Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome.
Identifieur interne : 000B72 ( Main/Exploration ); précédent : 000B71; suivant : 000B73Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome.
Auteurs : Gustavo M. Silva [Brésil] ; Luis E S. Netto ; Karen F. Discola ; Gilberto M. Piassa-Filho ; Daniel C. Pimenta ; José A. Bárcena ; Marilene DemasiSource :
- The FEBS journal [ 1742-464X ] ; 2008.
Descripteurs français
- KwdFr :
- Clonage moléculaire (MeSH), Cystéine (composition chimique), Cytosol (métabolisme), Glutarédoxines (métabolisme), Glutarédoxines (physiologie), Glutathion (composition chimique), Glutathion (métabolisme), Hydrolyse (MeSH), Modèles biologiques (MeSH), Oxydoréduction (MeSH), Proteasome endopeptidase complex (composition chimique), Proteasome endopeptidase complex (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (métabolisme), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Cystéine, Glutathion, Proteasome endopeptidase complex.
- métabolisme : Cytosol, Glutarédoxines, Glutathion, Proteasome endopeptidase complex, Saccharomyces cerevisiae, Thiorédoxines.
- physiologie : Glutarédoxines.
- Clonage moléculaire, Hydrolyse, Modèles biologiques, Oxydoréduction, Régulation de l'expression des gènes fongiques.
English descriptors
- KwdEn :
- Cloning, Molecular (MeSH), Cysteine (chemistry), Cytosol (metabolism), Gene Expression Regulation, Fungal (MeSH), Glutaredoxins (metabolism), Glutaredoxins (physiology), Glutathione (chemistry), Glutathione (metabolism), Hydrolysis (MeSH), Models, Biological (MeSH), Oxidation-Reduction (MeSH), Proteasome Endopeptidase Complex (chemistry), Proteasome Endopeptidase Complex (metabolism), Saccharomyces cerevisiae (metabolism), Thioredoxins (metabolism).
- MESH :
- chemical , chemistry : Cysteine, Glutathione, Proteasome Endopeptidase Complex.
- metabolism : Cytosol, Glutaredoxins, Glutathione, Proteasome Endopeptidase Complex, Saccharomyces cerevisiae, Thioredoxins.
- chemical , physiology : Glutaredoxins.
- Cloning, Molecular, Gene Expression Regulation, Fungal, Hydrolysis, Models, Biological, Oxidation-Reduction.
Abstract
The yeast 20S proteasome is subject to sulfhydryl redox alterations, such as the oxidation of cysteine residues (Cys-SH) into cysteine sulfenic acid (Cys-SOH), followed by S-glutathionylation (Cys-S-SG). Proteasome S-glutathionylation promotes partial loss of chymotrypsin-like activity and post-acidic cleavage without alteration of the trypsin-like proteasomal activity. Here we show that the 20S proteasome purified from stationary-phase cells was natively S-glutathionylated. Moreover, recombinant glutaredoxin 2 removes glutathione from natively or in vitro S-glutathionylated 20S proteasome, allowing the recovery of chymotrypsin-like activity and post-acidic cleavage. Glutaredoxin 2 deglutathionylase activity was dependent on its entry into the core particle, as demonstrated by stimulating S-glutathionylated proteasome opening. Under these conditions, deglutathionylation of the 20S proteasome and glutaredoxin 2 degradation were increased when compared to non-stimulated samples. Glutaredoxin 2 fragmentation by the 20S proteasome was evaluated by SDS-PAGE and mass spectrometry, and S-glutathionylation was evaluated by either western blot analyses with anti-glutathione IgG or by spectrophotometry with the thiol reactant 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. It was also observed in vivo that glutaredoxin 2 was ubiquitinated in cellular extracts of yeast cells grown in glucose-containing medium. Other cytoplasmic oxido-reductases, namely thioredoxins 1 and 2, were also active in 20S proteasome deglutathionylation by a similar mechanism. These results indicate for the first time that 20S proteasome cysteinyl redox modification is a regulated mechanism coupled to enzymatic deglutathionylase activity.
