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    <title>DSpace Community:</title>
    <link>http://10.9.150.37:8080/dspace//handle/atmiyauni/273</link>
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    <pubDate>Mon, 27 Apr 2026 20:13:16 GMT</pubDate>
    <dc:date>2026-04-27T20:13:16Z</dc:date>
    <item>
      <title>Abrus precatorious: A review from ethno to nano application</title>
      <link>http://10.9.150.37:8080/dspace//handle/atmiyauni/2270</link>
      <description>Title: Abrus precatorious: A review from ethno to nano application
Authors: Joshi, Preetam</description>
      <pubDate>Tue, 01 Jan 2019 00:00:00 GMT</pubDate>
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      <dc:date>2019-01-01T00:00:00Z</dc:date>
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    <item>
      <title>Screening of Endophytic Actinomycetes for Cellulose Degradation</title>
      <link>http://10.9.150.37:8080/dspace//handle/atmiyauni/2269</link>
      <description>Title: Screening of Endophytic Actinomycetes for Cellulose Degradation
Authors: Ranjan, Ravi
Abstract: Actinomycetes or Actinobacteria are Gram positive, filamentous, spore forming ahigh GC containing(60-75% in their DNA) prokaryotes. Endophytic Actinomycetes are the microbes living in the inner part of plant tissues and important for production of the bioactive molecules. Much of the work on these group were restricted on antibiotic potentiality. In the present study an exploration was carried out with the available six endophytic isolates (from Dept of Biotechnology, Atmiya University Rajkot)for cellulase synthesis by primary Screening and secondary screening. Three types cellulase activity (Endoglucanase0.368IUat72h, FPase-0.06IU at 96hand cellobiase-0.321 IU at 96 h ) of incubation periodwere found to be recorded by employing the strain Nocardiopsis alba EA23 Important morphological, biochemical &amp; physiological identification at preliminary level found to reveal both branched and un branched type of actinomycetes whose genus and species identification yet under progress.</description>
      <pubDate>Fri, 01 May 2020 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://10.9.150.37:8080/dspace//handle/atmiyauni/2269</guid>
      <dc:date>2020-05-01T00:00:00Z</dc:date>
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    <item>
      <title>Controlled release of sulfasalazine loaded amidated pectin microparticles through Eudragit S 100 coated capsule for management of inflammatory bowel disease</title>
      <link>http://10.9.150.37:8080/dspace//handle/atmiyauni/2254</link>
      <description>Title: Controlled release of sulfasalazine loaded amidated pectin microparticles through Eudragit S 100 coated capsule for management of inflammatory bowel disease
Authors: Shukla, Rishikesh; Deshmukh, Rohitas; Harwans, Ranjit K.; Paul, Swarnali Das
Abstract: Inflammatory bowel disease (IBD) is a common colonic disorder affecting most of the world population. In order to overcome the IBD, present study was aimed to fabricate the sulfasalazine loaded amidated pectin microparticles by ionic gelation technique. The microparticles were filled in Eudragit S 100 coated hard gelatin capsules for pH and time dependent drug delivery to the colon especially for the treatment of IBD. The effects of variables such as concentration of crosslinking agent (calcium chloride) and amidated pectin-sulfasalazine ratio were optimized through the particle size, zeta potential, % yield, encapsulation efficiency (% EE), swelling index and in vitro drug release. The optimized formulation, F4 exhibited average particle size (463.33 ± 6.72 μm), zeta potential (−32.10 ± 0.80 mV), yield (91.62 ± 1.97%) and EE (95.62 ± 1.21%). The significant swelling index, 0.88 ± 0.02 θ and 0.98 ± 0.03 θ was achieved with F4 at pH 6.8 and pH 7.4 respectively. The F4 showed maximum drug release (91.12 ± 5.11%) in simulated colonic fluid (SCF, pH 7.4) and 98.07 ± 3.92% (P &lt; 0.05) in rat cecal content (RCC, pH 7.4) for 24 h in a sustained manner. It may be due to the drug released through polymer by diffusion-matrix erosion and bacterial degradation of the microparticles. The F4 formulation displayed non-Fickian pattern of drug release. In vivo study in rabbits confirmed that the enteric polymer coated capsule dissolve at colonic pH 7.4 to release the drug from microparticles. The F4 exhibited remarkable stability at room temperature and shelf-life was found to be 3.3 years. Thus, the sulfasalazine loaded amidated pectin microparticles filled in Eudragit S 100 coated hard gelatin capsule was found to be a potential delivery system for management of IBD.</description>
      <pubDate>Wed, 01 Jan 2020 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://10.9.150.37:8080/dspace//handle/atmiyauni/2254</guid>
      <dc:date>2020-01-01T00:00:00Z</dc:date>
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    <item>
      <title>The Collagen-Modifying Enzyme PLOD2 Is Induced and Required during L1-Mediated Colon Cancer Progression</title>
      <link>http://10.9.150.37:8080/dspace//handle/atmiyauni/2248</link>
      <description>Title: The Collagen-Modifying Enzyme PLOD2 Is Induced and Required during L1-Mediated Colon Cancer Progression
Authors: Kumar, Anmol; Gavert, Nancy; Brabletz, Thomas; Cheriyamundath, Sanith
Abstract: The overactivation of Wnt/β-catenin signaling is a hallmark of colorectal cancer (CRC) development. We identified the cell adhesion molecule L1CAM (L1) as a target of β-catenin-TCF transactivation in CRC cells. The overexpression of L1 in CRC cells confers enhanced proliferation, motility, tumorigenesis and liver metastasis, and L1 is exclusively localized in the invasive areas of human CRC tissue. A number of genes are induced after L1 transfection into CRC cells by a mechanism involving the cytoskeletal protein ezrin and the NF-κB pathway. When studying the changes in gene expression in CRC cells overexpressing L1 in which ezrin levels were suppressed by shRNA to ezrin, we discovered the collagen-modifying enzyme lysyl hydroxylase 2 (PLOD2) among these genes. We found that increased PLOD2 expression was required for the cellular processes conferred by L1, including enhanced proliferation, motility, tumorigenesis and liver metastasis, since the suppression of endogenous PLOD2 expression, or its enzymatic activity, blocked the enhanced tumorigenic properties conferred by L1. The mechanism involved in increased PLOD2 expression by L1 involves ezrin signaling and PLOD2 that affect the SMAD2/3 pathway. We found that PLOD2 is localized in the colonic crypts in the stem cell compartment of the normal mucosa and is found at increased levels in invasive areas of the tumor and, in some cases, throughout the tumor tissue. The therapeutic strategies to target PLOD2 expression might provide a useful approach for CRC treatment</description>
      <pubDate>Fri, 01 Jan 2021 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://10.9.150.37:8080/dspace//handle/atmiyauni/2248</guid>
      <dc:date>2021-01-01T00:00:00Z</dc:date>
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