Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.
Identifieur interne : 000B38 ( Main/Exploration ); précédent : 000B37; suivant : 000B39Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.
Auteurs : Ji Won Park [États-Unis] ; John J. Mieyal ; Sue Goo Rhee ; P Boon ChockSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2009.
Descripteurs français
- KwdFr :
- Biocatalyse (MeSH), Cinétique (MeSH), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (métabolisme), Humains (MeSH), Lignée cellulaire (MeSH), Maturation post-traductionnelle des protéines (MeSH), Mutagenèse dirigée (MeSH), Oxidoreductases acting on sulfur group donors (composition chimique), Oxidoreductases acting on sulfur group donors (génétique), Oxidoreductases acting on sulfur group donors (métabolisme), Peroxirédoxines (composition chimique), Peroxirédoxines (génétique), Peroxirédoxines (métabolisme), Spécificité du substrat (MeSH).
- MESH :
- composition chimique : Oxidoreductases acting on sulfur group donors, Peroxirédoxines.
- génétique : Glutarédoxines, Oxidoreductases acting on sulfur group donors, Peroxirédoxines.
- métabolisme : Glutarédoxines, Glutathion, Oxidoreductases acting on sulfur group donors, Peroxirédoxines.
- Biocatalyse, Cinétique, Humains, Lignée cellulaire, Maturation post-traductionnelle des protéines, Mutagenèse dirigée, Spécificité du substrat.
English descriptors
- KwdEn :
- Biocatalysis (MeSH), Cell Line (MeSH), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (metabolism), Humans (MeSH), Kinetics (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidoreductases Acting on Sulfur Group Donors (chemistry), Oxidoreductases Acting on Sulfur Group Donors (genetics), Oxidoreductases Acting on Sulfur Group Donors (metabolism), Peroxiredoxins (chemistry), Peroxiredoxins (genetics), Peroxiredoxins (metabolism), Protein Processing, Post-Translational (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Oxidoreductases Acting on Sulfur Group Donors, Peroxiredoxins.
- chemical , genetics : Glutaredoxins, Oxidoreductases Acting on Sulfur Group Donors, Peroxiredoxins.
- chemical , metabolism : Glutaredoxins, Glutathione, Oxidoreductases Acting on Sulfur Group Donors, Peroxiredoxins.
- Biocatalysis, Cell Line, Humans, Kinetics, Mutagenesis, Site-Directed, Protein Processing, Post-Translational, Substrate Specificity.
Abstract
Reversible protein glutathionylation plays a key role in cellular regulation and cell signaling and protects protein thiols from hyperoxidation. Sulfiredoxin (Srx), an enzyme that catalyzes the reduction of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys Prxs), has been shown to catalyze the deglutathionylation of actin. We show that deglutathionylation of 2-Cys Prx, a family of peroxidases, is specifically catalyzed by Srx. Using the ubiquitously expressed member of 2-Cys Prx, Prx I, we revealed the following. (i) Among its four Cys residues, Cys(52), Cys(83), and Cys(173) can be glutathionylated in vitro. Deglutathionylation with Cys mutants showed that Cys(83) and Cys(173) were preferentially catalyzed by Srx, with glutathionylated Srx as the reaction intermediate, whereas glutaredoxin I was more favorable for deglutathionylating Cys(52). (ii) Studies using site-directed mutagenesis coupled with binding and deglutathionylation activities revealed that Pro(174) and Pro(179) of Prx I and Tyr(92) of Srx are essential for both activities. Furthermore, relative to glutaredoxin I, Srx exhibited negligible deglutathionylation activity for glutathionylated cysteine and glutathionylated BSA. These results indicate that Srx is specific for deglutathionylating Prx I due to its favorable affinity for Prx I. To assess the biological relevance of these observations, we showed that Prx I is glutathionylated in A549 and HeLa cells under modest levels of H(2)O(2). In addition, the level of glutathionylated Prx I was substantially elevated in small interfering RNA-mediated Srx-knocked down cells, whereas the reverse was observed in Srx-overexpressing cells. However, glutathionylation of Prx V, not known to bind to Srx, was not affected by the change in Srx expression levels.
