalized medicine and diagnostics aimed towards improving visual health.

46 citations


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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20238
202224
2021214
2020189
2019139
2018135