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    <title>NOPR Collection:</title>
    <link>http://nopr.niscpr.res.in/handle/123456789/59861</link>
    <description />
    <pubDate>Mon, 12 Oct 2026 01:08:08 GMT</pubDate>
    <dc:date>2026-10-12T01:08:08Z</dc:date>
    <item>
      <title>Complete genome sequence and comparative analysis of antibiotic resistance plasmids in carbapenem-resistant Escherichia coli from bovine mastitis</title>
      <link>http://nopr.niscpr.res.in/handle/123456789/59871</link>
      <description>Title: Complete genome sequence and comparative analysis of antibiotic resistance plasmids in carbapenem-resistant Escherichia coli from bovine mastitis
Authors: Chopra, Meenu; Bandyopadhyay, Samiran; Bhattacharya, Debaraj; Singh, Anil Kumar; Singh, Ravi Kant; De, Sachinandan
Abstract: The present study illustrates plasmidome and resistome profile of two carbapenem-resistant Escherichia coli isolates from milk of two different cows with recurrent subclinical mastitis from semi-urban region of Kolkata, India. Both E.coli strains (IVRI KOL CP4 and CM IVRI KOL-1) were sequenced and subreads were de novo assembled. Genomeanalysis and gene prediction data revealed the presence of multi-resistance plasmids conferring resistance to β-lactams,sulphonamide, tetracycline, trimethoprim, aminoglycosides even to the last-resort drugs carbapenem in both the strains. Thestrain IVRI Kol CP4 carried 3 plasmids: a 92840 bp IncFII plasmid (CP034254) with blaTEM-1B, blaNDM-5, sul-1, dfra12,rmtB, aadA2 genes; a 50882 bp IncI plasmid (CP034255) with blaCMY-42 gene and a 28652 bp undermined replicon typeplasmid (CP034256) having blaTEM-1B, mphA and tet(A) genes. Other strain CM IVRI Kol-1 also had 3 plasmids: a146286 bp IncFIA plasmid (CP033159) with blaTEM-1B, blaNDM-5, mph(A), sul1, tet(A), dfra12, rmtB, aadA2,and TetR genes; a 62055 bp IncI plasmid (CP033160) with two copy of blaCMY-42 and a 6346 bp plasmid (CP033161) ofunknown replicon type. Additionally, two plasmids (CP034254 and CP033159) harboured dfra12-aadA2 gene cassette inthe variable region of int1 conferring resistance to trimethoprim and aminoglycoside. We compare our five plasmidsequences with publicly available data to know the evolutionary picture of how multiple drug resistant (MDR) evolutionoccurs across the plasmids from different locations. This first-ever study on the whole genome sequence of NDM-5producing E. coli from bovine milk in India highlights the role of IncF type plasmid as a common vehicle for the carriageand spread of NDM-5 gene in food animals.
Page(s): 113-123</description>
      <pubDate>Thu, 01 Apr 2021 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://nopr.niscpr.res.in/handle/123456789/59871</guid>
      <dc:date>2021-04-01T00:00:00Z</dc:date>
    </item>
    <item>
      <title>Quantitative proteomics identified lncRNA HOTAIR regulated nucleoproteins in HeLa cells</title>
      <link>http://nopr.niscpr.res.in/handle/123456789/59870</link>
      <description>Title: Quantitative proteomics identified lncRNA HOTAIR regulated nucleoproteins in HeLa cells
Authors: Zheng, Peng; Liu, Cheng Lin Zi; Hu, Fan; Chen, Zhuo; Zhang, Tong-cun
Abstract: Hox transcript antisense intergenic RNA (HOTAIR), which was called oncogenic long non-coding RNA (lncRNA) over&#xD;
expressed in the vast majority of cancer types, regulated various biological processes such as cell growth, apoptosis,&#xD;
proliferation and metastasis. It can regulate hundreds of genes via recruiting complexes: polycomb repressive complex 2&#xD;
(PRC2) and lysine specific demethylase 1 (LSD1). At that, majority processes happened in nucleic. However, there are no&#xD;
reports to comprehensively research the regulated protein of HOTAIR in nucleic, which is important for explore the mechanism&#xD;
of HOTAIR functions. In this study, we employed a quantitative proteomics analysis of HOTAIR regulated nucleoproteins in&#xD;
cancer cells. Bioinformatical analysis, such as PANTHER, STRING, DAVID were used to understand the function and&#xD;
relationship of these nucleoproteins. In total, we found that 224 nucleoproteins were differential expressed after inhibition&#xD;
HOTAIR, implying that they could be potential targets of HOTAIR. Western blotting analysis, which was used to validation of&#xD;
the quantitative proteomics data, was consistent with stable isotope labelling by amino acids in cell culture (SILAC)&#xD;
experiments. Bioinformatic analysis shown that major changes in nucleoproteins involved in diverse protein class, including the&#xD;
nucleic acid binding and cytoskeletal proteins. Further functional studies of proliferating cell nuclear antigen (PCNA) revealed&#xD;
that various phenotypic effects observed after HOTAIR inhibition, at least in part, through the regulation of PCNA expression.&#xD;
By correlating the proteomic data with these functional studies, the current results provide novel insights into the mechanism&#xD;
underlying HOTAIR functions in cancer cells.
