GlutaredoxinV1, Main, Exploration, bibRecord, 000027

Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins.

Identifieur interne : 000027 ( Main/Exploration ); précédent : 000026; suivant : 000028

Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins.

Auteurs : Linda Liedgens [Allemagne] ; Jannik Zimmermann [Allemagne] ; Lucas W Schenbach [Allemagne] ; Fabian Geissel [Allemagne] ; Hugo Laporte [Allemagne] ; Holger Gohlke [Allemagne] ; Bruce Morgan [Allemagne] ; Marcel Deponte [Allemagne]

Source :

Nature communications [ 2041-1723 ] ; 2020.

RBID : pubmed:32265442

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (genetics), Catalysis (MeSH), Catalytic Domain (genetics), Disulfides (chemistry), Enzyme Activation (MeSH), Enzyme Assays (MeSH), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (chemistry), Glutathione (metabolism), Kinetics (MeSH), Models, Molecular (MeSH), Molecular Dynamics Simulation (MeSH), Mutation (MeSH), Oxidation-Reduction (MeSH), Protein Conformation, alpha-Helical (MeSH), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism).
MESH :
- chemical , chemistry : Disulfides, Glutaredoxins, Glutathione, Saccharomyces cerevisiae Proteins.
- cytology : Saccharomyces cerevisiae.
- enzymology : Saccharomyces cerevisiae.
- genetics : Amino Acid Sequence, Catalytic Domain, Glutaredoxins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Glutaredoxins, Glutathione, Saccharomyces cerevisiae Proteins.
- Catalysis, Enzyme Activation, Enzyme Assays, Kinetics, Models, Molecular, Molecular Dynamics Simulation, Mutation, Oxidation-Reduction, Protein Conformation, alpha-Helical.

Abstract

Class I glutaredoxins are enzymatically active, glutathione-dependent oxidoreductases, whilst class II glutaredoxins are typically enzymatically inactive, Fe-S cluster-binding proteins. Enzymatically active glutaredoxins harbor both a glutathione-scaffold site for reacting with glutathionylated disulfide substrates and a glutathione-activator site for reacting with reduced glutathione. Here, using yeast ScGrx7 as a model protein, we comprehensively identified and characterized key residues from four distinct protein regions, as well as the covalently bound glutathione moiety, and quantified their contribution to both interaction sites. Additionally, we developed a redox-sensitive GFP2-based assay, which allowed the real-time assessment of glutaredoxin structure-function relationships inside living cells. Finally, we employed this assay to rapidly screen multiple glutaredoxin mutants, ultimately enabling us to convert enzymatically active and inactive glutaredoxins into each other. In summary, we have gained a comprehensive understanding of the mechanistic underpinnings of glutaredoxin catalysis and have elucidated the determinant structural differences between the two main classes of glutaredoxins.

DOI: 10.1038/s41467-020-15441-3
PubMed: 32265442
PubMed Central: PMC7138851

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000065
to stream Main, to step Curation: 000065

Le document en format XML

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<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Mathematisch-Naturwissenschaftliche Fakultät, Institut für Pharmazeutische und Medizinische Chemie, Heinrich-Heine-Universität Düsseldorf, D-40225, Düsseldorf</wicri:regionArea>
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<affiliation wicri:level="3"><nlm:affiliation>John von Neumann Institute for Computing (NIC), Jülich Supercomputing Centre (JSC) & Institute of Complex Systems, ICS-6: Structural Biochemistry, Forschungszentrum Jülich GmbH, D-52425, Jülich, Germany. gohlke@uni-duesseldorf.de.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>John von Neumann Institute for Computing (NIC), Jülich Supercomputing Centre (JSC) & Institute of Complex Systems, ICS-6: Structural Biochemistry, Forschungszentrum Jülich GmbH, D-52425, Jülich</wicri:regionArea>
<placeName><region type="land" nuts="1">Rhénanie-du-Nord-Westphalie</region>
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<author><name sortKey="Morgan, Bruce" sort="Morgan, Bruce" uniqKey="Morgan B" first="Bruce" last="Morgan">Bruce Morgan</name>
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<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institut für Biochemie, Zentrum für Human- und Molekularbiologie (ZHMB), Universität des Saarlandes, D-66123, Saarbrücken</wicri:regionArea>
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<author><name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name>
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<term>Catalysis (MeSH)</term>
<term>Catalytic Domain (genetics)</term>
<term>Disulfides (chemistry)</term>
<term>Enzyme Activation (MeSH)</term>
<term>Enzyme Assays (MeSH)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione (chemistry)</term>
<term>Glutathione (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Dynamics Simulation (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Protein Conformation, alpha-Helical (MeSH)</term>
<term>Saccharomyces cerevisiae (cytology)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term>
<term>Catalyse (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Disulfures (composition chimique)</term>
<term>Domaine catalytique (génétique)</term>
<term>Dosages enzymatiques (MeSH)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (composition chimique)</term>
<term>Glutathion (métabolisme)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (composition chimique)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (cytologie)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Simulation de dynamique moléculaire (MeSH)</term>
<term>Structure en hélice alpha (MeSH)</term>
<term>Séquence d'acides aminés (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term>
<term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Disulfures</term>
<term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Protéines de Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Catalytic Domain</term>
<term>Glutaredoxins</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Domaine catalytique</term>
<term>Glutarédoxines</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Séquence d'acides aminés</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Protéines de Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Catalysis</term>
<term>Enzyme Activation</term>
<term>Enzyme Assays</term>
<term>Kinetics</term>
<term>Models, Molecular</term>
<term>Molecular Dynamics Simulation</term>
<term>Mutation</term>
<term>Oxidation-Reduction</term>
<term>Protein Conformation, alpha-Helical</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term>
<term>Catalyse</term>
<term>Cinétique</term>
<term>Dosages enzymatiques</term>
<term>Modèles moléculaires</term>
<term>Mutation</term>
<term>Oxydoréduction</term>
<term>Simulation de dynamique moléculaire</term>
<term>Structure en hélice alpha</term>
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<front><div type="abstract" xml:lang="en">Class I glutaredoxins are enzymatically active, glutathione-dependent oxidoreductases, whilst class II glutaredoxins are typically enzymatically inactive, Fe-S cluster-binding proteins. Enzymatically active glutaredoxins harbor both a glutathione-scaffold site for reacting with glutathionylated disulfide substrates and a glutathione-activator site for reacting with reduced glutathione. Here, using yeast ScGrx7 as a model protein, we comprehensively identified and characterized key residues from four distinct protein regions, as well as the covalently bound glutathione moiety, and quantified their contribution to both interaction sites. Additionally, we developed a redox-sensitive GFP2-based assay, which allowed the real-time assessment of glutaredoxin structure-function relationships inside living cells. Finally, we employed this assay to rapidly screen multiple glutaredoxin mutants, ultimately enabling us to convert enzymatically active and inactive glutaredoxins into each other. In summary, we have gained a comprehensive understanding of the mechanistic underpinnings of glutaredoxin catalysis and have elucidated the determinant structural differences between the two main classes of glutaredoxins.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32265442</PMID>
<DateCompleted><Year>2020</Year>
<Month>07</Month>
<Day>29</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>07</Month>
<Day>29</Day>
</DateRevised>
<Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2041-1723</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>11</Volume>
<Issue>1</Issue>
<PubDate><Year>2020</Year>
<Month>04</Month>
<Day>07</Day>
</PubDate>
</JournalIssue>
<Title>Nature communications</Title>
<ISOAbbreviation>Nat Commun</ISOAbbreviation>
</Journal>