DOI: 10.1074/jbc.M109.021394
PubMed: 19561357
PubMed Central: PMC2749110
Affiliations:
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Mieyal</name></author><author><name sortKey="Rhee, Sue Goo" sort="Rhee, Sue Goo" uniqKey="Rhee S" first="Sue Goo" last="Rhee">Sue Goo Rhee</name></author><author><name sortKey="Chock, P Boon" sort="Chock, P Boon" uniqKey="Chock P" first="P Boon" last="Chock">P Boon Chock</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biocatalysis (MeSH)</term><term>Cell Line (MeSH)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Humans (MeSH)</term><term>Kinetics (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Oxidoreductases Acting on Sulfur Group Donors (chemistry)</term><term>Oxidoreductases Acting on Sulfur Group Donors (genetics)</term><term>Oxidoreductases Acting on Sulfur Group Donors (metabolism)</term><term>Peroxiredoxins (chemistry)</term><term>Peroxiredoxins (genetics)</term><term>Peroxiredoxins (metabolism)</term><term>Protein Processing, Post-Translational (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biocatalyse (MeSH)</term><term>Cinétique (MeSH)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Lignée cellulaire (MeSH)</term><term>Maturation post-traductionnelle des protéines (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Oxidoreductases acting on sulfur group donors (composition chimique)</term><term>Oxidoreductases acting on sulfur group donors (génétique)</term><term>Oxidoreductases acting on sulfur group donors (métabolisme)</term><term>Peroxirédoxines (composition chimique)</term><term>Peroxirédoxines (génétique)</term><term>Peroxirédoxines (métabolisme)</term><term>Spécificité du substrat (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oxidoreductases Acting on Sulfur Group Donors</term><term>Peroxiredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Oxidoreductases Acting on Sulfur Group Donors</term><term>Peroxiredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Glutathione</term><term>Oxidoreductases Acting on Sulfur Group Donors</term><term>Peroxiredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Oxidoreductases acting on sulfur group donors</term><term>Peroxirédoxines</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term><term>Oxidoreductases acting on sulfur group donors</term><term>Peroxirédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Glutathion</term><term>Oxidoreductases acting on sulfur group donors</term><term>Peroxirédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biocatalysis</term><term>Cell Line</term><term>Humans</term><term>Kinetics</term><term>Mutagenesis, Site-Directed</term><term>Protein Processing, Post-Translational</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biocatalyse</term><term>Cinétique</term><term>Humains</term><term>Lignée cellulaire</term><term>Maturation post-traductionnelle des protéines</term><term>Mutagenèse dirigée</term><term>Spécificité du substrat</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Reversible protein glutathionylation plays a key role in cellular regulation and cell signaling and protects protein thiols from hyperoxidation. Sulfiredoxin (Srx), an enzyme that catalyzes the reduction of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys Prxs), has been shown to catalyze the deglutathionylation of actin. We show that deglutathionylation of 2-Cys Prx, a family of peroxidases, is specifically catalyzed by Srx. Using the ubiquitously expressed member of 2-Cys Prx, Prx I, we revealed the following. (i) Among its four Cys residues, Cys(52), Cys(83), and Cys(173) can be glutathionylated in vitro. Deglutathionylation with Cys mutants showed that Cys(83) and Cys(173) were preferentially catalyzed by Srx, with glutathionylated Srx as the reaction intermediate, whereas glutaredoxin I was more favorable for deglutathionylating Cys(52). (ii) Studies using site-directed mutagenesis coupled with binding and deglutathionylation activities revealed that Pro(174) and Pro(179) of Prx I and Tyr(92) of Srx are essential for both activities. Furthermore, relative to glutaredoxin I, Srx exhibited negligible deglutathionylation activity for glutathionylated cysteine and glutathionylated BSA. These results indicate that Srx is specific for deglutathionylating Prx I due to its favorable affinity for Prx I. To assess the biological relevance of these observations, we showed that Prx I is glutathionylated in A549 and HeLa cells under modest levels of H(2)O(2). In addition, the level of glutathionylated Prx I was substantially elevated in small interfering RNA-mediated Srx-knocked down cells, whereas the reverse was observed in Srx-overexpressing cells. However, glutathionylation of Prx V, not known to bind to Srx, was not affected by the change in Srx expression levels.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19561357</PMID><DateCompleted><Year>2009</Year><Month>10</Month><Day>19</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>284</Volume><Issue>35</Issue><PubDate><Year>2009</Year><Month>Aug</Month><Day>28</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.</ArticleTitle><Pagination><MedlinePgn>23364-74</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M109.021394</ELocationID><Abstract><AbstractText>Reversible protein glutathionylation plays a key role in cellular regulation and cell signaling and protects protein thiols from hyperoxidation. Sulfiredoxin (Srx), an enzyme that catalyzes the reduction of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys Prxs), has been shown to catalyze the deglutathionylation of actin. We show that deglutathionylation of 2-Cys Prx, a family of peroxidases, is specifically catalyzed by Srx. Using the ubiquitously expressed member of 2-Cys Prx, Prx I, we revealed the following. (i) Among its four Cys residues, Cys(52), Cys(83), and Cys(173) can be glutathionylated in vitro. Deglutathionylation with Cys mutants showed that Cys(83) and Cys(173) were preferentially catalyzed by Srx, with glutathionylated Srx as the reaction intermediate, whereas glutaredoxin I was more favorable for deglutathionylating Cys(52). (ii) Studies using site-directed mutagenesis coupled with binding and deglutathionylation activities revealed that Pro(174) and Pro(179) of Prx I and Tyr(92) of Srx are essential for both activities. Furthermore, relative to glutaredoxin I, Srx exhibited negligible deglutathionylation activity for glutathionylated cysteine and glutathionylated BSA. These results indicate that Srx is specific for deglutathionylating Prx I due to its favorable affinity for Prx I. To assess the biological relevance of these observations, we showed that Prx I is glutathionylated in A549 and HeLa cells under modest levels of H(2)O(2). In addition, the level of glutathionylated Prx I was substantially elevated in small interfering RNA-mediated Srx-knocked down cells, whereas the reverse was observed in Srx-overexpressing cells. However, glutathionylation of Prx V, not known to bind to Srx, was not affected by the change in Srx expression levels.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Park</LastName><ForeName>Ji Won</ForeName><Initials>JW</Initials><AffiliationInfo><Affiliation>Laboratory of Biochemistry, Biochemistry and Biophysics Center, Division of Intramural Research, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-8012, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mieyal</LastName><ForeName>John J</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Rhee</LastName><ForeName>Sue Goo</ForeName><Initials>SG</Initials></Author><Author ValidYN="Y"><LastName>Chock</LastName><ForeName>P Boon</ForeName><Initials>PB</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P01 AG015885</GrantID><Acronym>AG</Acronym><Agency>NIA NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>2 PO1 AG 15885</GrantID><Acronym>AG</Acronym><Agency>NIA NIH HHS</Agency><Country>United States</Country></Grant><Grant><Agency>Intramural NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D052060">Research Support, N.I.H., Intramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>06</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.-</RegistryNumber><NameOfSubstance UI="D050862">Oxidoreductases Acting on Sulfur Group Donors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.98.2</RegistryNumber><NameOfSubstance UI="C504024">SRXN1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D055162" MajorTopicYN="N">Biocatalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050862" MajorTopicYN="N">Oxidoreductases Acting on Sulfur Group Donors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>6</Month><Day>30</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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IdType="pubmed">10588361</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2000 Aug 25;275(34):26556-65</Citation><ArticleIdList><ArticleId IdType="pubmed">10854441</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. 