Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta.
Identifieur interne : 000D56 ( Main/Exploration ); précédent : 000D55; suivant : 000D57Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta.
Auteurs : Niki L. Reynaert [États-Unis] ; Albert Van Der Vliet ; Amy S. Guala ; Toby Mcgovern ; Milena Hristova ; Cristen Pantano ; Nicholas H. Heintz ; John Heim ; Ye-Shih Ho ; Dwight E. Matthews ; Emiel F M. Wouters ; Yvonne M W. Janssen-HeiningerSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2006.
Descripteurs français
- KwdFr :
- Acides sulféniques (métabolisme), Animaux (MeSH), Appareil respiratoire (cytologie), Appareil respiratoire (effets des médicaments et des substances chimiques), Cellules cultivées (MeSH), Chimiokine CXCL2 (MeSH), Chimiokines (biosynthèse), Cystéine (métabolisme), Facteur de transcription NF-kappa B (métabolisme), Glutarédoxines (MeSH), Glutathion (métabolisme), I-kappa B Kinase (antagonistes et inhibiteurs), Kératinocytes (cytologie), Kératinocytes (effets des médicaments et des substances chimiques), Lipopolysaccharides (immunologie), Monokines (métabolisme), Oxidoreductases (déficit), Oxidoreductases (métabolisme), Oxydoréduction (effets des médicaments et des substances chimiques), Peroxyde d'hydrogène (pharmacologie), Souris (MeSH), Souris de lignée C57BL (MeSH), Sous-unités de protéines (métabolisme).
- MESH :
- antagonistes et inhibiteurs : I-kappa B Kinase.
- biosynthèse : Chimiokines.
- cytologie : Appareil respiratoire, Kératinocytes.
- déficit : Oxidoreductases.
- effets des médicaments et des substances chimiques : Appareil respiratoire, Kératinocytes, Oxydoréduction.
- immunologie : Lipopolysaccharides.
- métabolisme : Acides sulféniques, Cystéine, Facteur de transcription NF-kappa B, Glutathion, Monokines, Oxidoreductases, Sous-unités de protéines.
- pharmacologie : Peroxyde d'hydrogène.
- Animaux, Cellules cultivées, Chimiokine CXCL2, Glutarédoxines, Souris, Souris de lignée C57BL.
English descriptors
- KwdEn :
- Animals (MeSH), Cells, Cultured (MeSH), Chemokine CXCL2 (MeSH), Chemokines (biosynthesis), Cysteine (metabolism), Glutaredoxins (MeSH), Glutathione (metabolism), Hydrogen Peroxide (pharmacology), I-kappa B Kinase (antagonists & inhibitors), Keratinocytes (cytology), Keratinocytes (drug effects), Lipopolysaccharides (immunology), Mice (MeSH), Mice, Inbred C57BL (MeSH), Monokines (metabolism), NF-kappa B (metabolism), Oxidation-Reduction (drug effects), Oxidoreductases (deficiency), Oxidoreductases (metabolism), Protein Subunits (metabolism), Respiratory System (cytology), Respiratory System (drug effects), Sulfenic Acids (metabolism).
- MESH :
- chemical , antagonists & inhibitors : I-kappa B Kinase.
- chemical , biosynthesis : Chemokines.
- chemical , deficiency : Oxidoreductases.
- chemical , immunology : Lipopolysaccharides.
- chemical , metabolism : Cysteine, Glutathione, Monokines, NF-kappa B, Oxidoreductases, Protein Subunits, Sulfenic Acids.
- chemical , pharmacology : Hydrogen Peroxide.
- chemical : Chemokine CXCL2, Glutaredoxins.
- cytology : Keratinocytes, Respiratory System.
- drug effects : Keratinocytes, Oxidation-Reduction, Respiratory System.
- Animals, Cells, Cultured, Mice, Mice, Inbred C57BL.
Abstract
The transcription factor NF-kappaB, a central regulator of immunity, is subject to regulation by redox changes. We now report that cysteine-179 of the inhibitory kappaB kinase (IKK) beta-subunit of the IKK signalosome is a central target for oxidative inactivation by means of S-glutathionylation. S-glutathionylation of IKK-beta Cys-179 is reversed by glutaredoxin (GRX), which restores kinase activity. Conversely, GRX1 knockdown sensitizes cells to oxidative inactivation of IKK-beta and dampens TNF-alpha-induced IKK and NF-kappaB activation. Primary tracheal epithelial cells from Glrx1-deficient mice display reduced NF-kappaB DNA binding, RelA nuclear translocation, and MIP-2 (macrophage inflammatory protein 2) and keratinocyte-derived chemokine production in response to LPS. Collectively, these findings demonstrate the physiological relevance of the S-glutathionylation-GRX redox module in controlling the magnitude of activation of the NF-kappaB pathway.