DOI: 10.1111/j.1742-4658.2008.06441.x
PubMed: 18435761
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome.</title><author><name sortKey="Silva, Gustavo M" sort="Silva, Gustavo M" uniqKey="Silva G" first="Gustavo M" last="Silva">Gustavo M. Silva</name><affiliation wicri:level="4"><nlm:affiliation>Instituto Butantan, Laboratório de Bioquímica e Biofísica, São Paulo, Brazil, and Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Instituto Butantan, Laboratório de Bioquímica e Biofísica, São Paulo, Brazil, and Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo</wicri:regionArea><placeName><settlement type="city">São Paulo</settlement><region type="state">État de São Paulo</region></placeName><orgName type="university">Université de São Paulo</orgName></affiliation></author><author><name sortKey="Netto, Luis E S" sort="Netto, Luis E S" uniqKey="Netto L" first="Luis E S" last="Netto">Luis E S. Netto</name></author><author><name sortKey="Discola, Karen F" sort="Discola, Karen F" uniqKey="Discola K" first="Karen F" last="Discola">Karen F. Discola</name></author><author><name sortKey="Piassa Filho, Gilberto M" sort="Piassa Filho, Gilberto M" uniqKey="Piassa Filho G" first="Gilberto M" last="Piassa-Filho">Gilberto M. Piassa-Filho</name></author><author><name sortKey="Pimenta, Daniel C" sort="Pimenta, Daniel C" uniqKey="Pimenta D" first="Daniel C" last="Pimenta">Daniel C. Pimenta</name></author><author><name sortKey="Barcena, Jose A" sort="Barcena, Jose A" uniqKey="Barcena J" first="José A" last="Bárcena">José A. Bárcena</name></author><author><name sortKey="Demasi, Marilene" sort="Demasi, Marilene" uniqKey="Demasi M" first="Marilene" last="Demasi">Marilene Demasi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18435761</idno><idno type="pmid">18435761</idno><idno type="doi">10.1111/j.1742-4658.2008.06441.x</idno><idno type="wicri:Area/Main/Corpus">000B95</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000B95</idno><idno type="wicri:Area/Main/Curation">000B95</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000B95</idno><idno type="wicri:Area/Main/Exploration">000B95</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome.</title><author><name sortKey="Silva, Gustavo M" sort="Silva, Gustavo M" uniqKey="Silva G" first="Gustavo M" last="Silva">Gustavo M. Silva</name><affiliation wicri:level="4"><nlm:affiliation>Instituto Butantan, Laboratório de Bioquímica e Biofísica, São Paulo, Brazil, and Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Instituto Butantan, Laboratório de Bioquímica e Biofísica, São Paulo, Brazil, and Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo</wicri:regionArea><placeName><settlement type="city">São Paulo</settlement><region type="state">État de São Paulo</region></placeName><orgName type="university">Université de São Paulo</orgName></affiliation></author><author><name sortKey="Netto, Luis E S" sort="Netto, Luis E S" uniqKey="Netto L" first="Luis E S" last="Netto">Luis E S. Netto</name></author><author><name sortKey="Discola, Karen F" sort="Discola, Karen F" uniqKey="Discola K" first="Karen F" last="Discola">Karen F. Discola</name></author><author><name sortKey="Piassa Filho, Gilberto M" sort="Piassa Filho, Gilberto M" uniqKey="Piassa Filho G" first="Gilberto M" last="Piassa-Filho">Gilberto M. Piassa-Filho</name></author><author><name sortKey="Pimenta, Daniel C" sort="Pimenta, Daniel C" uniqKey="Pimenta D" first="Daniel C" last="Pimenta">Daniel C. Pimenta</name></author><author><name sortKey="Barcena, Jose A" sort="Barcena, Jose A" uniqKey="Barcena J" first="José A" last="Bárcena">José A. Bárcena</name></author><author><name sortKey="Demasi, Marilene" sort="Demasi, Marilene" uniqKey="Demasi M" first="Marilene" last="Demasi">Marilene Demasi</name></author></analytic><series><title level="j">The FEBS journal</title><idno type="ISSN">1742-464X</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cloning, Molecular (MeSH)</term><term>Cysteine (chemistry)</term><term>Cytosol (metabolism)</term><term>Gene Expression Regulation, Fungal (MeSH)</term><term>Glutaredoxins (metabolism)</term><term>Glutaredoxins (physiology)</term><term>Glutathione (chemistry)</term><term>Glutathione (metabolism)</term><term>Hydrolysis (MeSH)</term><term>Models, Biological (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Proteasome Endopeptidase Complex (chemistry)</term><term>Proteasome Endopeptidase Complex (metabolism)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Clonage moléculaire (MeSH)</term><term>Cystéine (composition chimique)</term><term>Cytosol (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>Glutarédoxines (physiologie)</term><term>Glutathion (composition chimique)</term><term>Glutathion (métabolisme)</term><term>Hydrolyse (MeSH)</term><term>Modèles biologiques (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Proteasome endopeptidase complex (composition chimique)</term><term>Proteasome endopeptidase complex (métabolisme)</term><term>Régulation de l'expression des gènes fongiques (MeSH)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Glutathione</term><term>Proteasome Endopeptidase Complex</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Glutathion</term><term>Proteasome endopeptidase complex</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytosol</term><term>Glutaredoxins</term><term>Glutathione</term><term>Proteasome Endopeptidase Complex</term><term>Saccharomyces cerevisiae</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytosol</term><term>Glutarédoxines</term><term>Glutathion</term><term>Proteasome endopeptidase complex</term><term>Saccharomyces cerevisiae</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Gene Expression Regulation, Fungal</term><term>Hydrolysis</term><term>Models, Biological</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Hydrolyse</term><term>Modèles biologiques</term><term>Oxydoréduction</term><term>Régulation de l'expression des gènes fongiques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The yeast 20S proteasome is subject to sulfhydryl redox alterations, such as the oxidation of cysteine residues (Cys-SH) into cysteine sulfenic acid (Cys-SOH), followed by S-glutathionylation (Cys-S-SG). Proteasome S-glutathionylation promotes partial loss of chymotrypsin-like activity and post-acidic cleavage without alteration of the trypsin-like proteasomal activity. Here we show that the 20S proteasome purified from stationary-phase cells was natively S-glutathionylated. Moreover, recombinant glutaredoxin 2 removes glutathione from natively or in vitro S-glutathionylated 20S proteasome, allowing the recovery of chymotrypsin-like activity and post-acidic cleavage. Glutaredoxin 2 deglutathionylase activity was dependent on its entry into the core particle, as demonstrated by stimulating S-glutathionylated proteasome opening. Under these conditions, deglutathionylation of the 20S proteasome and glutaredoxin 2 degradation were increased when compared to non-stimulated samples. Glutaredoxin 2 fragmentation by the 20S proteasome was evaluated by SDS-PAGE and mass spectrometry, and S-glutathionylation was evaluated by either western blot analyses with anti-glutathione IgG or by spectrophotometry with the thiol reactant 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. It was also observed in vivo that glutaredoxin 2 was ubiquitinated in cellular extracts of yeast cells grown in glucose-containing medium. Other cytoplasmic oxido-reductases, namely thioredoxins 1 and 2, were also active in 20S proteasome deglutathionylation by a similar mechanism. These results indicate for the first time that 20S proteasome cysteinyl redox modification is a regulated mechanism coupled to enzymatic deglutathionylase activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18435761</PMID><DateCompleted><Year>2008</Year><Month>07</Month><Day>15</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1742-464X</ISSN><JournalIssue CitedMedium="Print"><Volume>275</Volume><Issue>11</Issue><PubDate><Year>2008</Year><Month>Jun</Month></PubDate></JournalIssue><Title>The FEBS journal</Title><ISOAbbreviation>FEBS J</ISOAbbreviation></Journal><ArticleTitle>Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome.</ArticleTitle><Pagination><MedlinePgn>2942-55</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1742-4658.2008.06441.x</ELocationID><Abstract><AbstractText>The yeast 20S proteasome is subject to sulfhydryl redox alterations, such as the oxidation of cysteine residues (Cys-SH) into cysteine sulfenic acid (Cys-SOH), followed by S-glutathionylation (Cys-S-SG). Proteasome S-glutathionylation promotes partial loss of chymotrypsin-like activity and post-acidic cleavage without alteration of the trypsin-like proteasomal activity. Here we show that the 20S proteasome purified from stationary-phase cells was natively S-glutathionylated. Moreover, recombinant glutaredoxin 2 removes glutathione from natively or in vitro S-glutathionylated 20S