S-glutathionylation of human glyceraldehyde-3-phosphate dehydrogenase and possible role of Cys152-Cys156 disulfide bridge in the active site of the protein.
Identifieur interne : 000018 ( Main/Exploration ); précédent : 000017; suivant : 000019S-glutathionylation of human glyceraldehyde-3-phosphate dehydrogenase and possible role of Cys152-Cys156 disulfide bridge in the active site of the protein.
Auteurs : K V Barinova [Russie] ; M V Serebryakova [Russie] ; M A Eldarov [Russie] ; A A Kulikova [Russie] ; V A Mitkevich [Russie] ; V I Muronetz [Russie] ; E V Schmalhausen [Russie]Source :
- Biochimica et biophysica acta. General subjects [ 1872-8006 ] ; 2020.
Descripteurs français
- KwdFr :
- Catalyse (MeSH), Disulfure de glutathion (composition chimique), Disulfures (composition chimique), Domaine catalytique (effets des médicaments et des substances chimiques), Glutathion (composition chimique), Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating) (composition chimique), Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating) (génétique), Humains (MeSH), Oxydoréduction (effets des médicaments et des substances chimiques), Peroxyde d'hydrogène (composition chimique), Stress oxydatif (effets des médicaments et des substances chimiques).
- MESH :
- composition chimique : Disulfure de glutathion, Disulfures, Glutathion, Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating), Peroxyde d'hydrogène.
- effets des médicaments et des substances chimiques : Domaine catalytique, Oxydoréduction, Stress oxydatif.
- génétique : Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating).
- Catalyse, Humains.
English descriptors
- KwdEn :
- Catalysis (MeSH), Catalytic Domain (drug effects), Disulfides (chemistry), Glutathione (chemistry), Glutathione Disulfide (chemistry), Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) (chemistry), Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) (genetics), Humans (MeSH), Hydrogen Peroxide (chemistry), Oxidation-Reduction (drug effects), Oxidative Stress (drug effects).
- MESH :
- chemical , chemistry : Disulfides, Glutathione, Glutathione Disulfide, Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating), Hydrogen Peroxide.
- drug effects : Catalytic Domain, Oxidation-Reduction, Oxidative Stress.
- chemical , genetics : Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating).
- Catalysis, Humans.
Abstract
BACKGROUND
We previously showed that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is S-glutathionylated in the presence of H
METHODS
Human recombinant GAPDH with the mutation C156S (hGAPDH_C156S) was obtained to prevent the formation of the disulfide bridge. Properties of S-glutathionylated hGAPDH_C156S were studied in comparison with those of the wild-type protein hGAPDH.
RESULTS
S-glutathionylation of hGAPDH and hGAPDH_C156S results in the reversible inactivation of the proteins. In both cases, the modification results in corresponding mixed disulfides between the catalytic Cys152 and GSH. In the case of hGAPDH, the mixed disulfide breaks down yielding Cys152-Cys156 disulfide bridge in the active site. In hGAPDH_C156S, the mixed disulfide is stable. Differential scanning calorimetry method showed that S-glutathionylation leads to destabilization of hGAPDH molecule, but does not affect significantly hGAPDH_C156S. Reactivation of S-glutathionylated hGAPDH in the presence of GSH and glutaredoxin 1 is approximately two-fold more efficient compared to that of hGAPDH_C156S.
CONCLUSIONS
S-glutathionylation induces the formation of Cys152-Cys156 disulfide bond in the active site of hGAPDH, which results in structural changes of the protein molecule. Cys156 is important for reactivation of S-glutathionylated GAPDH by glutaredoxin 1.
GENERAL SIGNIFICANCE
The described mechanism may be important for interaction between GAPDH and other proteins and ligands, involved in cell signaling.