DOI: 10.1073/pnas.0603290103
PubMed: 16916935
PubMed Central: PMC1559757
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Reynaert</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pathology and Chemistry, University of Vermont, Burlington, 05405, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology and Chemistry, University of Vermont, Burlington, 05405</wicri:regionArea><wicri:noRegion>05405</wicri:noRegion></affiliation></author><author><name sortKey="Van Der Vliet, Albert" sort="Van Der Vliet, Albert" uniqKey="Van Der Vliet A" first="Albert" last="Van Der Vliet">Albert Van Der Vliet</name></author><author><name sortKey="Guala, Amy S" sort="Guala, Amy S" uniqKey="Guala A" first="Amy S" last="Guala">Amy S. Guala</name></author><author><name sortKey="Mcgovern, Toby" sort="Mcgovern, Toby" uniqKey="Mcgovern T" first="Toby" last="Mcgovern">Toby Mcgovern</name></author><author><name sortKey="Hristova, Milena" sort="Hristova, Milena" uniqKey="Hristova M" first="Milena" last="Hristova">Milena Hristova</name></author><author><name sortKey="Pantano, Cristen" sort="Pantano, Cristen" uniqKey="Pantano C" first="Cristen" last="Pantano">Cristen Pantano</name></author><author><name sortKey="Heintz, Nicholas H" sort="Heintz, Nicholas H" uniqKey="Heintz N" first="Nicholas H" last="Heintz">Nicholas H. Heintz</name></author><author><name sortKey="Heim, John" sort="Heim, John" uniqKey="Heim J" first="John" last="Heim">John Heim</name></author><author><name sortKey="Ho, Ye Shih" sort="Ho, Ye Shih" uniqKey="Ho Y" first="Ye-Shih" last="Ho">Ye-Shih Ho</name></author><author><name sortKey="Matthews, Dwight E" sort="Matthews, Dwight E" uniqKey="Matthews D" first="Dwight E" last="Matthews">Dwight E. Matthews</name></author><author><name sortKey="Wouters, Emiel F M" sort="Wouters, Emiel F M" uniqKey="Wouters E" first="Emiel F M" last="Wouters">Emiel F M. Wouters</name></author><author><name sortKey="Janssen Heininger, Yvonne M W" sort="Janssen Heininger, Yvonne M W" uniqKey="Janssen Heininger Y" first="Yvonne M W" last="Janssen-Heininger">Yvonne M W. Janssen-Heininger</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cells, Cultured (MeSH)</term><term>Chemokine CXCL2 (MeSH)</term><term>Chemokines (biosynthesis)</term><term>Cysteine (metabolism)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (metabolism)</term><term>Hydrogen Peroxide (pharmacology)</term><term>I-kappa B Kinase (antagonists & inhibitors)</term><term>Keratinocytes (cytology)</term><term>Keratinocytes (drug effects)</term><term>Lipopolysaccharides (immunology)</term><term>Mice (MeSH)</term><term>Mice, Inbred C57BL (MeSH)</term><term>Monokines (metabolism)</term><term>NF-kappa B (metabolism)</term><term>Oxidation-Reduction (drug effects)</term><term>Oxidoreductases (deficiency)</term><term>Oxidoreductases (metabolism)</term><term>Protein Subunits (metabolism)</term><term>Respiratory System (cytology)</term><term>Respiratory System (drug effects)</term><term>Sulfenic Acids (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides sulféniques (métabolisme)</term><term>Animaux (MeSH)</term><term>Appareil respiratoire (cytologie)</term><term>Appareil respiratoire (effets des médicaments et des substances chimiques)</term><term>Cellules cultivées (MeSH)</term><term>Chimiokine CXCL2 (MeSH)</term><term>Chimiokines (biosynthèse)</term><term>Cystéine (métabolisme)</term><term>Facteur de transcription NF-kappa B (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (métabolisme)</term><term>I-kappa B Kinase (antagonistes et inhibiteurs)</term><term>Kératinocytes (cytologie)</term><term>Kératinocytes (effets des médicaments et des substances chimiques)</term><term>Lipopolysaccharides (immunologie)</term><term>Monokines (métabolisme)</term><term>Oxidoreductases (déficit)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (effets des médicaments et des substances chimiques)</term><term>Peroxyde d'hydrogène (pharmacologie)</term><term>Souris (MeSH)</term><term>Souris de lignée C57BL (MeSH)</term><term>Sous-unités de protéines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>I-kappa B Kinase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Chemokines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Lipopolysaccharides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term><term>Glutathione</term><term>Monokines</term><term>NF-kappa B</term><term>Oxidoreductases</term><term>Protein Subunits</term><term>Sulfenic Acids</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Hydrogen Peroxide</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Chemokine CXCL2</term><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>I-kappa B