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  <title>NOPR Collection:</title>
  <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/31255" />
  <subtitle />
  <id>http://nopr.niscpr.res.in/handle/123456789/31255</id>
  <updated>2026-10-12T09:00:04Z</updated>
  <dc:date>2026-10-12T09:00:04Z</dc:date>
  <entry>
    <title>Serum neuron-specific enolase and S-100β levels as prognostic follow-up markers for oxygen administered carbon monoxide intoxication cases</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/31270" />
    <author>
      <name>Yildirim, Ali Osman</name>
    </author>
    <author>
      <name>Eroglu, Murat</name>
    </author>
    <author>
      <name>Kaldirim, Umit</name>
    </author>
    <author>
      <name>Eyi, Yusuf Emrah</name>
    </author>
    <author>
      <name>Simsek, Kemal</name>
    </author>
    <author>
      <name>Durusu, Murat</name>
    </author>
    <author>
      <name>Yamanel, Levent</name>
    </author>
    <author>
      <name>Arziman, Ibrahim</name>
    </author>
    <author>
      <name>Tuncer, Salim Kemal</name>
    </author>
    <author>
      <name>Toygar, Mehmet</name>
    </author>
    <author>
      <name>Balkan, Arzu</name>
    </author>
    <author>
      <name>Cayci, Tuncer</name>
    </author>
    <author>
      <name>Demirbas, Seref</name>
    </author>
    <author>
      <name>Oter, Sukru</name>
    </author>
    <author>
      <name>Bilgi, Cumhur</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/31270</id>
    <updated>2016-07-20T05:09:59Z</updated>
    <published>2015-02-01T00:00:00Z</published>
    <summary type="text">Title: Serum neuron-specific enolase and S-100β levels as prognostic follow-up markers for oxygen administered carbon monoxide intoxication cases
Authors: Yildirim, Ali Osman; Eroglu, Murat; Kaldirim, Umit; Eyi, Yusuf Emrah; Simsek, Kemal; Durusu, Murat; Yamanel, Levent; Arziman, Ibrahim; Tuncer, Salim Kemal; Toygar, Mehmet; Balkan, Arzu; Cayci, Tuncer; Demirbas, Seref; Oter, Sukru; Bilgi, Cumhur
Abstract: Serum neuron-specific&#xD;
enolase (NSE) and S-100β levels are considered novel biochemical markers of&#xD;
neuronal cell injury. In this study,&lt;b style="mso-bidi-font-weight:normal"&gt; &lt;/b&gt;the&#xD;
initial and post-treatment levels of NSE and S-100β were compared in carbon&#xD;
monoxide (CO) poisoning patients, who received normorbaric oxygen (NBO) or&#xD;
hyperbaric oxygen (HBO) therapy. Forty consecutive patients with acute CO&#xD;
poisoning&lt;b style="mso-bidi-font-weight:normal"&gt; &lt;/b&gt;were enrolled in this &lt;span style="mso-bidi-font-weight:bold"&gt;prospective, observational study.&#xD;
According to their clinical symptoms and observations, twenty patients were&#xD;
treated with NBO, and the other twenty with HBO. Serum S-100β and NSE levels&#xD;
were measured both at time of admission and 6 h later (post-treatment).&#xD;
Serum NSE and S-100β values decreased significantly in both of the therapeutic&#xD;
modalities. The initial and post-treatment values of NSE and S-100β in NBO or&#xD;
HBO patients were comparable. A clear negative correlation was observed between&#xD;
the decrease of NSE and &#xD;
S-100β levels and initial blood carboxyhemoglobin levels. In conclusion, the&#xD;
present results suggested the use of serum &#xD;
S-100β and NSE levels as indicators for brain injury. Due to the significant&#xD;
increase of their values with oxygen therapy, they may also be useful as&#xD;
prognostic follow-up markers. However, the current findings reflected no&#xD;
difference between the efficacy of NBO or HBO therapy.&#xD;
&#xD;
&lt;/span&gt;
Page(s): 29-33</summary>
    <dc:date>2015-02-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Rapid and simple method of photobleaching to reduce background autofluorescence in lung tissue sections</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/31269" />
    <author>
      <name>Kumar, B Santhosh</name>
    </author>
    <author>
      <name>Sandhyamani, S</name>
    </author>
    <author>
      <name>Nazeer, Shaiju S</name>
    </author>
    <author>
      <name>Jayasree, R S</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/31269</id>
    <updated>2016-07-20T05:09:05Z</updated>
    <published>2015-02-01T00:00:00Z</published>
    <summary type="text">Title: Rapid and simple method of photobleaching to reduce background autofluorescence in lung tissue sections
Authors: Kumar, B Santhosh; Sandhyamani, S; Nazeer, Shaiju S; Jayasree, R S
Abstract: Autofluorescence&#xD;
exhibited by tissues often interferes with immunofluorescence. Using imaging&#xD;
and spectral analysis, we observed remarkable reduction of autofluorescence of&#xD;
formalin fixed paraffin embedded tissues irradiated with light prior to&#xD;
incubation with immunofluorescent dyes. The technique of photobleaching offers&#xD;
significant improvement in the quality and specificity of immunofluorescence.&#xD;
This has the potential for better techniques for disease diagnosis.
