26 research outputs found

    Organization of the course contents in the Virtual Proteomics Laboratory at IIT Bombay.

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    <p>(A) Module I (an overview of gel-based proteomics) consists of three experiments: gel-based proteomics (2DE) to analyze human serum, bacterial, and plant proteome; and analysis of differential expression of proteins between test and control samples. (B) Module II (an overview of MALDI-TOF MS) is focused on MS-based proteomics and consists of five experiments: in-gel digestion of proteins for MS analysis; sample preparation for the MALDI-TOF MS analysis; MALDI-TOF instrumentation and analysis of serum proteins; MS data analysis, peptide mass fingerprinting (PMF); and molecular weight determination of intact proteins. Schematic representation of MALDI-TOF instrument and operation procedure for generating peptide/protein spectrum for protein identification. (C) Module III (an overview of bioinformatics) covers the bioinformatics tools that are commonly used in proteomics. This module includes four experiments: sequence alignment, homology modeling, functional annotation, and molecular docking. Structural analysis and 3-D modeling of target proteins has been depicted.</p

    Schematic representation of the step-wise development of Virtual Proteomics Laboratory.

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    <p>Virtualization of proteomics data and experimental procedures from “bench-side” and storage in discrete compartments on the common “Virtual Lab server” for development of the course contents. Every experiment is explained in a step-by-step manner that follows the order of the tabs: theory, experimental procedure, simulator, video, download, assignment, quiz, references, and feedback. The server is connected to the Internet by a “LAN/WAN network” that contains the gateway portal and system firewall that protects the data from being changed by unauthorized people. The end users present on the “Client Side” can access the Virtual Lab via the LAN/WAN network portal. All course materials are freely available all over the world through the Internet and intended to be used in the teaching/learning experience particularly in universities and colleges. Moreover, the course content will be interesting and valuable for research labs working in the similar fields.</p

    Phomacins:  Three Novel Antitumor Cytochalasan Constituents Produced by a <i>Phoma</i> sp.

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    Three novel cytochalasans, phomacins A, B and C, were isolated from a fermentation broth of the fungus Phoma sp. and purified by HSCCC (high speed countercurrent chromatography) followed by HPLC. The structures were determined by 1D and 2D NMR techniques. All three compounds have shown potent inhibitory activity against the HT29 colonic adenocarcinoma cell line

    Table_1_Dickkopf Homolog 3 (DKK3) Acts as a Potential Tumor Suppressor in Gallbladder Cancer.XLSX

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    Gallbladder cancer (GBC) is a common malignancy of biliary tract cancers and its incidence has been rising rapidly worldwide. The prognosis for this disease is dismal as most of the symptoms are non-specific leading to a definitive diagnosis only at a late stage. Loss of DKK3 gene is associated with a possible tumor suppressor role in human cancers. The role and regulation of DKK3 in GBC have not been studied. We found that DKK3 expression levels were low in GBC patients and cell lines. Treatment of GBC cell lines with demethylating agent 5-Aza- 2'-deoxycytidine enhances its expression, establishing impact of methylation on DKK3 expression. We observed low expression of DKK3 in gallbladder adenocarcinoma tumors and highly invasive GBC cell lines. We showed that overexpression of DKK3 can decrease cell invasion, proliferation, and colony forming ability of GBC cells. Our data thus demonstrated the DKK3 gene is a potential tumor suppressor gene in GBC and aberrant promoter methylation could be involved in its downregulation, which may play a role in the tumorigenesis and aggressiveness of GBC.</p

    Additional file 5: Figure S3. of Weight control interventions improve therapeutic efficacy of dacarbazine in melanoma by reversing obesity-induced drug resistance

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    Effect of inhibition of FASN, Cav-1, and P-gp on response of B16F1 cells to DTIC. B16F1 cells were chronically grown in medium containing 5% serum collected from experimental ND or HFD C57BL/6J mice for 15 days. Thereafter, these cells were subjected to long-term survival assay. First, cells were treated with respective inhibitors followed by treatment of DTIC for 48 h. Then, the medium was changed and fresh medium was added. The medium was changed every 2–3 days. After 10 days, the cells were stained with 0.05% crystal violet and images were taken using Olympus digital camera. Data were quantitated using ImageJ software. The data are representative of experiments performed three times; Ceru or C = cerulenin; MCD or M = methyl β-cyclodextrin; Vera or V = verapamil. The results are given as means ± standard deviation; *, p < 0.05. (PDF 666 kb

    Additional file 3: Figure S1. of Weight control interventions improve therapeutic efficacy of dacarbazine in melanoma by reversing obesity-induced drug resistance

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    Effect of obesity-associated serum factors on the protein level of P-gp, Cav-1, and FASN in B16F1 cells. B16F1 cells were chronically grown in medium containing 5% serum collected from ND or HFD C57BL/6J mice for 15 days. Thereafter, these cells were subjected to immunofluorescence confocal staining of the indicated molecules. The data were recorded using Zeiss LSM510 META Confocal Microscope. (Scale bar = 20 μm). (PDF 189 kb

    Additional file 9: Figure S7. of Weight control interventions improve therapeutic efficacy of dacarbazine in melanoma by reversing obesity-induced drug resistance

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    MS analysis on the distribution of DTIC in tumors and organ samples collected from experimental ND or HFD mice. Lysates of tumors and organ samples from the experimental ND or HFD mice were prepared and subjected to liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI MS/MS). The spectrum shows protonated mass of DTIC at 183.0984, m/z and the product ions at m/z, 166.0733, 138.0396, and 123.0427 (similar fragmentation patterns were observed in tumors and tissue samples of mice treated with DTIC). The inset contains chemical structure of DTIC with the fragmentation patterns marked. All the MS data were collected in the presence of internal standards, where mass tolerance of DTIC was maintained well within 3 ppm. (PDF 122 kb
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