DOI: 10.1016/j.bbagen.2020.129560
PubMed: 32061786
Affiliations:
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Electronic address: shmal@belozersky.msu.ru.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32061786</idno><idno type="pmid">32061786</idno><idno type="doi">10.1016/j.bbagen.2020.129560</idno><idno type="wicri:Area/Main/Corpus">000083</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000083</idno><idno type="wicri:Area/Main/Curation">000083</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000083</idno><idno type="wicri:Area/Main/Exploration">000083</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">S-glutathionylation of human glyceraldehyde-3-phosphate dehydrogenase and possible role of Cys152-Cys156 disulfide bridge in the active site of the protein.</title><author><name sortKey="Barinova, K V" sort="Barinova, K V" uniqKey="Barinova K" first="K V" last="Barinova">K V Barinova</name><affiliation wicri:level="1"><nlm:affiliation>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Serebryakova, M V" sort="Serebryakova, M V" uniqKey="Serebryakova M" first="M V" last="Serebryakova">M V Serebryakova</name><affiliation wicri:level="1"><nlm:affiliation>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Eldarov, M A" sort="Eldarov, M A" uniqKey="Eldarov M" first="M A" last="Eldarov">M A Eldarov</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Bioengineering, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky prosp. 33-2, Moscow 119071, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Institute of Bioengineering, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky prosp. 33-2, Moscow 119071</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Kulikova, A A" sort="Kulikova, A A" uniqKey="Kulikova A" first="A A" last="Kulikova">A A Kulikova</name><affiliation wicri:level="1"><nlm:affiliation>Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova 32, Moscow 119991, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova 32, Moscow 119991</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Mitkevich, V A" sort="Mitkevich, V A" uniqKey="Mitkevich V" first="V A" last="Mitkevich">V A Mitkevich</name><affiliation wicri:level="1"><nlm:affiliation>Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova 32, Moscow 119991, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova 32, Moscow 119991</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Muronetz, V I" sort="Muronetz, V I" uniqKey="Muronetz V" first="V I" last="Muronetz">V I Muronetz</name><affiliation wicri:level="1"><nlm:affiliation>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119234, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119234</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Schmalhausen, E V" sort="Schmalhausen, E V" uniqKey="Schmalhausen E" first="E V" last="Schmalhausen">E V Schmalhausen</name><affiliation wicri:level="1"><nlm:affiliation>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia. Electronic address: shmal@belozersky.msu.ru.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta. General subjects</title><idno type="eISSN">1872-8006</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Catalysis (MeSH)</term><term>Catalytic Domain (drug effects)</term><term>Disulfides (chemistry)</term><term>Glutathione (chemistry)</term><term>Glutathione Disulfide (chemistry)</term><term>Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) (chemistry)</term><term>Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) (genetics)</term><term>Humans (MeSH)</term><term>Hydrogen Peroxide (chemistry)</term><term>Oxidation-Reduction (drug effects)</term><term>Oxidative Stress (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse (MeSH)</term><term>Disulfure de glutathion (composition chimique)</term><term>Disulfures (composition chimique)</term><term>Domaine catalytique (effets des médicaments et des substances chimiques)</term><term>Glutathion (composition chimique)</term><term>Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating) (composition chimique)</term><term>Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating) (génétique)</term><term>Humains (MeSH)</term><term>Oxydoréduction (effets des médicaments et des substances chimiques)</term><term>Peroxyde d'hydrogène (composition chimique)</term><term>Stress oxydatif (effets des médicaments et des substances chimiques)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term><term>Glutathione</term><term>Glutathione Disulfide</term><term>Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)</term><term>Hydrogen Peroxide</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Disulfure de glutathion</term><term>Disulfures</term><term>Glutathion</term><term>Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating)</term><term>Peroxyde d'hydrogène</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Catalytic Domain</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Domaine catalytique</term><term>Oxydoréduction</term><term>Stress oxydatif</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating)</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Humains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b></p><p>We previously showed that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is S-glutathionylated in the presence of H</p></div><div type="abstract" xml:lang="en"><p><b>METHODS</b></p><p>Human recombinant GAPDH with the mutation C156S (hGAPDH_C156S) was obtained to prevent the formation of the disulfide bridge. Properties of S-glutathionylated hGAPDH_C156S were studied in comparison with those of the wild-type protein hGAPDH.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>S-glutathionylation of hGAPDH and hGAPDH_C156S results in the reversible inactivation of the proteins. In both cases, the modification results in corresponding mixed disulfides between the catalytic Cys152 and GSH. In the case of hGAPDH, the mixed disulfide breaks down yielding Cys152-Cys156 disulfide bridge in the active site. In hGAPDH_C156S, the mixed disulfide is stable. Differential scanning calorimetry method showed that S-glutathionylation leads to destabilization of hGAPDH molecule, but does not affect significantly hGAPDH_C156S. Reactivation of S-glutathionylated hGAPDH in the presence of GSH and glutaredoxin 1 is approximately two-fold more efficient compared to that of hGAPDH_C156S.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b></p><p>S-glutathionylation induces the formation of Cys152-Cys156 disulfide bond in the active site of hGAPDH, which results in structural changes of the protein molecule. Cys156 is important for reactivation of S-glutathionylated GAPDH by glutaredoxin 1.</p></div><div type="abstract" xml:lang="en"><p><b>GENERAL SIGNIFICANCE</b></p><p>The described mechanism may be important for interaction between GAPDH and other proteins and ligands, involved in cell signaling.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32061786</PMID><DateCompleted><Year>2020</Year><Month>10</Month><Day>22</Day></DateCompleted><DateRevised><Year>2020</Year><Month>10</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-8006</ISSN><JournalIssue CitedMedium="Internet"><Volume>1864</Volume><Issue>6</Issue><PubDate><Year>2020</Year><Month>06</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta. General subjects</Title><ISOAbbreviation>Biochim Biophys Acta Gen Subj</ISOAbbreviation></Journal><ArticleTitle>S-glutathionylation of human glyceraldehyde-3-phosphate dehydrogenase and possible role of Cys152-Cys156 disulfide bridge in the active site of the protein.</ArticleTitle><Pagination><MedlinePgn>129560</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0304-4165(20)30050-7</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbagen.2020.129560</ELocationID><Abstract><AbstractText Label="BACKGROUND">We previously showed that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is S-glutathionylated in the presence of H<sub>2</sub>O<sub>2</sub> and GSH. S-glutathionylation was shown to result in the formation of a disulfide bridge in the active site of the protein. In the present work, the possible biological significance of the disulfide bridge was investigated.</AbstractText><AbstractText Label="METHODS">Human recombinant GAPDH with the mutation C156S (hGAPDH_C156S) was obtained to prevent the formation of the disulfide bridge. Properties of S-glutathionylated hGAPDH_C156S were studied in comparison with those of the wild-type protein hGAPDH.</AbstractText><AbstractText Label="RESULTS">S-glutathionylation of hGAPDH and hGAPDH_C156S results in the reversible inactivation of the proteins. In both cases, the modification results in corresponding mixed disulfides between the catalytic Cys152 and GSH. In the case of hGAPDH, the mixed disulfide breaks down yielding Cys152-Cys156 disulfide bridge in the active site. In hGAPDH_C156S, the mixed disulfide is stable. Differential scanning calorimetry method showed that S-glutathionylation leads to destabilization of hGAPDH molecule, but does not affect significantly hGAPDH_C156S. Reactivation of S-glutathionylated hGAPDH in the presence of GSH and glutaredoxin 1 is approximately two-fold more efficient compared to that of hGAPDH_C156S.</AbstractText><AbstractText Label="CONCLUSIONS">S-glutathionylation induces the formation of Cys152-Cys156 disulfide bond in the active site of hGAPDH, which results in structural changes of the protein molecule. Cys156 is important for reactivation of S-glutathionylated GAPDH by glutaredoxin 1.</AbstractText><AbstractText Label="GENERAL SIGNIFICANCE">The described mechanism may be important for interaction between GAPDH and other proteins and ligands, involved in cell signaling.</AbstractText><CopyrightInformation>Copyright © 2020 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Barinova</LastName><ForeName>K V</ForeName><Initials>KV</Initials><AffiliationInfo><Affiliation>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Serebryakova</LastName><ForeName>M V</ForeName><Initials>MV</Initials><AffiliationInfo><Affiliation>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Eldarov</LastName><ForeName>M A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Institute of Bioengineering, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky prosp. 33-2, Moscow 119071, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kulikova</LastName><ForeName>A A</ForeName><Initials>AA</Initials><AffiliationInfo><Affiliation>Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova 32, Moscow 119991, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mitkevich</LastName><ForeName>V A</ForeName><Initials>VA</Initials><AffiliationInfo><Affiliation>Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova 32, Moscow 119991, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Muronetz</LastName><ForeName>V I</ForeName><Initials>VI</Initials><AffiliationInfo><Affiliation>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119234, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schmalhausen</LastName><ForeName>E V</ForeName><Initials>EV</Initials><AffiliationInfo><Affiliation>Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia. Electronic address: shmal@belozersky.msu.ru.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>02</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Gen Subj</MedlineTA><NlmUniqueID>101731726</NlmUniqueID><ISSNLinking>0304-4165</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.2.1.12</RegistryNumber><NameOfSubstance UI="C000709228">GAPDH protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.2.1.12</RegistryNumber><NameOfSubstance UI="D024581">Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>ULW86O013H</RegistryNumber><NameOfSubstance UI="D019803">Glutathione Disulfide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="Y">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019803" MajorTopicYN="N">Glutathione Disulfide</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D024581" MajorTopicYN="N">Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Disulfide bridge</Keyword><Keyword MajorTopicYN="Y">Glutathione</Keyword><Keyword MajorTopicYN="Y">Glyceraldehyde-3-phosphate dehydrogenase</Keyword><Keyword MajorTopicYN="Y">Oxidation</Keyword><Keyword MajorTopicYN="Y">S-glutathionylation</Keyword></KeywordList><CoiStatement>Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>11</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>01</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>02</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>2</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>2</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32061786</ArticleId><ArticleId IdType="pii">S0304-4165(20)30050-7</ArticleId><ArticleId IdType="doi">10.1016/j.bbagen.2020.129560</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Russie</li></country><region><li>District fédéral central</li></region><settlement><li>Moscou</li></settlement></list><tree><country name="Russie"><region name="District fédéral central"><name sortKey="Barinova, K V" sort="Barinova, K V" uniqKey="Barinova K" first="K V" last="Barinova">K V Barinova</name></region><name sortKey="Eldarov, M A" sort="Eldarov, M A" uniqKey="Eldarov M" first="M A" last="Eldarov">M A Eldarov</name><name sortKey="Kulikova, A A" sort="Kulikova, A A" uniqKey="Kulikova A" first="A A" last="Kulikova">A A Kulikova</name><name sortKey="Mitkevich, V A" sort="Mitkevich, V A" uniqKey="Mitkevich V" first="V A" last="Mitkevich">V A Mitkevich</name><name sortKey="Muronetz, V I" sort="Muronetz, V I" uniqKey="Muronetz V" first="V I" last="Muronetz">V I Muronetz</name><name sortKey="Schmalhausen, E V" sort="Schmalhausen, E V" uniqKey="Schmalhausen E" first="E V" last="Schmalhausen">E V Schmalhausen</name><name sortKey="Serebryakova, M V" sort="Serebryakova, M V" uniqKey="Serebryakova M" first="M V" last="Serebryakova">M V Serebryakova</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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