Page(s): 107-110</summary>
    <dc:date>2015-02-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Evaluation of different protein extraction methods for banana (&lt;i&gt;Musa&lt;/i&gt; spp.) root proteome analysis by two-dimensional electrophoresis</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/31268" />
    <author>
      <name>Vaganan, M Mayil</name>
    </author>
    <author>
      <name>Sarumathi, S</name>
    </author>
    <author>
      <name>Nandakumar, A</name>
    </author>
    <author>
      <name>Ravi, I</name>
    </author>
    <author>
      <name>Mustaffa, M M</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/31268</id>
    <updated>2016-07-20T05:07:04Z</updated>
    <published>2015-02-01T00:00:00Z</published>
    <summary type="text">Title: Evaluation of different protein extraction methods for banana (&lt;i&gt;Musa&lt;/i&gt; spp.) root proteome analysis by two-dimensional electrophoresis
Authors: Vaganan, M Mayil; Sarumathi, S; Nandakumar, A; Ravi, I; Mustaffa, M M
Abstract: Four protocols &lt;i style="mso-bidi-font-style:&#xD;
normal"&gt;viz&lt;/i&gt;., the trichloroacetic acid-acetone (TCA), phenol-ammonium&#xD;
acetate (PAA), phenol/SDS-ammonium acetate (PSA) and trisbase-acetone (TBA)&#xD;
were evaluated with modifications for protein extraction from banana (Grand&#xD;
Naine) roots, considered as recalcitrant tissues for proteomic analysis. The &lt;span style="mso-bidi-font-weight:bold"&gt;two-dimensional electrophoresis&lt;span style="mso-bidi-font-weight:bold"&gt; (2-DE) separated proteins were&#xD;
compared based on protein yield, number of resolved proteins, sum of spot&#xD;
quantity, average spot intensity and proteins resolved in 4-7 p&lt;i style="mso-bidi-font-style:normal"&gt;I&lt;/i&gt; range. The PAA protocol yielded more&#xD;
proteins (0.89 mg/g of tissues) and protein spots (584) in 2-DE gel than TCA&#xD;
and other protocols. Also, the PAA protocol was superior in terms of sum of&#xD;
total spot quantity and average spot intensity than TCA and other protocols,&#xD;
suggesting phenol as extractant and ammonium acetate as precipitant of proteins&#xD;
were the most suitable for banana rooteomics analysis by 2-DE. In addition, 1:3&#xD;
ratios of root tissue to extraction buffer and overnight protein precipitation&#xD;
were most efficient to obtain maximum protein yield.&#xD;
&#xD;
&lt;/span&gt;&lt;/span&gt;
Page(s): 101-106</summary>
    <dc:date>2015-02-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>&lt;i style="mso-bidi-font-style:normal"&gt;&lt;span style="font-size:11.0pt;mso-bidi-font-size:10.0pt;font-family:"Times New Roman"; mso-fareast-font-family:"Times New Roman";mso-bidi-font-family:"Times New Roman"; mso-ansi-language:EN-GB;mso-fareast-language:EN-US;mso-bidi-language:AR-SA" lang="EN-GB"&gt;In silico&lt;/span&gt;&lt;/i&gt;&lt;span style="font-size:11.0pt;mso-bidi-font-size: 10.0pt;font-family:"Times New Roman";mso-fareast-font-family:"Times New Roman"; mso-bidi-font-family:"Times New Roman";mso-ansi-language:EN-GB;mso-fareast-language: EN-US;mso-bidi-language:AR-SA" lang="EN-GB"&gt; structural and functional analysis of protein encoded by wheat early salt-stress response gene (WESR3)&lt;/span&gt;</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/31267" />
    <author>
      <name>Mishra, A K</name>
    </author>
    <author>
      <name>Tandon, Gitanjali</name>
    </author>
    <author>
      <name>Sharma, Rajendra</name>
    </author>
    <author>
      <name>Chandrasekharan, H</name>
    </author>
    <author>
      <name>Pandey, P S</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/31267</id>
    <updated>2016-07-20T05:05:24Z</updated>
    <published>2015-02-01T00:00:00Z</published>
    <summary type="text">Title: &lt;i style="mso-bidi-font-style:normal"&gt;&lt;span style="font-size:11.0pt;mso-bidi-font-size:10.0pt;font-family:"Times New Roman"; mso-fareast-font-family:"Times New Roman";mso-bidi-font-family:"Times New Roman"; mso-ansi-language:EN-GB;mso-fareast-language:EN-US;mso-bidi-language:AR-SA" lang="EN-GB"&gt;In silico&lt;/span&gt;&lt;/i&gt;&lt;span style="font-size:11.0pt;mso-bidi-font-size: 10.0pt;font-family:"Times New Roman";mso-fareast-font-family:"Times New Roman"; mso-bidi-font-family:"Times New Roman";mso-ansi-language:EN-GB;mso-fareast-language: EN-US;mso-bidi-language:AR-SA" lang="EN-GB"&gt; structural and functional analysis of protein encoded by wheat early salt-stress response gene (WESR3)&lt;/span&gt;
Authors: Mishra, A K; Tandon, Gitanjali; Sharma, Rajendra; Chandrasekharan, H; Pandey, P S
Abstract: Salt stress is&#xD;
one of the major abiotic stresses limiting grain yield in wheat (&lt;i&gt;Triticum&#xD;
aestivum &lt;/i&gt;&lt;span style="mso-bidi-font-style:italic"&gt;L.)&lt;i&gt;.&lt;/i&gt; Wheat&#xD;
early salt-stress response gene (&lt;i style="mso-bidi-font-style:normal"&gt;WESR3&lt;/i&gt;)&#xD;
is one of the major salt stress genes, which is affected in the first phase of&#xD;
salt stress. In this study, sequence and structural analysis of protein coded&#xD;
by &lt;i style="mso-bidi-font-style:normal"&gt;WESR3 &lt;/i&gt;gene was carried out using&#xD;
various bioinformatics tools. Sequence analysis of WESR3 protein revealed the presence&#xD;
of highly conserved regions of &lt;i style="mso-bidi-font-style:normal"&gt;Mlo&lt;/i&gt;&#xD;
gene family. Three-dimensional modeling was carried out to elucidate its&#xD;
structure and its active site. The sequence analysis revealed that WESR3&#xD;
protein might be involved in fungal pathogen attack pathway. Thus, in addition&#xD;
to its involvement in abiotic stresses, it also seemed to play an important&#xD;
part in biotic stress pathways. Out of the three modeled protein structures&#xD;
obtained from I-TASSER, HHPred and QUARK, the I-TASSER protein model was the&#xD;
best model based on high confidence score and lesser number of bad contacts.&#xD;
The Ramchandran plot analysis also showed that all amino acid residues of&#xD;
I-TASSER model lie in the allowed region and thus indicating towards the&#xD;
overall good quality of the predicted model. Seventeen active sites were&#xD;
predicted in the protein bearing resemblance to the Mlo family conserved&#xD;
regions. In conclusion, a detailed analysis of WESR3 protein suggested an&#xD;
important role of WESR3 in biotic and abiotic stress. These results aid&#xD;
to the experimental data and help to build up a complete view of WESR3 proteins&#xD;
and their role in plant stress response. &#xD;
&#xD;
&lt;/span&gt;
Page(s): 95-100</summary>
    <dc:date>2015-02-01T00:00:00Z</dc:date>
  </entry>
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