Kinase</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Chimiokines</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Appareil respiratoire</term><term>Kératinocytes</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Keratinocytes</term><term>Respiratory System</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Keratinocytes</term><term>Oxidation-Reduction</term><term>Respiratory System</term></keywords><keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Appareil respiratoire</term><term>Kératinocytes</term><term>Oxydoréduction</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Lipopolysaccharides</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides sulféniques</term><term>Cystéine</term><term>Facteur de transcription NF-kappa B</term><term>Glutathion</term><term>Monokines</term><term>Oxidoreductases</term><term>Sous-unités de protéines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Peroxyde d'hydrogène</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Mice</term><term>Mice, Inbred C57BL</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules cultivées</term><term>Chimiokine CXCL2</term><term>Glutarédoxines</term><term>Souris</term><term>Souris de lignée C57BL</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The transcription factor NF-kappaB, a central regulator of immunity, is subject to regulation by redox changes. We now report that cysteine-179 of the inhibitory kappaB kinase (IKK) beta-subunit of the IKK signalosome is a central target for oxidative inactivation by means of S-glutathionylation. S-glutathionylation of IKK-beta Cys-179 is reversed by glutaredoxin (GRX), which restores kinase activity. Conversely, GRX1 knockdown sensitizes cells to oxidative inactivation of IKK-beta and dampens TNF-alpha-induced IKK and NF-kappaB activation. Primary tracheal epithelial cells from Glrx1-deficient mice display reduced NF-kappaB DNA binding, RelA nuclear translocation, and MIP-2 (macrophage inflammatory protein 2) and keratinocyte-derived chemokine production in response to LPS. Collectively, these findings demonstrate the physiological relevance of the S-glutathionylation-GRX redox module in controlling the magnitude of activation of the NF-kappaB pathway.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16916935</PMID><DateCompleted><Year>2006</Year><Month>09</Month><Day>29</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>103</Volume><Issue>35</Issue><PubDate><Year>2006</Year><Month>Aug</Month><Day>29</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta.</ArticleTitle><Pagination><MedlinePgn>13086-91</MedlinePgn></Pagination><Abstract><AbstractText>The transcription factor NF-kappaB, a central regulator of immunity, is subject to regulation by redox changes. We now report that cysteine-179 of the inhibitory kappaB kinase (IKK) beta-subunit of the IKK signalosome is a central target for oxidative inactivation by means of S-glutathionylation. S-glutathionylation of IKK-beta Cys-179 is reversed by glutaredoxin (GRX), which restores kinase activity. Conversely, GRX1 knockdown sensitizes cells to oxidative inactivation of IKK-beta and dampens TNF-alpha-induced IKK and NF-kappaB activation. Primary tracheal epithelial cells from Glrx1-deficient mice display reduced NF-kappaB DNA binding, RelA nuclear translocation, and MIP-2 (macrophage inflammatory protein 2) and keratinocyte-derived chemokine production in response to LPS. Collectively, these findings demonstrate the physiological relevance of the S-glutathionylation-GRX redox module in controlling the magnitude of activation of the NF-kappaB pathway.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Reynaert</LastName><ForeName>Niki L</ForeName><Initials>NL</Initials><AffiliationInfo><Affiliation>Department of Pathology and Chemistry, University of Vermont, Burlington, 05405, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>van der Vliet</LastName><ForeName>Albert</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Guala</LastName><ForeName>Amy S</ForeName><Initials>AS</Initials></Author><Author ValidYN="Y"><LastName>McGovern</LastName><ForeName>Toby</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Hristova</LastName><ForeName>Milena</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Pantano</LastName><ForeName>Cristen</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Heintz</LastName><ForeName>Nicholas H</ForeName><Initials>NH</Initials></Author><Author ValidYN="Y"><LastName>Heim</LastName><ForeName>John</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Ho</LastName><ForeName>Ye-Shih</ForeName><Initials>YS</Initials></Author><Author ValidYN="Y"><LastName>Matthews</LastName><ForeName>Dwight E</ForeName><Initials>DE</Initials></Author><Author