Stress-Induced Protein S-Glutathionylation and S-Trypanothionylation in African Trypanosomes-A Quantitative Redox Proteome and Thiol Analysis.
Identifieur interne : 000310 ( Main/Exploration ); précédent : 000309; suivant : 000311Stress-Induced Protein S-Glutathionylation and S-Trypanothionylation in African Trypanosomes-A Quantitative Redox Proteome and Thiol Analysis.
Auteurs : Kathrin Ulrich [Allemagne] ; Caroline Finkenzeller [Allemagne] ; Sabine Merker [Allemagne] ; Federico Rojas [Royaume-Uni] ; Keith Matthews [Royaume-Uni] ; Thomas Ruppert [Allemagne] ; R Luise Krauth-Siegel [Allemagne]Source :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2017.
Descripteurs français
- KwdFr :
- Acide hypochloreux (pharmacologie), Glutathion (analogues et dérivés), Glutathion (métabolisme), Humains (MeSH), Peroxyde d'hydrogène (pharmacologie), Protéine S (métabolisme), Protéines de protozoaire (analyse), Protéome (analyse), Spermidine (analogues et dérivés), Spermidine (métabolisme), Stress oxydatif (MeSH), Thiols (analyse), Trypanosoma brucei brucei (métabolisme), Tétraméthyl-diazènedicarboxamide (pharmacologie).
- MESH :
- analogues et dérivés : Glutathion, Spermidine.
- analyse : Protéines de protozoaire, Protéome, Thiols.
- métabolisme : Glutathion, Protéine S, Spermidine, Trypanosoma brucei brucei.
- pharmacologie : Acide hypochloreux, Peroxyde d'hydrogène, Tétraméthyl-diazènedicarboxamide.
- Humains, Stress oxydatif.
English descriptors
- KwdEn :
- Diamide (pharmacology), Glutathione (analogs & derivatives), Glutathione (metabolism), Humans (MeSH), Hydrogen Peroxide (pharmacology), Hypochlorous Acid (pharmacology), Oxidative Stress (MeSH), Protein S (metabolism), Proteome (analysis), Protozoan Proteins (analysis), Spermidine (analogs & derivatives), Spermidine (metabolism), Sulfhydryl Compounds (analysis), Trypanosoma brucei brucei (metabolism).
- MESH :
- chemical , analogs & derivatives : Glutathione, Spermidine.
- chemical , analysis : Proteome, Protozoan Proteins, Sulfhydryl Compounds.
- chemical , metabolism : Glutathione, Protein S, Spermidine.
- chemical , pharmacology : Diamide, Hydrogen Peroxide, Hypochlorous Acid.
- metabolism : Trypanosoma brucei brucei.
- Humans, Oxidative Stress.
Abstract
AIMS
Trypanosomatids have a unique trypanothione-based thiol redox metabolism. The parasite-specific dithiol is synthesized from glutathione and spermidine, with glutathionylspermidine as intermediate catalyzed by trypanothione synthetase. In this study, we address the oxidative stress response of African trypanosomes with special focus on putative protein S-thiolation.
RESULTS
Challenging bloodstream Trypanosoma brucei with diamide, H
INNOVATION
Our data reveal for the first time that trypanosomes employ protein S-thiolation when exposed to exogenous and endogenous oxidative stresses and trypanothione, despite its dithiol character, forms protein-mixed disulfides.
CONCLUSION
The stress-specific responses shown here emphasize protein S-trypanothionylation and S-glutathionylation as reversible protection mechanism in these parasites. Antioxid. Redox Signal. 27, 517-533.
