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<pubDate>Sat, 26 Jul 2008 17:07:30 BST</pubDate>


	<title>CiteULike: Author Bonetto</title>
	<description>CiteULike: Author Bonetto</description>


	<link>http://www.citeulike.org/author/Bonetto</link>
	<dc:publisher>CiteULike.org</dc:publisher>
	<dc:language>en-gb</dc:language>
	<dc:rights>Copyright &#169; 2004-2008 citeulike.org</dc:rights>
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        <rdf:li rdf:resource="http://www.citeulike.org/user/cartagema/article/3043369"/>
        <rdf:li rdf:resource="http://www.citeulike.org/user/dchen/article/2767692"/>
        <rdf:li rdf:resource="http://www.citeulike.org/user/austin987/article/1438309"/>
        <rdf:li rdf:resource="http://www.citeulike.org/user/Gehrke/article/431972"/>
        <rdf:li rdf:resource="http://www.citeulike.org/user/Gehrke/article/604924"/>
        <rdf:li rdf:resource="http://www.citeulike.org/user/Gehrke/article/333192"/>
        <rdf:li rdf:resource="http://www.citeulike.org/user/proportional/article/614294"/>

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<item rdf:about="http://www.citeulike.org/user/cartagema/article/3043369">
    <title>MedIGrid: A Medical Imaging Application for Computational Grids</title>
    <link>http://www.citeulike.org/user/cartagema/article/3043369</link>
    <description>&lt;i&gt;ipdps, Vol. 00 (2003)&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;In this work we describe MedIGrid, an application that enables nuclear doctors to transparently use high performance computers and storage systems for the PET/SPECT (Positron Emission Tomography/Single Photon Emission Computed Tomography) image processing, management, visualization and analysis. MedIGrid is the result of the joint efforts of a group of researchers committed to the development of a distributed application to test and deploy new reconstruction methods in clinical environments. In the following we describe how the collaboration among different research groups has contributed to the integration of the application into a single framework. The results of our work will be discussed.</description>
    <dc:title>MedIGrid: A Medical Imaging Application for Computational Grids</dc:title>

    <dc:creator>M Bertero</dc:creator>
    <dc:creator>P Bonetto</dc:creator>
    <dc:creator>L Carracciuolo</dc:creator>
    <dc:creator>L D'Amore</dc:creator>
    <dc:creator>A Formiconi</dc:creator>
    <dc:creator>MR Guarracino</dc:creator>
    <dc:creator>G Laccetti</dc:creator>
    <dc:creator>A Murli</dc:creator>
    <dc:creator>G Oliva</dc:creator>
    <dc:identifier>doi:10.1109/IPDPS.2003.1213457</dc:identifier>
    <dc:source>ipdps, Vol. 00 (2003)</dc:source>
    <dc:date>2008-07-25T18:02:55-00:00</dc:date>
    <prism:publicationYear>2003</prism:publicationYear>
    <prism:publicationName>ipdps</prism:publicationName>
    <prism:volume>00</prism:volume>
    <prism:publisher>IEEE Computer Society</prism:publisher>
    <prism:category>grid</prism:category>
    <prism:category>medical</prism:category>
    <prism:category>storage</prism:category>
</item>



<item rdf:about="http://www.citeulike.org/user/dchen/article/2767692">
    <title>Trapping an Intensely Bright, Stable Sonoluminescing Bubble</title>
    <link>http://www.citeulike.org/user/dchen/article/2767692</link>
    <description>&lt;i&gt;Physical Review Letters, Vol. 100, No. 7. (2008)&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;Previous works on single bubble sonoluminescence in sulfuric acid solutions have stressed the fact that the sonoluminescence (SL) emissions are the highest ever found, but at the same time the bubble moves in orbits. We have fixed the SL bubble spatially and at the same time we have reached higher SL emissions using another harmonic acoustic signal to produce the acoustic excitation. Multiple harmonic excitation produces up to a fourfold increase in SL emissions, reaching the peak value of about 40 &#181;W for a moving bubble and 15 &#181;W for a nonmoving bubble. The ability to have a bright stationary bubble also opens new research opportunities. In particular, we develop a new method to measure the absolute radius evolution of the bubble that exploits this stability.</description>
    <dc:title>Trapping an Intensely Bright, Stable Sonoluminescing Bubble</dc:title>

    <dc:creator>Ra&#250;l Urteaga</dc:creator>
    <dc:creator>Fabi&#225;n Bonetto</dc:creator>
    <dc:identifier>doi:10.1103/PhysRevLett.100.074302</dc:identifier>
    <dc:source>Physical Review Letters, Vol. 100, No. 7. (2008)</dc:source>
    <dc:date>2008-05-07T23:29:17-00:00</dc:date>
    <prism:publicationYear>2008</prism:publicationYear>
    <prism:publicationName>Physical Review Letters</prism:publicationName>
    <prism:volume>100</prism:volume>
    <prism:number>7</prism:number>
    <prism:publisher>APS</prism:publisher>
    <prism:category>2008</prism:category>
    <prism:category>bubbles</prism:category>
    <prism:category>cool</prism:category>
</item>



<item rdf:about="http://www.citeulike.org/user/austin987/article/1438309">
    <title>Radiotherapy-induced lymphocytopenia: changes in total lymphocyte count and in lymphocyte subpopulations under pelvic irradiation in gynecologic neoplasms.</title>
    <link>http://www.citeulike.org/user/austin987/article/1438309</link>
    <description>&lt;i&gt;Journal of biological regulators and homeostatic agents, Vol. 19, No. 3-4. (c 2005), pp. 153-158.&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;Lymphocytopenia is one of the most negative biological prognostic factors in cancer patients. Lymphocytopenia may depend on tumor progression, or on various anticancer therapies. In particular, radiotherapy (RT) may induce direct lymphocyte damage. The present study was carried out to evaluate the influence of pelvic irradiation on lymphocyte number and lymphocyte subpopulations in patients with gynecologic tumors. The study included 40 patients affected by locally limited or advanced uterine tumors, who underwent pelvic irradiation for a total dose of 50.4 Gy. RT induced a significant decline in total lymphocyte number, with values lower than 500/mm3 in 29/40 (73%) patients and with a mean decrease of 71 +/- 4%. In the same way, T lymphocyte, CD4, CD8 and NK cell mean numbers significantly decreased under RT. The decline in NK and CD8 cells was limited to the first 2-3 weeks of irradiation, whereas that involving T lymphocytes and CD4 cells was progressive and persistent until the end of RT. Finally, the decline in total lymphocyte number was significantly greater in patients who had no tumor regression in response to RT. This study confirms that pelvic RT may induce severe lymphocytopenia which could negatively influence the efficacy of RT itself.</description>
    <dc:title>Radiotherapy-induced lymphocytopenia: changes in total lymphocyte count and in lymphocyte subpopulations under pelvic irradiation in gynecologic neoplasms.</dc:title>

    <dc:creator>P Lissoni</dc:creator>
    <dc:creator>S Meregalli</dc:creator>
    <dc:creator>E Bonetto</dc:creator>
    <dc:creator>M Mancuso</dc:creator>
    <dc:creator>F Brivio</dc:creator>
    <dc:creator>M Colciago</dc:creator>
    <dc:creator>G Gardani</dc:creator>
    <dc:source>Journal of biological regulators and homeostatic agents, Vol. 19, No. 3-4. (c 2005), pp. 153-158.</dc:source>
    <dc:date>2007-07-05T20:19:53-00:00</dc:date>
    <prism:publicationYear>2005</prism:publicationYear>
    <prism:publicationName>Journal of biological regulators and homeostatic agents</prism:publicationName>
    <prism:issn>0393-974X</prism:issn>
    <prism:volume>19</prism:volume>
    <prism:number>3-4</prism:number>
    <prism:startingPage>153</prism:startingPage>
    <prism:endingPage>158</prism:endingPage>
    <prism:category>endometrial_cancer</prism:category>
    <prism:category>findthis</prism:category>
</item>



<item rdf:about="http://www.citeulike.org/user/Gehrke/article/431972">
    <title>Redox proteomics: identification of oxidatively modified proteins.</title>
    <link>http://www.citeulike.org/user/Gehrke/article/431972</link>
    <description>&lt;i&gt;Proteomics, Vol. 3, No. 7. (July 2003), pp. 1145-1153.&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;Reactive oxygen and nitrogen species may cause various types of chemical modifications on specific proteins, Such modifications if irreversible are often associated with permanent loss of function and may lead to the elimination or to the accumulation of the damaged proteins. Reversible modifications, particularly at the cysteine residues, may have a dual role of protection from cysteine irreversible oxidation and modulation of protein function (redox regulation). Here we will review the techniques available for identifying proteins based on their redox state. In particular, we will focus on protein carbonylation, tyrosine nitration and thiol-disulfide chemistry of cysteines, with special emphasis on glutathionylation, because these are the fields where the tools of proteome analysis have been applied.</description>
    <dc:title>Redox proteomics: identification of oxidatively modified proteins.</dc:title>

    <dc:creator>P Ghezzi</dc:creator>
    <dc:creator>V Bonetto</dc:creator>
    <dc:identifier>doi:10.1002/pmic.200300435</dc:identifier>
    <dc:source>Proteomics, Vol. 3, No. 7. (July 2003), pp. 1145-1153.</dc:source>
    <dc:date>2005-12-09T14:00:49-00:00</dc:date>
    <prism:publicationYear>2003</prism:publicationYear>
    <prism:publicationName>Proteomics</prism:publicationName>
    <prism:issn>1615-9853</prism:issn>
    <prism:volume>3</prism:volume>
    <prism:number>7</prism:number>
    <prism:startingPage>1145</prism:startingPage>
    <prism:endingPage>1153</prism:endingPage>
    <prism:category>introduction</prism:category>
</item>



<item rdf:about="http://www.citeulike.org/user/Gehrke/article/604924">
    <title>Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes.</title>
    <link>http://www.citeulike.org/user/Gehrke/article/604924</link>
    <description>&lt;i&gt;Proc Natl Acad Sci U S A, Vol. 99, No. 6. (19 March 2002), pp. 3505-3510.&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;Formation of mixed disulfides between glutathione and the cysteines of some proteins (glutathionylation) has been suggested as a mechanism through which protein functions can be regulated by the redox status. The aim of this study was to identify the proteins of T cell blasts that undergo glutathionylation under oxidative stress. To this purpose, we radiolabeled cellular glutathione with (35)S, exposed T cells to oxidants (diamide or hydrogen peroxide), and performed nonreducing, two-dimensional electrophoresis followed by detection of labeled proteins by phosphorimaging and their identification by mass spectrometry techniques. We detected several proteins previously not recognized to be glutathionylated, including cytoskeletal proteins (vimentin, myosin, tropomyosin, cofilin, profilin, and the already known actin), enzymes (enolase, aldolase, 6-phosphogluconolactonase, adenylate kinase, ubiquitin-conjugating enzyme, phosphoglycerate kinase, triosephosphate isomerase, and pyrophosphatase), redox enzymes (peroxiredoxin 1, protein disulfide isomerase, and cytochrome c oxidase), cyclophilin, stress proteins (HSP70 and HSP60), nucleophosmin, transgelin, galectin, and fatty acid binding protein. Based on the presence of several protein isoforms in control cells, we suggest that enolase and cyclophilin are heavily glutathionylated under basal conditions. We studied the effect of glutathionylation on some of the enzymes identified in the present study and found that some of them (enolase and 6-phosphogluconolactonase) are inhibited by glutathionylation, whereas the enzymatic activity of cyclophilin (peptidylprolyl isomerase) is not. These findings suggest that protein glutathionylation might be a common mechanism for the global regulation of protein functions.</description>
    <dc:title>Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes.</dc:title>

    <dc:creator>M Fratelli</dc:creator>
    <dc:creator>H Demol</dc:creator>
    <dc:creator>M Puype</dc:creator>
    <dc:creator>S Casagrande</dc:creator>
    <dc:creator>I Eberini</dc:creator>
    <dc:creator>M Salmona</dc:creator>
    <dc:creator>V Bonetto</dc:creator>
    <dc:creator>M Mengozzi</dc:creator>
    <dc:creator>F Duffieux</dc:creator>
    <dc:creator>E Miclet</dc:creator>
    <dc:creator>A Bachi</dc:creator>
    <dc:creator>J Vandekerckhove</dc:creator>
    <dc:creator>E Gianazza</dc:creator>
    <dc:creator>P Ghezzi</dc:creator>
    <dc:identifier>doi:10.1073/pnas.052592699</dc:identifier>
    <dc:source>Proc Natl Acad Sci U S A, Vol. 99, No. 6. (19 March 2002), pp. 3505-3510.</dc:source>
    <dc:date>2006-04-27T19:47:59-00:00</dc:date>
    <prism:publicationYear>2002</prism:publicationYear>
    <prism:publicationName>Proc Natl Acad Sci U S A</prism:publicationName>
    <prism:issn>0027-8424</prism:issn>
    <prism:volume>99</prism:volume>
    <prism:number>6</prism:number>
    <prism:startingPage>3505</prism:startingPage>
    <prism:endingPage>3510</prism:endingPage>
    <prism:category>introduction</prism:category>
</item>



<item rdf:about="http://www.citeulike.org/user/Gehrke/article/333192">
    <title>Thiol-disulfide balance: from the concept of oxidative stress to that of redox regulation.</title>
    <link>http://www.citeulike.org/user/Gehrke/article/333192</link>
    <description>&lt;i&gt;Antioxid Redox Signal, Vol. 7, No. 7-8. (g 2005), pp. 964-972.&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;Originally, small thiols, including glutathione, were viewed as protective antioxidants, acting as free radical scavengers in the context of oxidative damage. Recently, there is a growing literature showing that protein glutathionylation (formation of protein-glutathione mixed disulfides) and other forms of cysteine oxidation may be a means of redox regulation under physiological conditions. This review discusses the importance of protein oxidation in redox regulation in view of the recent data originating from the application of redox proteomics to identify redox-sensitive targets.</description>
    <dc:title>Thiol-disulfide balance: from the concept of oxidative stress to that of redox regulation.</dc:title>

    <dc:creator>P Ghezzi</dc:creator>
    <dc:creator>V Bonetto</dc:creator>
    <dc:creator>M Fratelli</dc:creator>
    <dc:identifier>doi:10.1089/ars.2005.7.964</dc:identifier>
    <dc:source>Antioxid Redox Signal, Vol. 7, No. 7-8. (g 2005), pp. 964-972.</dc:source>
    <dc:date>2005-09-27T17:29:04-00:00</dc:date>
    <prism:publicationYear>2005</prism:publicationYear>
    <prism:publicationName>Antioxid Redox Signal</prism:publicationName>
    <prism:issn>1523-0864</prism:issn>
    <prism:volume>7</prism:volume>
    <prism:number>7-8</prism:number>
    <prism:startingPage>964</prism:startingPage>
    <prism:endingPage>972</prism:endingPage>
    <prism:category>introduction</prism:category>
</item>



<item rdf:about="http://www.citeulike.org/user/proportional/article/614294">
    <title>A fluctuation theorem in a random environment</title>
    <link>http://www.citeulike.org/user/proportional/article/614294</link>
    <description>&lt;i&gt;(29 Apr 2006)&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;A simple class of chaotic systems in a random environment is considered and the fluctuation theorem is extended under the assumption of reversibility.</description>
    <dc:title>A fluctuation theorem in a random environment</dc:title>

    <dc:creator>F Bonetto</dc:creator>
    <dc:creator>G Gallavotti</dc:creator>
    <dc:creator>G Gentile</dc:creator>
    <dc:source>(29 Apr 2006)</dc:source>
    <dc:date>2006-05-05T08:07:45-00:00</dc:date>
    <prism:publicationYear>2006</prism:publicationYear>
    <prism:category>no-tag</prism:category>
</item>



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