ValidYN="Y"><LastName>Wouters</LastName><ForeName>Emiel F M</ForeName><Initials>EF</Initials></Author><Author ValidYN="Y"><LastName>Janssen-Heininger</LastName><ForeName>Yvonne M W</ForeName><Initials>YM</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 HL060812</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P20 RR015557</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL060014</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P20 RL15557</GrantID><Agency>PHS HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL60014</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 HL074295</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>HL60812</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P01 HL074295</GrantID><Acronym>HL</Acronym><Agency>NHLBI 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="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>08</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054426">Chemokine CXCL2</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018925">Chemokines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516006">Glrx protein, mouse</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008070">Lipopolysaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015846">Monokines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016328">NF-kappa B</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D021122">Protein Subunits</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013434">Sulfenic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.10</RegistryNumber><NameOfSubstance UI="D051550">I-kappa B Kinase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054426" MajorTopicYN="N">Chemokine CXCL2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018925" MajorTopicYN="N">Chemokines</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" 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MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021122" MajorTopicYN="N">Protein Subunits</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012137" MajorTopicYN="N">Respiratory System</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013434" MajorTopicYN="N">Sulfenic Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>8</Month><Day>19</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>9</Month><Day>30</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>8</Month><Day>19</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16916935</ArticleId><ArticleId IdType="pii">0603290103</ArticleId><ArticleId IdType="doi">10.1073/pnas.0603290103</ArticleId><ArticleId IdType="pmc">PMC1559757</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Nature. 2000 Jan 6;403(6765):103-8</Citation><ArticleIdList><ArticleId IdType="pubmed">10638762</ArticleId></ArticleIdList></Reference><Reference><Citation>In Vitro. 1982 Sep;18(9):800-12</Citation><ArticleIdList><ArticleId IdType="pubmed">6757109</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2000 Nov 17;275(46):36062-6</Citation><ArticleIdList><ArticleId IdType="pubmed">10967126</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 2001 Apr 1;355(Pt 1):145-53</Citation><ArticleIdList><ArticleId IdType="pubmed">11256959</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Jul 13;276(28):26269-75</Citation><ArticleIdList><ArticleId IdType="pubmed">11297543</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Aug 10;276(32):30374-80</Citation><ArticleIdList><ArticleId IdType="pubmed">11397793</ArticleId></ArticleIdList></Reference><Reference><Citation>Chem Biol. 2001 Aug;8(8):759-66</Citation><ArticleIdList><ArticleId IdType="pubmed">11514225</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Sep 21;276(38):35693-700</Citation><ArticleIdList><ArticleId IdType="pubmed">11479295</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2001 Nov 27;40(47):14134-42</Citation><ArticleIdList><ArticleId IdType="pubmed">11714266</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Dec 21;276(51):47763-6</Citation><ArticleIdList><ArticleId IdType="pubmed">11684673</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2003 Jan 3;278(1):679-85</Citation><ArticleIdList><ArticleId IdType="pubmed">12409293</ArticleId></ArticleIdList></Reference><Reference><Citation>Exp Mol Med. 2003 Apr 30;35(2):61-6</Citation><ArticleIdList><ArticleId IdType="pubmed">12754408</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2003 Jun 5;423(6940):655-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12789342</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2003 Jun 5;423(6940):659-63</Citation><ArticleIdList><ArticleId IdType="pubmed">12789343</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2003 Nov 7;278(45):44091-6</Citation><ArticleIdList><ArticleId IdType="pubmed">12939259</ArticleId></ArticleIdList></Reference><Reference><Citation>Antioxid Redox Signal. 