DOI: 10.1089/ars.2016.6947
PubMed: 28338335
PubMed Central: PMC5567454
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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last="Ulrich">Kathrin Ulrich</name><affiliation wicri:level="3"><nlm:affiliation>1 Biochemie-Zentrum der Universität Heidelberg (BZH) , Heidelberg, Germany .</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>1 Biochemie-Zentrum der Universität Heidelberg (BZH) , Heidelberg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Karlsruhe</region><settlement type="city">Heidelberg</settlement></placeName></affiliation></author><author><name sortKey="Finkenzeller, Caroline" sort="Finkenzeller, Caroline" uniqKey="Finkenzeller C" first="Caroline" last="Finkenzeller">Caroline Finkenzeller</name><affiliation wicri:level="3"><nlm:affiliation>1 Biochemie-Zentrum der Universität Heidelberg (BZH) , Heidelberg, Germany .</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>1 Biochemie-Zentrum der Universität Heidelberg (BZH) , Heidelberg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Karlsruhe</region><settlement type="city">Heidelberg</settlement></placeName></affiliation></author><author><name sortKey="Merker, Sabine" sort="Merker, Sabine" uniqKey="Merker S" first="Sabine" last="Merker">Sabine Merker</name><affiliation wicri:level="3"><nlm:affiliation>2 Zentrum für Molekularbiologie der Universität Heidelberg (ZMBH) , Heidelberg, Germany .</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>2 Zentrum für Molekularbiologie der Universität Heidelberg (ZMBH) , Heidelberg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Karlsruhe</region><settlement type="city">Heidelberg</settlement></placeName></affiliation></author><author><name sortKey="Rojas, Federico" sort="Rojas, Federico" uniqKey="Rojas F" first="Federico" last="Rojas">Federico Rojas</name><affiliation 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type="city">Heidelberg</settlement></placeName></affiliation></author><author><name sortKey="Krauth Siegel, R Luise" sort="Krauth Siegel, R Luise" uniqKey="Krauth Siegel R" first="R Luise" last="Krauth-Siegel">R Luise Krauth-Siegel</name><affiliation wicri:level="3"><nlm:affiliation>1 Biochemie-Zentrum der Universität Heidelberg (BZH) , Heidelberg, Germany .</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>1 Biochemie-Zentrum der Universität Heidelberg (BZH) , Heidelberg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Karlsruhe</region><settlement type="city">Heidelberg</settlement></placeName></affiliation></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="eISSN">1557-7716</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Diamide (pharmacology)</term><term>Glutathione (analogs & derivatives)</term><term>Glutathione (metabolism)</term><term>Humans (MeSH)</term><term>Hydrogen Peroxide (pharmacology)</term><term>Hypochlorous Acid (pharmacology)</term><term>Oxidative Stress (MeSH)</term><term>Protein S (metabolism)</term><term>Proteome (analysis)</term><term>Protozoan Proteins (analysis)</term><term>Spermidine (analogs & derivatives)</term><term>Spermidine (metabolism)</term><term>Sulfhydryl Compounds (analysis)</term><term>Trypanosoma brucei brucei (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide hypochloreux (pharmacologie)</term><term>Glutathion (analogues et dérivés)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Peroxyde d'hydrogène (pharmacologie)</term><term>Protéine S (métabolisme)</term><term>Protéines de protozoaire (analyse)</term><term>Protéome (analyse)</term><term>Spermidine (analogues et dérivés)</term><term>Spermidine (métabolisme)</term><term>Stress oxydatif (MeSH)</term><term>Thiols (analyse)</term><term>Trypanosoma brucei brucei (métabolisme)</term><term>Tétraméthyl-diazènedicarboxamide (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Glutathione</term><term>Spermidine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Proteome</term><term>Protozoan Proteins</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Protein S</term><term>Spermidine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Diamide</term><term>Hydrogen Peroxide</term><term>Hypochlorous Acid</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Glutathion</term><term>Spermidine</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Protéines de protozoaire</term><term>Protéome</term><term>Thiols</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Protéine S</term><term>Spermidine</term><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acide hypochloreux</term><term>Peroxyde d'hydrogène</term><term>Tétraméthyl-diazènedicarboxamide</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>AIMS</b></p><p>Trypanosomatids have a unique trypanothione-based thiol redox metabolism. The parasite-specific dithiol is synthesized from glutathione and spermidine, with glutathionylspermidine as intermediate catalyzed by trypanothione synthetase. In this study, we address the oxidative stress response of African trypanosomes with special focus on putative protein S-thiolation.