Page(s): 124-137</description>
      <pubDate>Thu, 01 Apr 2021 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://nopr.niscpr.res.in/handle/123456789/59870</guid>
      <dc:date>2021-04-01T00:00:00Z</dc:date>
    </item>
    <item>
      <title>Expression, purification and antimicrobial activity analysis of recombination peptide subtilosin A in Escherichia coli using SUMO fusion technology</title>
      <link>http://nopr.niscpr.res.in/handle/123456789/59869</link>
      <description>Title: Expression, purification and antimicrobial activity analysis of recombination peptide subtilosin A in Escherichia coli using SUMO fusion technology
Authors: Lu, Xuan; Hu, Shimeng; Li, Qiaohong; Song, Xia; Zhou, Li; Wang, Yefu
Abstract: Subtilosin A is an antimicrobial peptide isolated from Bacillus subtilis, and it possess broad-spectrum antibacterial&#xD;
activity. As subtilosin A prevents biofilm formation by inhibiting bacterial quorum sensing processes against Gram-positive,&#xD;
Gram-negative, and Gram-variable bacteria, it is urgent to obtain high-quality subtilosin A production in an economical and&#xD;
effective way. Escherichia coli is undoubtedly a most preferred host system for production of heterologous recombinant&#xD;
proteins. However, subtilosin A has the inhibitory effects against E. coli and it is easily to be degraded. To produce&#xD;
subtilosin A in E. coli, the application of small ubiquitin-related modifier (SUMO) fusion system with the purpose of&#xD;
stability and prevention of antimicrobial activity is the best practices in this regard. In this study, subtilosin A gene with&#xD;
codon optimization was cloned into the Stu I/Hind III sites of pSUMO vector after SUMO tag and transformed to&#xD;
E. coli BL21 (DE3). The SUMO-subtilosin A fusion protein was induced at 15ºC for 16 hours with 0.5 mM isopropyl&#xD;
thio-β-D- galactoside (IPTG) induction. The fusion protein with a molecular weight of approximately 20 kDa was confirmed&#xD;
by SDS-PAGE. The subtilosin A was then released by SUMO protease cleavage at the junction site and isolated and purified&#xD;
by affinity and cation exchange chromatography. The recombinant subtilosin A demonstrated a good antibacterial activity&#xD;
against Pseudomonas aeruginosa (Gram-negative bacteria) and Staphylococcus aureus (Gram-positive bacteria), with&#xD;
minimum inhibitory concentrations (MICs) of 100 mg/L and 100 mg/L, respectively. These results showed an efficient&#xD;
method for synthesis functional subtilosin A.
Page(s): 138-144</description>
      <pubDate>Thu, 01 Apr 2021 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://nopr.niscpr.res.in/handle/123456789/59869</guid>
      <dc:date>2021-04-01T00:00:00Z</dc:date>
    </item>
    <item>
      <title>Purification and characterization of tyrosinase from Streptomyces vinceudrauppus DSV 5</title>
      <link>http://nopr.niscpr.res.in/handle/123456789/59868</link>
      <description>Title: Purification and characterization of tyrosinase from Streptomyces vinceudrauppus DSV 5
Authors: S, Shivaveerakumar; Agsar, Dayanand
Abstract: Streptomyces vinceudrauppus DSV 5 is the first investigated report for tyrosinase activity. The studies presented in this research show that this organism may be a future source for larger production of tyrosinase. The enzyme was purified initially with 140 ml of culture filtrate. The crude enzyme was primarily purified by centrifugation, followed by ammonium sulfate precipitation and ultrafiltration and employed to ion exchange chromatography. Thereafter, the enzyme was loaded on a Sephadex G-75 column and, after ultra filtration, 0.54 mg of purified tyrosinase were obtained and confirmed results from sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Tyrosinase kinetics was determined with L-DOPA as substrate, the kinetic parameters are Km - 0.17 mM and Vmax - 227 IU/ml were determined.
Page(s): 145-153</description>
      <pubDate>Thu, 01 Apr 2021 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://nopr.niscpr.res.in/handle/123456789/59868</guid>
      <dc:date>2021-04-01T00:00:00Z</dc:date>
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