2004 Feb;6(1):63-74</Citation><ArticleIdList><ArticleId IdType="pubmed">14713336</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Rev Immunol. 2004 Mar;4(3):181-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15039755</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2004 Apr 23;304(5670):596-600</Citation><ArticleIdList><ArticleId IdType="pubmed">15105503</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8945-50</Citation><ArticleIdList><ArticleId IdType="pubmed">15184672</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1993 Apr 6;32(13):3368-76</Citation><ArticleIdList><ArticleId IdType="pubmed">8461300</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1996 Feb 20;35(7):2482-8</Citation><ArticleIdList><ArticleId IdType="pubmed">8652592</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 1996 Jun 15;24(12):2236-42</Citation><ArticleIdList><ArticleId IdType="pubmed">8710491</ArticleId></ArticleIdList></Reference><Reference><Citation>Am J Pathol. 1997 Aug;151(2):389-401</Citation><ArticleIdList><ArticleId IdType="pubmed">9250152</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1997 Aug 7;388(6642):548-54</Citation><ArticleIdList><ArticleId IdType="pubmed">9252186</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1997 Oct 31;278(5339):860-6</Citation><ArticleIdList><ArticleId IdType="pubmed">9346484</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1998 Sep 17;395(6699):297-300</Citation><ArticleIdList><ArticleId IdType="pubmed">9751060</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1998 Dec 8;37(49):17145-56</Citation><ArticleIdList><ArticleId IdType="pubmed">9860827</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1999 Apr 9;284(5412):309-13</Citation><ArticleIdList><ArticleId IdType="pubmed">10195894</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1999 Apr 9;284(5412):271-3</Citation><ArticleIdList><ArticleId IdType="pubmed">10232975</ArticleId></ArticleIdList></Reference><Reference><Citation>FASEB J. 1999 Sep;13(12):1481-90</Citation><ArticleIdList><ArticleId IdType="pubmed">10463938</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Med. 2004 Nov;10(11):1200-7</Citation><ArticleIdList><ArticleId IdType="pubmed">15489859</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>J Biol Chem. 2005 Feb 4;280(5):3125-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15590625</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>Biochim Biophys Acta. 2006 Mar;1760(3):380-7</Citation><ArticleIdList><ArticleId IdType="pubmed">16515838</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2004 Sep 28;43(38):12177-88</Citation><ArticleIdList><ArticleId IdType="pubmed">15379556</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 2000 Jun 30;476(1-2):52-4</Citation><ArticleIdList><ArticleId IdType="pubmed">10878249</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Guala, Amy S" sort="Guala, Amy S" uniqKey="Guala A" first="Amy S" last="Guala">Amy S. Guala</name><name sortKey="Heim, John" sort="Heim, John" uniqKey="Heim J" first="John" last="Heim">John Heim</name><name sortKey="Heintz, Nicholas H" sort="Heintz, Nicholas H" uniqKey="Heintz N" first="Nicholas H" last="Heintz">Nicholas H. Heintz</name><name sortKey="Ho, Ye Shih" sort="Ho, Ye Shih" uniqKey="Ho Y" first="Ye-Shih" last="Ho">Ye-Shih Ho</name><name sortKey="Hristova, Milena" sort="Hristova, Milena" uniqKey="Hristova M" first="Milena" last="Hristova">Milena Hristova</name><name sortKey="Janssen Heininger, Yvonne M W" sort="Janssen Heininger, Yvonne M W" uniqKey="Janssen Heininger Y" first="Yvonne M W" last="Janssen-Heininger">Yvonne M W. Janssen-Heininger</name><name sortKey="Matthews, Dwight E" sort="Matthews, Dwight E" uniqKey="Matthews D" first="Dwight E" last="Matthews">Dwight E. Matthews</name><name sortKey="Mcgovern, Toby" sort="Mcgovern, Toby" uniqKey="Mcgovern T" first="Toby" last="Mcgovern">Toby Mcgovern</name><name sortKey="Pantano, Cristen" sort="Pantano, Cristen" uniqKey="Pantano C" first="Cristen" last="Pantano">Cristen Pantano</name><name sortKey="Van Der Vliet, Albert" sort="Van Der Vliet, Albert" uniqKey="Van Der Vliet A" first="Albert" last="Van Der Vliet">Albert Van Der Vliet</name><name sortKey="Wouters, Emiel F M" sort="Wouters, Emiel F M" uniqKey="Wouters E" first="Emiel F M" last="Wouters">Emiel F M. Wouters</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Reynaert, Niki L" sort="Reynaert, Niki L" uniqKey="Reynaert N" first="Niki L" last="Reynaert">Niki L. Reynaert</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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