2000 Winter;2(4):811-20</Citation><ArticleIdList><ArticleId IdType="pubmed">11213485</ArticleId></ArticleIdList></Reference><Reference><Citation>IUBMB Life. 2001 Jul;52(1-2):35-41</Citation><ArticleIdList><ArticleId IdType="pubmed">11795591</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2002 Mar 22;277(12):9655-60</Citation><ArticleIdList><ArticleId IdType="pubmed">11751890</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>J Biol Chem. 2002 May 31;277(22):19396-401</Citation><ArticleIdList><ArticleId IdType="pubmed">11904290</ArticleId></ArticleIdList></Reference><Reference><Citation>Biol Chem. 2002 Mar-Apr;383(3-4):347-64</Citation><ArticleIdList><ArticleId IdType="pubmed">12033427</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9745-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12119401</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2002 Oct 11;277(41):38029-36</Citation><ArticleIdList><ArticleId IdType="pubmed">12161445</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2003 Apr 25;300(5619):653-6</Citation><ArticleIdList><ArticleId IdType="pubmed">12714748</ArticleId></ArticleIdList></Reference><Reference><Citation>Proteomics. 2003 Jul;3(7):1154-61</Citation><ArticleIdList><ArticleId IdType="pubmed">12872216</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2003 Oct 30;425(6961):980-4</Citation><ArticleIdList><ArticleId IdType="pubmed">14586471</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Biophys Res Commun. 1969 Nov 6;37(4):593-6</Citation><ArticleIdList><ArticleId IdType="pubmed">5353890</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1993 Apr 6;32(13):3368-76</Citation><ArticleIdList><ArticleId IdType="pubmed">8461300</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7022-6</Citation><ArticleIdList><ArticleId IdType="pubmed">8041739</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1994 Nov 4;269(44):27670-8</Citation><ArticleIdList><ArticleId IdType="pubmed">7961686</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1995 Jan 27;80(2):225-36</Citation><ArticleIdList><ArticleId IdType="pubmed">7834742</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1995 Oct 13;270(5234):296-9</Citation><ArticleIdList><ArticleId IdType="pubmed">7569979</ArticleId></ArticleIdList></Reference><Reference><Citation>J Chromatogr A. 1995 Sep 29;712(1):177-90</Citation><ArticleIdList><ArticleId IdType="pubmed">8556150</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1997 Jan 3;272(1):217-21</Citation><ArticleIdList><ArticleId IdType="pubmed">8995250</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 1999;300:219-26</Citation><ArticleIdList><ArticleId IdType="pubmed">9919524</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2004 Dec 3;279(49):50994-1001</Citation><ArticleIdList><ArticleId IdType="pubmed">15448164</ArticleId></ArticleIdList></Reference><Reference><Citation>Antioxid Redox Signal. 2005 Mar-Apr;7(3-4):348-66</Citation><ArticleIdList><ArticleId IdType="pubmed">15706083</ArticleId></ArticleIdList></Reference><Reference><Citation>Free Radic Res. 2005 Jun;39(6):573-80</Citation><ArticleIdList><ArticleId IdType="pubmed">16036334</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2005 Aug 9;44(31):10583-92</Citation><ArticleIdList><ArticleId IdType="pubmed">16060667</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2006 Jun 30;312(5782):1882-3</Citation><ArticleIdList><ArticleId IdType="pubmed">16809515</ArticleId></ArticleIdList></Reference><Reference><Citation>Cancer Res. 2006 Jul 1;66(13):6800-6</Citation><ArticleIdList><ArticleId IdType="pubmed">16818657</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Oct 20;281(42):31736-42</Citation><ArticleIdList><ArticleId IdType="pubmed">16916801</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2006 Dec 26;45(51):15301-9</Citation><ArticleIdList><ArticleId IdType="pubmed">17176052</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2007 Jul 27;282(30):22011-22</Citation><ArticleIdList><ArticleId IdType="pubmed">17519234</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Pharmacol. 2007 Aug;7(4):381-91</Citation><ArticleIdList><ArticleId IdType="pubmed">17662654</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2008 Jan 4;283(1):284-93</Citation><ArticleIdList><ArticleId IdType="pubmed">17974571</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1999 Dec 3;274(49):34543-6</Citation><ArticleIdList><ArticleId IdType="pubmed">10574916</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Chock, P Boon" sort="Chock, P Boon" uniqKey="Chock P" first="P Boon" last="Chock">P Boon Chock</name><name sortKey="Mieyal, John J" sort="Mieyal, John J" uniqKey="Mieyal J" first="John J" last="Mieyal">John J. Mieyal</name><name sortKey="Rhee, Sue Goo" sort="Rhee, Sue Goo" uniqKey="Rhee S" first="Sue Goo" last="Rhee">Sue Goo Rhee</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Park, Ji Won" sort="Park, Ji Won" uniqKey="Park J" first="Ji Won" last="Park">Ji Won Park</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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