proteasome, allowing the recovery of chymotrypsin-like activity and post-acidic cleavage. Glutaredoxin 2 deglutathionylase activity was dependent on its entry into the core particle, as demonstrated by stimulating S-glutathionylated proteasome opening. Under these conditions, deglutathionylation of the 20S proteasome and glutaredoxin 2 degradation were increased when compared to non-stimulated samples. Glutaredoxin 2 fragmentation by the 20S proteasome was evaluated by SDS-PAGE and mass spectrometry, and S-glutathionylation was evaluated by either western blot analyses with anti-glutathione IgG or by spectrophotometry with the thiol reactant 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. It was also observed in vivo that glutaredoxin 2 was ubiquitinated in cellular extracts of yeast cells grown in glucose-containing medium. Other cytoplasmic oxido-reductases, namely thioredoxins 1 and 2, were also active in 20S proteasome deglutathionylation by a similar mechanism. These results indicate for the first time that 20S proteasome cysteinyl redox modification is a regulated mechanism coupled to enzymatic deglutathionylase activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Silva</LastName><ForeName>Gustavo M</ForeName><Initials>GM</Initials><AffiliationInfo><Affiliation>Instituto Butantan, Laboratório de Bioquímica e Biofísica, São Paulo, Brazil, and Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Netto</LastName><ForeName>Luis E S</ForeName><Initials>LE</Initials></Author><Author ValidYN="Y"><LastName>Discola</LastName><ForeName>Karen F</ForeName><Initials>KF</Initials></Author><Author ValidYN="Y"><LastName>Piassa-Filho</LastName><ForeName>Gilberto M</ForeName><Initials>GM</Initials></Author><Author ValidYN="Y"><LastName>Pimenta</LastName><ForeName>Daniel C</ForeName><Initials>DC</Initials></Author><Author ValidYN="Y"><LastName>Bárcena</LastName><ForeName>José A</ForeName><Initials>JA</Initials></Author><Author ValidYN="Y"><LastName>Demasi</LastName><ForeName>Marilene</ForeName><Initials>M</Initials></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>2008</Year><Month>04</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS J</MedlineTA><NlmUniqueID>101229646</NlmUniqueID><ISSNLinking>1742-464X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.25.1</RegistryNumber><NameOfSubstance UI="D046988">Proteasome Endopeptidase Complex</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="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="Y">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046988" MajorTopicYN="N">Proteasome Endopeptidase Complex</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>4</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>7</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>4</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18435761</ArticleId><ArticleId IdType="pii">EJB6441</ArticleId><ArticleId IdType="doi">10.1111/j.1742-4658.2008.06441.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Brésil</li></country><region><li>État de São Paulo</li></region><settlement><li>São Paulo</li></settlement><orgName><li>Université de São Paulo</li></orgName></list><tree><noCountry><name sortKey="Barcena, Jose A" sort="Barcena, Jose A" uniqKey="Barcena J" first="José A" last="Bárcena">José A. Bárcena</name><name sortKey="Demasi, Marilene" sort="Demasi, Marilene" uniqKey="Demasi M" first="Marilene" last="Demasi">Marilene Demasi</name><name sortKey="Discola, Karen F" sort="Discola, Karen F" uniqKey="Discola K" first="Karen F" last="Discola">Karen F. Discola</name><name sortKey="Netto, Luis E S" sort="Netto, Luis E S" uniqKey="Netto L" first="Luis E S" last="Netto">Luis E S. Netto</name><name sortKey="Piassa Filho, Gilberto M" sort="Piassa Filho, Gilberto M" uniqKey="Piassa Filho G" first="Gilberto M" last="Piassa-Filho">Gilberto M. Piassa-Filho</name><name sortKey="Pimenta, Daniel C" sort="Pimenta, Daniel C" uniqKey="Pimenta D" first="Daniel C" last="Pimenta">Daniel C. Pimenta</name></noCountry><country name="Brésil"><region name="État de São Paulo"><name sortKey="Silva, Gustavo M" sort="Silva, Gustavo M" uniqKey="Silva G" first="Gustavo M" last="Silva">Gustavo M. Silva</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000B72 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000B72 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:18435761
|texte= Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:18435761" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |