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Prediction of Substrates for Glutathione Transferases by Covalent Docking

Guang Qiang Dong, Sara Calhoun, Hao Fan, Chakrapani Kalyanaraman, Megan C. Branch, Susan T. Mashiyama, Nir London, Matthew P. Jacobson, Patricia C. Babbitt, Brian K. Shoichet, Richard N. Armstrong, Andrej Sali
<span title="2014-05-16">2014</span> <i title="American Chemical Society (ACS)"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/uilc246nrbhffhjy3flluhazbi" style="color: black;">Journal of Chemical Information and Modeling</a> </i> &nbsp;
Enzymes in the glutathione transferase (GST) superfamily catalyze the conjugation of glutathione (GSH) to electrophilic substrates.  ...  Although virtual screening has been used widely to discover substrates by docking potential noncovalent ligands into active site clefts of enzymes, docking has been rarely constrained by a covalent bond  ...  ■ INTRODUCTION The canonical glutathione transferases (also known as GSTs; EC 2.5.1.18) catalyze addition of an excellent nucleophile to an electrophilic center.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1021/ci5001554">doi:10.1021/ci5001554</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/24802635">pmid:24802635</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC4068255/">pmcid:PMC4068255</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/vsbc3wsbqje5taqapmw2htu7iy">fatcat:vsbc3wsbqje5taqapmw2htu7iy</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200209233246/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC4068255&amp;blobtype=pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/ea/29/ea298c58e088104977bba26c5b647902ece203b1.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1021/ci5001554"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> acs.org </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4068255" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase π

Luis A. Ralat, Roberta F. Colman
<span title="2009-01-01">2009</span> <i title="Wiley"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/6bubxfqklvdwthsc43yvjbtjae" style="color: black;">Protein Science</a> </i> &nbsp;
Monobromobimane (mBBr), functions as a substrate of porcine glutathione S-transferase (GST ): The enzyme catalyzes the reaction of mBBr with glutathione.  ...  These results support the concept that glutathione S-transferase accomplishes its ability to react with a diversity of substrates in part by harboring distinct xenobiotic substrate sites.  ...  Hearne for the gift of glutathione-bimane, Dr. Yu-Chu Huang for performing the peptide sequencing, and Dr. John Dykins for help with the mass spectrometry.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1110/ps.03249303">doi:10.1110/ps.03249303</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/14573868">pmid:14573868</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC2366952/">pmcid:PMC2366952</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/a6vor3qzofagfe6uaqny4nnata">fatcat:a6vor3qzofagfe6uaqny4nnata</a> </span>
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The Interaction of Human Glutathione Transferase GSTA1-1 with Reactive Dyes

Mohammed Hamed Alqarni, Ahmed Ibrahim Foudah, Magdy Mohamed Muharram, Nikolaos E. Labrou
<span title="2021-04-20">2021</span> <i title="MDPI AG"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/dstyyzbt45gknhqqjsh45p55h4" style="color: black;">Molecules</a> </i> &nbsp;
Human glutathione transferase A1-1 (hGSTA1-1) contributes to developing resistance to anticancer drugs and, therefore, is promising in terms of drug-design targets for coping with this phenomenon.  ...  The present study results suggest that PBMX-R is a useful probe suitable for assessing by kinetic means the drugability of the enzyme in future drug-design efforts.  ...  The Identification of hGSTA1-1 Residue Was Modified by PBMX-R A molecular docking study was employed to predict the binding site of the PBMX-R.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.3390/molecules26082399">doi:10.3390/molecules26082399</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/33924269">pmid:33924269</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC8074892/">pmcid:PMC8074892</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/krwbsa5wqbgbbgtdo6hbu2ps3i">fatcat:krwbsa5wqbgbbgtdo6hbu2ps3i</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20210422040127/https://res.mdpi.com/d_attachment/molecules/molecules-26-02399/article_deploy/molecules-26-02399-v2.pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/32/3d/323d500779829565a5a90b947f52e2a15c66bc0e.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.3390/molecules26082399"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="unlock alternate icon" style="background-color: #fb971f;"></i> mdpi.com </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8074892" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

Glutathione transferase-P1-1 binding with naturally occurring ligands: assessment by docking simulations

Anupam J. Das, Sreeda Chalil, Poonam Nigam, Pamela Magee, Omar Janneh, Richard Owusu-Apenten
<span title="">2011</span> <i title="Scientific Research Publishing, Inc,"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/qbfz3tb7fbftxal477aoqh6rmq" style="color: black;">Journal of Biophysical Chemistry</a> </i> &nbsp;
Glutathione transferase-P1-1 (hGSTP1-1), which is associated with acquired drug resistance in some tumour cells, requires two identical subunits for full activity.  ...  Simulations were performed with commercial docking software and with GST monomer or dimer as template. Docking results using hGSTP1-1 dimer showed one binding site for most of the ligands tested.  ...  of human glutathione transferase P1-1 (hGSTp1-1).  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.4236/jbpc.2011.24046">doi:10.4236/jbpc.2011.24046</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/zkx5saobv5a3xedosso3a3kduy">fatcat:zkx5saobv5a3xedosso3a3kduy</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20150227224136/http://www.scirp.org/journal/PaperDownload.aspx?DOI=10.4236/jbpc.2011.24046" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/37/80/3780be6088866682729d4b2d56d924e2682457e1.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.4236/jbpc.2011.24046"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="unlock alternate icon" style="background-color: #fb971f;"></i> Publisher / doi.org </button> </a>

Covalent Docking Predicts Substrates for Haloalkanoate Dehalogenase Superfamily Phosphatases

Nir London, Jeremiah D. Farelli, Shoshana D. Brown, Chunliang Liu, Hua Huang, Magdalena Korczynska, Nawar F. Al-Obaidi, Patricia C. Babbitt, Steven C. Almo, Karen N. Allen, Brian K. Shoichet
<span title="2015-01-05">2015</span> <i title="American Chemical Society (ACS)"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/4qyryvw5mvde5nt6xjruewxve4" style="color: black;">Biochemistry</a> </i> &nbsp;
For one of those cases, a covalent docking prediction, confirmed by empirical screening, and combined with genomic context analysis, suggested the identity of the enzyme that catalyzes the orphan phosphatase  ...  In comparison, noncovalent docking of high-energy intermediates yielded nonproductive poses. In prospective predictions against seven enzymes, a substrate was identified for five.  ...  While covalent docking was used in the past retrospectively to predict substrates of glutathione transferases 33 and predict the chain length of polyprenyl transferases substrates, 34 to our knowledge  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1021/bi501140k">doi:10.1021/bi501140k</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/25513739">pmid:25513739</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC4303301/">pmcid:PMC4303301</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/gymfgaiznrevzdzpz5o7flgjde">fatcat:gymfgaiznrevzdzpz5o7flgjde</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200208073228/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC4303301&amp;blobtype=pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/03/ef/03efe4d94d8ad3805f3a568216249895ea46a4a3.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1021/bi501140k"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> acs.org </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4303301" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

Theory and Applications of Covalent Docking in Drug Discovery: Merits and Pitfalls

Hezekiel Kumalo, Soumendranath Bhakat, Mahmoud Soliman
<span title="2015-01-27">2015</span> <i title="MDPI AG"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/dstyyzbt45gknhqqjsh45p55h4" style="color: black;">Molecules</a> </i> &nbsp;
design workflows; (iv) applications covalent docking: case studies and (v) shortcomings and future perspectives of covalent docking.  ...  In this review we highlight: (i) covalent interactions in biomolecular systems; (ii) the mathematical framework of covalent molecular docking; (iii) implementation of covalent docking protocol in drug  ...  H.M.K acknowledges the help of National Research Foundation, South Africa for financial support.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.3390/molecules20021984">doi:10.3390/molecules20021984</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/25633330">pmid:25633330</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/lphyxur5tndspj7oxeomiuttda">fatcat:lphyxur5tndspj7oxeomiuttda</a> </span>
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Trametes versicolor glutathione transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes

Mathieu Schwartz, Thomas Perrot, Aurélie Deroy, Thomas Roret, Mélanie Morel-Rouhier, Guillermo Mulliert, Eric Gelhaye, Frédérique Favier, Claude Didierjean
<span title="2018-09-06">2018</span> <i title="Wiley"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/kn6dhptylrb77b5atyiom5ysjm" style="color: black;">FEBS Letters</a> </i> &nbsp;
Acknowledgements The authors would like to thank ESRF for beamtime, and the staff of beamline BM30A for data collections.  ...  The authors appreciated the access to the 'Plateforme de mesures de diffraction X' of the University of Lorraine with crystal testing.  ...  Glutathione transferases (GSTs) are widespread enzymes, which use glutathione (GSH) through several different types of reactions.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1002/1873-3468.13224">doi:10.1002/1873-3468.13224</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/30112765">pmid:30112765</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/aygh4xndzrgexoojtr4ghjfw6y">fatcat:aygh4xndzrgexoojtr4ghjfw6y</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20190503205709/https://hal.archives-ouvertes.fr/hal-01959634/document" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/d3/6a/d36a6fd63acbbb478d5b2bea5c437a8e133350fb.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1002/1873-3468.13224"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> wiley.com </button> </a>

GlutathioneS-Transferase Pi Has at Least Three Distinguishable Xenobiotic Substrate Sites Close to Its Glutathione-binding Site

Luis A. Ralat, Roberta F. Colman
<span title="2004-09-03">2004</span> <i title="American Society for Biochemistry &amp; Molecular Biology (ASBMB)"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/mryncoafc5cxdicldzfm4vlsze" style="color: black;">Journal of Biological Chemistry</a> </i> &nbsp;
Benzyl isothiocyanate (BITC), present in cruciferous vegetables, is an efficient substrate of human glutathione S-transferase P1-1 (hGST P1-1).  ...  This study provides evidence for the existence of a novel xenobiotic substrate site in hGST P1-1, which can be occupied by benzyl isothiocyanate and is distinct from that of monobromobimane and 1-chloro  ...  Misquitta for help with the expression of recombinant enzymes, Dr. Yu-Chu Huang for performing the peptide sequencing, and Dr. John Dykins for help with the mass spectrometry.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1074/jbc.m407445200">doi:10.1074/jbc.m407445200</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/15347687">pmid:15347687</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/magmj6fxkre2vgklj2q4ede35y">fatcat:magmj6fxkre2vgklj2q4ede35y</a> </span>
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Rutin-mediated Apoptosis and Glutathione Changes in Ascites Daltons Lymphoma Cells: In silico Analysis of Rutin Interactions with Some Antiapoptotic and Glutathione-related Proteins

R Prasad, S Banerjee, C. E Kharshiing, A Bhattacharjee, S. B Prasad
<span title="">2019</span> <i title="Indian Pharmaceutical Association - IPA"> Indian Journal of Pharmaceutical Sciences </i> &nbsp;
essential for the completion of the present studies.  ...  Acknowledgments: The authors gratefully acknowledge Department of Zoology and Department of Biotechnology and Bioinformatics, North Eastern Hill University, Shillong for providing the required facilities  ...  Interaction complex of rutin-glutathione S-transferase, B. ligplot analysis of rutin and glutathione S-transferase, C. interaction complex of rutin-glutathione reductase and D. ligplot analysis of rutin  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.36468/pharmaceutical-sciences.563">doi:10.36468/pharmaceutical-sciences.563</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/4ddslgkngbggzemyn3ixuavwue">fatcat:4ddslgkngbggzemyn3ixuavwue</a> </span>
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Discovery of M Protease inhibitors encoded by SARS-CoV-2

Hui-Chen Hung, Yi-Yu Ke, Sheng Yu Huang, Peng-Nien Huang, Yu-An Kung, Teng-Yuan Chang, Kuei-Jung Yen, Tzu-Ting Peng, Shao-En Chang, Chin-Ting Huang, Ya-Ru Tsai, Szu-Huei Wu (+7 others)
<span title="2020-07-15">2020</span> <i title="American Society for Microbiology"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/5yry76lrezcodh4zk6hgwgfwfi" style="color: black;">Antimicrobial Agents and Chemotherapy</a> </i> &nbsp;
Only a small portion of SARS-CoV-2-Mpro was covalently modified in the excess of GC376 as evaluated by mass spectrometry analysis; indicating that improved inhibitors are needed.  ...  Subsequently, molecular docking analysis revealing the recognition and binding groups of GC376 within the active site of SARS-CoV-2 Mpro provides important new information for the optimization of GC376  ...  The GST fusion protein was purified by glutathione affinity chromatography.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1128/aac.00872-20">doi:10.1128/aac.00872-20</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/32669265">pmid:32669265</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC7449189/">pmcid:PMC7449189</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/qpq5u6ytjvar5bmu3gxw34paq4">fatcat:qpq5u6ytjvar5bmu3gxw34paq4</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200905200807/https://aac.asm.org/content/aac/64/9/e00872-20.full.pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/f1/6b/f16b048bc534c8967a03a6e6ddca31b75ba242f3.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1128/aac.00872-20"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> asm.org </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7449189" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

The metabolic bioactivation of caffeic acid phenethyl ester (CAPE) mediated by tyrosinase selectively inhibits glutathione S-transferase

Shashi K. Kudugunti, Helen Thorsheim, Mohammad S. Yousef, Lan Guan, Majid Y. Moridani
<span title="">2011</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/2nebv7fkzjejdh4b5rrhgoakli" style="color: black;">Chemico-Biological Interactions</a> </i> &nbsp;
Keywords: Melanoma Quinone Glutathione GST Caffeic acid phenethyl ester MRP a b s t r a c t Glutathione S-transferase (GST) and multidrug resistance-associated proteins (MRPs) play major roles in drug  ...  Although, as controls, 4-hydroxyanisole and L-tyrosine were metabolized by tyrosinase to form quinones and glutathione conjugates, they exhibited no GST inhibition in the absence and presence of tyrosinase  ...  Acknowledgements The work was supported by NCI/NIH, 1R15CA122044-01A1 (to M.M.). The work was also partially supported by National Institutes of Health Grants R21HL087895 and R01GM095538 (to L.G.) and  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.cbi.2011.03.015">doi:10.1016/j.cbi.2011.03.015</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/21458432">pmid:21458432</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC3706206/">pmcid:PMC3706206</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/5s3k3r7osjbmnb36jvbyshon5q">fatcat:5s3k3r7osjbmnb36jvbyshon5q</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20130613075539/http://www.ttuhsc.edu/som/physiology/faculty/guan/21458432.pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/bf/97/bf97184a17b4b36140918576477db1617d1cb62f.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.cbi.2011.03.015"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> elsevier.com </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3706206" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

A model for glutathione binding and activation in the fosfomycin resistance protein, FosA

Rachel E. Rigsby, Daniel W. Brown, Eric Dawson, Terry P. Lybrand, Richard N. Armstrong
<span title="">2007</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/a7pnb366azhv7iwmrp4hjor3va" style="color: black;">Archives of Biochemistry and Biophysics</a> </i> &nbsp;
The genomically encoded fosfomycin resistance protein from Pseudomonas aeruginosa (FosA PA ) utilizes Mn(II) and K + to catalyze the addition of glutathione (GSH) to C1 of the antibiotic rendering it inactive  ...  In the absence of co-crystal structural data with the thiol substrate, these results provide important insights into the role of GSH in catalysis.  ...  The antibiotic covalently inhibits the enzyme MurA, the pyruvyl transferase that catalyzes the first step in cell wall biosynthesis.  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.abb.2007.04.035">doi:10.1016/j.abb.2007.04.035</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/17537395">pmid:17537395</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC2709490/">pmcid:PMC2709490</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/y6wsuovunzejrgfijt45imghv4">fatcat:y6wsuovunzejrgfijt45imghv4</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200206220053/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC2709490&amp;blobtype=pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/17/b8/17b8317800682e05895a8c10175e6cc0756d2ac2.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.abb.2007.04.035"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> elsevier.com </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2709490" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

2,2′-Dihydroxybenzophenones and their carbonyl N-analogues as inhibitor scaffolds for MDR-involved human glutathione transferase isoenzyme A1-1

Fereniki D. Perperopoulou, Petros G. Tsoungas, Trias N. Thireou, Vagelis E. Rinotas, Eleni K. Douni, Elias E. Eliopoulos, Nikolaos E. Labrou, Yannis D. Clonis
<span title="">2014</span> <i title="Elsevier BV"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/74assiiqmjamth6tcvry4hichm" style="color: black;">Bioorganic &amp; Medicinal Chemistry</a> </i> &nbsp;
A structure-based library of the latter was built-up by a nucleophilic cleavage of suitably substituted xanthones to 2,2 0 -dihydroxy-benzophenones (5-9) and subsequent formation of their N-derivatives  ...  Enzyme inhibition kinetics, molecular modeling and docking studies showed that they interact primarily at the CDNB-binding catalytic site of the enzyme.  ...  Acknowledgments The present work was partly supported by the action THALES: 'Glutathione transferases, multifunctional molecular tools in red and green biotechnology' falling under the Operational Programme  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.bmc.2014.06.007">doi:10.1016/j.bmc.2014.06.007</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/25002233">pmid:25002233</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/powvi43iqjggfkskdnjait3q3a">fatcat:powvi43iqjggfkskdnjait3q3a</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20170829172109/http://repository.edulll.gr/edulll/bitstream/10795/2678/2/2678_Paper%209.pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/2d/f8/2df848155072faef36f20359eb1cb7f5525b675f.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1016/j.bmc.2014.06.007"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> elsevier.com </button> </a>

Computational Studies of Hydroxychloroquine and Chloroquine Metabolites as Possible Candidates for Coronavirus (COVID-19) Treatment

Niteen A. Vaidya, Renu Vyas
<span title="2020-11-12">2020</span> <i title="Frontiers Media SA"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/qigargnicncadmdn56ei23yjnu" style="color: black;">Frontiers in Pharmacology</a> </i> &nbsp;
All the compounds were extensively studied computationally using docking, cheminformatics, and toxicity prediction tools.  ...  Based on the docking scores against ACE (angiotensin-converting enzyme) receptors and the toxicity data computed by employing the chemical analyzer module by ViridisChem™ Inc., the work reveals significant  ...  ., for allowing them to use the Chemical Analyzer production to develop some of the figures and tables, as well as the Director of the MIT School of Bioengineering Sciences and Research, MIT-ADT University  ... 
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.3389/fphar.2020.569665">doi:10.3389/fphar.2020.569665</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/33364944">pmid:33364944</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC7751693/">pmcid:PMC7751693</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/wb7erc5n5fgi5kcj7yoelrqfje">fatcat:wb7erc5n5fgi5kcj7yoelrqfje</a> </span>
<a target="_blank" rel="noopener" href="https://web.archive.org/web/20220125054018/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC7751693&amp;blobtype=pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/43/9a/439a597c5ec8e28a7cd9d0012cc6a15796d442bb.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.3389/fphar.2020.569665"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="unlock alternate icon" style="background-color: #fb971f;"></i> frontiersin.org </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7751693" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>

Regioselective Covalent Immobilization of Catalytically Active Glutathione S-Transferase on Glass Slides

Rajesh Viswanathan, Guillermo R. Labadie, C. Dale Poulter
<span title="2013-03-26">2013</span> <i title="American Chemical Society (ACS)"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/wb2mjyyn3vb4lhyj2jkqxf4vza" style="color: black;">Bioconjugate chemistry</a> </i> &nbsp;
glutathione S-transferase (GSTase) and the active modified protein was covalently attached to glass surfaces.  ...  The wells were washed and assayed for GSTase activity by monitoring the increase in A 340 upon addition of 1-chloro-2,4-dinitrobenzene (CDNB) and reduced glutathione (GT).  ...  The authors would like to thank Chad Nelson at the core Mass Spectral facility at the U. of Utah for analysis of protein samples by ESI-MS; Dr.  ... 
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<a target="_blank" rel="noopener" href="https://web.archive.org/web/20200207002315/http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC3644561&amp;blobtype=pdf" title="fulltext PDF download" data-goatcounter-click="serp-fulltext" data-goatcounter-title="serp-fulltext"> <button class="ui simple right pointing dropdown compact black labeled icon button serp-button"> <i class="icon ia-icon"></i> Web Archive [PDF] <div class="menu fulltext-thumbnail"> <img src="https://blobs.fatcat.wiki/thumbnail/pdf/29/7f/297f30ad02dcda190c55c15a08509063c7781773.180px.jpg" alt="fulltext thumbnail" loading="lazy"> </div> </button> </a> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1021/bc300462j"> <button class="ui left aligned compact blue labeled icon button serp-button"> <i class="external alternate icon"></i> acs.org </button> </a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3644561" title="pubmed link"> <button class="ui compact blue labeled icon button serp-button"> <i class="file alternate outline icon"></i> pubmed.gov </button> </a>
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