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>Challenging bloodstream Trypanosoma brucei with diamide, H</p></div><div type="abstract" xml:lang="en"><p><b>INNOVATION</b></p><p>Our data reveal for the first time that trypanosomes employ protein S-thiolation when exposed to exogenous and endogenous oxidative stresses and trypanothione, despite its dithiol character, forms protein-mixed disulfides.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>The stress-specific responses shown here emphasize protein S-trypanothionylation and S-glutathionylation as reversible protection mechanism in these parasites. Antioxid. Redox Signal. 27, 517-533.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28338335</PMID><DateCompleted><Year>2018</Year><Month>03</Month><Day>09</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>27</Volume><Issue>9</Issue><PubDate><Year>2017</Year><Month>Sep</Month><Day>20</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Stress-Induced Protein S-Glutathionylation and S-Trypanothionylation in African Trypanosomes-A Quantitative Redox Proteome and Thiol Analysis.</ArticleTitle><Pagination><MedlinePgn>517-533</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2016.6947</ELocationID><Abstract><AbstractText Label="AIMS" NlmCategory="OBJECTIVE">Trypanosomatids have a unique trypanothione-based thiol redox metabolism. The parasite-specific dithiol is synthesized from glutathione and spermidine, with glutathionylspermidine as intermediate catalyzed by trypanothione synthetase. In this study, we address the oxidative stress response of African trypanosomes with special focus on putative protein S-thiolation.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">Challenging bloodstream Trypanosoma brucei with diamide, H<sub>2</sub>O<sub>2</sub> or hypochlorite results in distinct levels of reversible overall protein S-thiolation. Quantitative proteome analyses reveal 84 proteins oxidized in diamide-stressed parasites. Fourteen of them, including several essential thiol redox proteins and chaperones, are also enriched when glutathione/glutaredoxin serves as a reducing system indicating S-thiolation. In parasites exposed to H<sub>2</sub>O<sub>2</sub>, other sets of proteins are modified. Only three proteins are S-thiolated under all stress conditions studied in accordance with a highly specific response. H<sub>2</sub>O<sub>2</sub> causes primarily the formation of free disulfides. In contrast, in diamide-treated cells, glutathione, glutathionylspermidine, and trypanothione are almost completely protein bound. Remarkably, the total level of trypanothione is decreased, whereas those of glutathione and glutathionylspermidine are increased, indicating partial hydrolysis of protein-bound trypanothione. Depletion of trypanothione synthetase exclusively induces protein S-glutathionylation. Total mass analyses of a recombinant peroxidase treated with T(SH)<sub>2</sub> and either diamide or hydrogen peroxide verify protein S-trypanothionylation as stable modification.</AbstractText><AbstractText Label="INNOVATION" NlmCategory="METHODS">Our data reveal for the first time that trypanosomes employ protein S-thiolation when exposed to exogenous and endogenous oxidative stresses and trypanothione, despite its dithiol character, forms protein-mixed disulfides.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">The stress-specific responses shown here emphasize protein S-trypanothionylation and S-glutathionylation as reversible protection mechanism in these parasites. Antioxid. Redox Signal. 27, 517-533.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ulrich</LastName><ForeName>Kathrin</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>1 Biochemie-Zentrum der Universität Heidelberg (BZH) , Heidelberg, Germany .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Finkenzeller</LastName><ForeName>Caroline</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>1 Biochemie-Zentrum der Universität Heidelberg (BZH) , Heidelberg, Germany .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Merker</LastName><ForeName>Sabine</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>2 Zentrum für Molekularbiologie der Universität Heidelberg (ZMBH) , Heidelberg, Germany .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rojas</LastName><ForeName>Federico</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>3 Centre for Immunity, Infection and Evolution, Institute for Immunology and Infection Research, School of Biological Sciences, University of Edinburgh , Edinburgh, United Kingdom .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matthews</LastName><ForeName>Keith</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>3 Centre for Immunity, Infection and Evolution, Institute for Immunology and Infection Research, School of Biological Sciences, University of Edinburgh , Edinburgh, United Kingdom .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ruppert</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>2 Zentrum für Molekularbiologie der Universität Heidelberg (ZMBH) , Heidelberg, Germany .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Krauth-Siegel</LastName><ForeName>R Luise</ForeName><Initials>RL</Initials><AffiliationInfo><Affiliation>1 Biochemie-Zentrum der Universität Heidelberg (BZH) , Heidelberg, Germany .</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>BB/I004602/1</GrantID><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>03</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017293">Protein S</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020543">Proteome</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015800">Protozoan Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>10465-78-8</RegistryNumber><NameOfSubstance UI="D003958">Diamide</NameOfSubstance></Chemical><Chemical><RegistryNumber>712K4CDC10</RegistryNumber><NameOfSubstance UI="D006997">Hypochlorous Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>96304-42-6</RegistryNumber><NameOfSubstance UI="C044809">trypanothione</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>U87FK77H25</RegistryNumber><NameOfSubstance 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PubStatus="entrez"><Year>2017</Year><Month>3</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28338335</ArticleId><ArticleId IdType="doi">10.1089/ars.2016.6947</ArticleId><ArticleId IdType="pmc">PMC5567454</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Biol Chem. 2003 Nov 28;278(48):47361-4</Citation><ArticleIdList><ArticleId IdType="pubmed">14559909</ArticleId></ArticleIdList></Reference><Reference><Citation>J Cell Biol. 1984 Apr;98(4):1178-84</Citation><ArticleIdList><ArticleId IdType="pubmed">6715405</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2009 Jan 13;106(2):422-7</Citation><ArticleIdList><ArticleId IdType="pubmed">19122143</ArticleId></ArticleIdList></Reference><Reference><Citation>Amino Acids. 2003 Dec;25(3-4):259-74</Citation><ArticleIdList><ArticleId IdType="pubmed">14661089</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2000 Sep 12;39(36):11121-8</Citation><ArticleIdList><ArticleId IdType="pubmed">10998251</ArticleId></ArticleIdList></Reference><Reference><Citation>Antioxid Redox Signal. 2008 Sep;10(9):1593-606</Citation><ArticleIdList><ArticleId IdType="pubmed">18498224</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2014 May 30;289(22):15536-43</Citation><ArticleIdList><ArticleId IdType="pubmed">24719319</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2011 Apr 19;50(15):3204-10</Citation><ArticleIdList><ArticleId IdType="pubmed">21401077</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 2012 Nov 1;527(1):45-54</Citation><ArticleIdList><ArticleId IdType="pubmed">22874433</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 2013 Feb 15;433(2):132-6</Citation><ArticleIdList><ArticleId IdType="pubmed">23072983</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Microbiol. 2009 Nov;74(3):529-40</Citation><ArticleIdList><ArticleId IdType="pubmed">19558432</ArticleId></ArticleIdList></Reference><Reference><Citation>BMC Genomics. 2014 Oct 20;15:911</Citation><ArticleIdList><ArticleId IdType="pubmed">25331479</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2013 Nov 8;288(45):32241-7</Citation><ArticleIdList><ArticleId IdType="pubmed">24062305</ArticleId></ArticleIdList></Reference><Reference><Citation>Free Radic Biol Med. 2004 May 15;36(10):1289-302</Citation><ArticleIdList><ArticleId IdType="pubmed">15110394</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2012;7(5):e36619</Citation><ArticleIdList><ArticleId IdType="pubmed">22574199</ArticleId></ArticleIdList></Reference><Reference><Citation>Annu Rev Microbiol. 1992;46:695-729</Citation><ArticleIdList><ArticleId IdType="pubmed">1444271</ArticleId></ArticleIdList></Reference><Reference><Citation>Antioxid Redox Signal. 2012 Dec 15;17(12):1748-63</Citation><ArticleIdList><ArticleId IdType="pubmed">22530666</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1989 Jul 25;28(15):6440-6</Citation><ArticleIdList><ArticleId IdType="pubmed">2551375</ArticleId></ArticleIdList></Reference><Reference><Citation>J Proteomics. 2015 Apr 29;120:95-104</Citation><ArticleIdList><ArticleId IdType="pubmed">25765699</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Chem. 1995 Dec 1;67(23):4261-8</Citation><ArticleIdList><ArticleId IdType="pubmed">8633771</ArticleId></ArticleIdList></Reference><Reference><Citation>Free Radic Res. 2011 Jan;45(1):3-15</Citation><ArticleIdList><ArticleId IdType="pubmed">20815784</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2006 Mar;1760(3):380-7</Citation><ArticleIdList><ArticleId IdType="pubmed">16515838</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Apr 14;281(15):10420-30</Citation><ArticleIdList><ArticleId IdType="pubmed">16418165</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 2005 Jul 1;342(1):160-2</Citation><ArticleIdList><ArticleId IdType="pubmed">15958193</ArticleId></ArticleIdList></Reference><Reference><Citation>J Proteomics. 2013 Apr 9;81:185-99</Citation><ArticleIdList><ArticleId IdType="pubmed">23376486</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3505-10</Citation><ArticleIdList><ArticleId IdType="pubmed">11904414</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 2002 Oct 15;406(2):229-40</Citation><ArticleIdList><ArticleId IdType="pubmed">12361711</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2007 Mar 23;282(12):8678-94</Citation><ArticleIdList><ArticleId IdType="pubmed">17242409</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biochem Parasitol. 2015 Dec;204(2):93-105</Citation><ArticleIdList><ArticleId IdType="pubmed">26854591</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2010 Nov 5;285(45):35224-37</Citation><ArticleIdList><ArticleId IdType="pubmed">20826822</ArticleId></ArticleIdList></Reference><Reference><Citation>J Proteomics. 2011 Aug 24;74(9):1683-92</Citation><ArticleIdList><ArticleId IdType="pubmed">21539948</ArticleId></ArticleIdList></Reference><Reference><Citation>Antioxid Redox Signal. 2011 Dec 1;15(11):2855-65</Citation><ArticleIdList><ArticleId IdType="pubmed">21595565</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2013 May;1830(5):3199-216</Citation><ArticleIdList><ArticleId IdType="pubmed">23396001</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Microbiol. 2002 Mar;43(5):1129-38</Citation><ArticleIdList><ArticleId IdType="pubmed">11918801</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2008 Jun 17;105(24):8197-202</Citation><ArticleIdList><ArticleId IdType="pubmed">18287020</ArticleId></ArticleIdList></Reference><Reference><Citation>RNA Biol. 2014;11(6):715-31</Citation><ArticleIdList><ArticleId IdType="pubmed">24922194</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 1998 Jul 24;431(3):381-5</Citation><ArticleIdList><ArticleId IdType="pubmed">9714547</ArticleId></ArticleIdList></Reference><Reference><Citation>Gene. 2000 Oct 31;257(2):251-7</Citation><ArticleIdList><ArticleId IdType="pubmed">11080591</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2008 Aug 1;283(31):21571-8</Citation><ArticleIdList><ArticleId IdType="pubmed">18534986</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Proteomics. 2012 Feb;11(2):M111.014142</Citation><ArticleIdList><ArticleId IdType="pubmed">22122882</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2004 May 21;279(21):21749-58</Citation><ArticleIdList><ArticleId IdType="pubmed">15031298</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1993 Apr 6;32(13):3368-76</Citation><ArticleIdList><ArticleId IdType="pubmed">8461300</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biochem Parasitol. 2003 Sep;131(1):25-33</Citation><ArticleIdList><ArticleId IdType="pubmed">12967709</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1975 Apr 10;250(7):2648-54</Citation><ArticleIdList><ArticleId IdType="pubmed">1091640</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2013 Aug 16;288(33):23751-64</Citation><ArticleIdList><ArticleId IdType="pubmed">23814051</ArticleId></ArticleIdList></Reference><Reference><Citation>Antioxid Redox Signal. 2017 Feb 20;26(6):247-261</Citation><ArticleIdList><ArticleId IdType="pubmed">26838680</ArticleId></ArticleIdList></Reference><Reference><Citation>Antioxid Redox Signal. 2012 Aug 15;17(4):583-607</Citation><ArticleIdList><ArticleId IdType="pubmed">22053812</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biochem Parasitol. 2008 Sep;161(1):76-9</Citation><ArticleIdList><ArticleId IdType="pubmed">18588918</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2008 Nov;1780(11):1236-48</Citation><ArticleIdList><ArticleId IdType="pubmed">18395526</ArticleId></ArticleIdList></Reference><Reference><Citation>Free Radic Biol Med. 2013 Oct;63:65-77</Citation><ArticleIdList><ArticleId IdType="pubmed">23665397</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1996 Jun 1;316 ( Pt 2):439-45</Citation><ArticleIdList><ArticleId IdType="pubmed">8687385</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2008 Feb 29;283(9):5380-8</Citation><ArticleIdList><ArticleId IdType="pubmed">18167353</ArticleId></ArticleIdList></Reference><Reference><Citation>Free Radic Biol Med. 2011 Aug 15;51(4):856-68</Citation><ArticleIdList><ArticleId IdType="pubmed">21640819</ArticleId></ArticleIdList></Reference><Reference><Citation>Int J Biol Macromol. 2013 Mar;54:238-43</Citation><ArticleIdList><ArticleId IdType="pubmed">23262386</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Protoc. 2006;1(6):2650-60</Citation><ArticleIdList><ArticleId IdType="pubmed">17406521</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 2003 Sep 1;374(Pt 2):513-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12755685</ArticleId></ArticleIdList></Reference><Reference><Citation>Int J Cell Biol. 2012;2012:273549</Citation><ArticleIdList><ArticleId IdType="pubmed">22654912</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 2007 Feb 15;402(1):43-9</Citation><ArticleIdList><ArticleId IdType="pubmed">17040206</ArticleId></ArticleIdList></Reference><Reference><Citation>J Proteomics. 2011 Oct 19;74(11):2476-86</Citation><ArticleIdList><ArticleId IdType="pubmed">21672643</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS Pathog. 2014 Apr 10;10(4):e1004075</Citation><ArticleIdList><ArticleId IdType="pubmed">24722489</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2016 Feb 5;291(6):3053-62</Citation><ArticleIdList><ArticleId IdType="pubmed">26601956</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2009 Nov 23;4(11):e7949</Citation><ArticleIdList><ArticleId IdType="pubmed">19956735</ArticleId></ArticleIdList></Reference><Reference><Citation>Trends Parasitol. 2011 Oct;27(10):434-41</Citation><ArticleIdList><ArticleId IdType="pubmed">21737348</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2008 Jun 20;283(25):17672-80</Citation><ArticleIdList><ArticleId IdType="pubmed">18420578</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 1995;251:123-33</Citation><ArticleIdList><ArticleId IdType="pubmed">7651192</ArticleId></ArticleIdList></Reference><Reference><Citation>Free Radic Biol Med. 2014 Feb;67:460-70</Citation><ArticleIdList><ArticleId IdType="pubmed">24333276</ArticleId></ArticleIdList></Reference><Reference><Citation>J Proteomics. 2009 May 2;72(4):677-89</Citation><ArticleIdList><ArticleId IdType="pubmed">19367685</ArticleId></ArticleIdList></Reference><Reference><Citation>FEMS Microbiol Rev. 2007 Jul;31(4):359-77</Citation><ArticleIdList><ArticleId IdType="pubmed">17459115</ArticleId></ArticleIdList></Reference><Reference><Citation>Electrophoresis. 2007 Jun;28(12):2095-9</Citation><ArticleIdList><ArticleId IdType="pubmed">17516579</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Protoc. 2009;4(4):484-94</Citation><ArticleIdList><ArticleId IdType="pubmed">19300442</ArticleId></ArticleIdList></Reference><Reference><Citation>Int J Parasitol. 2009 Aug;39(10):1059-62</Citation><ArticleIdList><ArticleId IdType="pubmed">19477177</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2010 Aug 13;285(33):25345-53</Citation><ArticleIdList><ArticleId IdType="pubmed">20530482</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2013 Jun 11;8(6):e65908</Citation><ArticleIdList><ArticleId IdType="pubmed">23776565</ArticleId></ArticleIdList></Reference><Reference><Citation>Antioxid Redox Signal. 2013 May 1;18(13):1642-53</Citation><ArticleIdList><ArticleId IdType="pubmed">23075082</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2013 May 17;288(20):14170-7</Citation><ArticleIdList><ArticleId IdType="pubmed">23543738</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1997 Sep 15;248(3):913-8</Citation><ArticleIdList><ArticleId IdType="pubmed">9342246</ArticleId></ArticleIdList></Reference><Reference><Citation>Cancer Res. 2009 Oct 1;69(19):7626-34</Citation><ArticleIdList><ArticleId IdType="pubmed">19773442</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2006 Dec;1763(12):1463-77</Citation><ArticleIdList><ArticleId IdType="pubmed">17023066</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li><li>Royaume-Uni</li></country><region><li>Bade-Wurtemberg</li><li>District de Karlsruhe</li><li>Écosse</li></region><settlement><li>Heidelberg</li><li>Édimbourg</li></settlement></list><tree><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Ulrich, Kathrin" sort="Ulrich, Kathrin" uniqKey="Ulrich K" first="Kathrin" last="Ulrich">Kathrin Ulrich</name></region><name sortKey="Finkenzeller, Caroline" sort="Finkenzeller, Caroline" uniqKey="Finkenzeller C" first="Caroline" last="Finkenzeller">Caroline 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