<ArticleTitle>Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins.</ArticleTitle>
<Pagination><MedlinePgn>1725</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1038/s41467-020-15441-3</ELocationID>
<Abstract><AbstractText>Class I glutaredoxins are enzymatically active, glutathione-dependent oxidoreductases, whilst class II glutaredoxins are typically enzymatically inactive, Fe-S cluster-binding proteins. Enzymatically active glutaredoxins harbor both a glutathione-scaffold site for reacting with glutathionylated disulfide substrates and a glutathione-activator site for reacting with reduced glutathione. Here, using yeast ScGrx7 as a model protein, we comprehensively identified and characterized key residues from four distinct protein regions, as well as the covalently bound glutathione moiety, and quantified their contribution to both interaction sites. Additionally, we developed a redox-sensitive GFP2-based assay, which allowed the real-time assessment of glutaredoxin structure-function relationships inside living cells. Finally, we employed this assay to rapidly screen multiple glutaredoxin mutants, ultimately enabling us to convert enzymatically active and inactive glutaredoxins into each other. In summary, we have gained a comprehensive understanding of the mechanistic underpinnings of glutaredoxin catalysis and have elucidated the determinant structural differences between the two main classes of glutaredoxins.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liedgens</LastName>
<ForeName>Linda</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Fachbereich Chemie, Abteilung Biochemie, Technische Universität Kaiserslautern, D-67663, Kaiserslautern, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zimmermann</LastName>
<ForeName>Jannik</ForeName>
<Initials>J</Initials>
<Identifier Source="ORCID">0000-0002-3336-042X</Identifier>
<AffiliationInfo><Affiliation>Institut für Biochemie, Zentrum für Human- und Molekularbiologie (ZHMB), Universität des Saarlandes, D-66123, Saarbrücken, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wäschenbach</LastName>
<ForeName>Lucas</ForeName>
<Initials>L</Initials>
<Identifier Source="ORCID">0000-0003-0044-4552</Identifier>
<AffiliationInfo><Affiliation>Mathematisch-Naturwissenschaftliche Fakultät, Institut für Pharmazeutische und Medizinische Chemie, Heinrich-Heine-Universität Düsseldorf, D-40225, Düsseldorf, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Geissel</LastName>
<ForeName>Fabian</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>Fachbereich Chemie, Abteilung Biochemie, Technische Universität Kaiserslautern, D-67663, Kaiserslautern, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Laporte</LastName>
<ForeName>Hugo</ForeName>
<Initials>H</Initials>
<Identifier Source="ORCID">0000-0002-3402-4014</Identifier>
<AffiliationInfo><Affiliation>Institut für Biochemie, Zentrum für Human- und Molekularbiologie (ZHMB), Universität des Saarlandes, D-66123, Saarbrücken, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gohlke</LastName>
<ForeName>Holger</ForeName>
<Initials>H</Initials>
<Identifier Source="ORCID">0000-0001-8613-1447</Identifier>
<AffiliationInfo><Affiliation>Mathematisch-Naturwissenschaftliche Fakultät, Institut für Pharmazeutische und Medizinische Chemie, Heinrich-Heine-Universität Düsseldorf, D-40225, Düsseldorf, Germany. gohlke@uni-duesseldorf.de.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>John von Neumann Institute for Computing (NIC), Jülich Supercomputing Centre (JSC) & Institute of Complex Systems, ICS-6: Structural Biochemistry, Forschungszentrum Jülich GmbH, D-52425, Jülich, Germany. gohlke@uni-duesseldorf.de.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Morgan</LastName>
<ForeName>Bruce</ForeName>
<Initials>B</Initials>
<Identifier Source="ORCID">0000-0001-9393-1071</Identifier>
<AffiliationInfo><Affiliation>Institut für Biochemie, Zentrum für Human- und Molekularbiologie (ZHMB), Universität des Saarlandes, D-66123, Saarbrücken, Germany. bruce.morgan@uni-saarland.de.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Deponte</LastName>
<ForeName>Marcel</ForeName>
<Initials>M</Initials>
<Identifier Source="ORCID">0000-0003-2141-917X</Identifier>
<AffiliationInfo><Affiliation>Fachbereich Chemie, Abteilung Biochemie, Technische Universität Kaiserslautern, D-67663, Kaiserslautern, Germany. deponte@chemie.uni-kl.de.</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>04</Month>
<Day>07</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Nat Commun</MedlineTA>
<NlmUniqueID>101528555</NlmUniqueID>
<ISSNLinking>2041-1723</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D004220">Disulfides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C532450">GRX7 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber>
<NameOfSubstance UI="D005978">Glutathione</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D057075" MajorTopicYN="N">Enzyme Assays</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<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="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D056004" MajorTopicYN="N">Molecular Dynamics Simulation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000072756" MajorTopicYN="N">Protein Conformation, alpha-Helical</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName>
<QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year>
<Month>10</Month>
<Day>30</Day>
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<PubMedPubDate PubStatus="accepted"><Year>2020</Year>
<Month>03</Month>
<Day>04</Day>
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<Month>4</Month>
<Day>9</Day>
<Hour>6</Hour>
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<affiliations><list><country><li>Allemagne</li>
</country>
<region><li>District de Cologne</li>
<li>District de Düsseldorf</li>
<li>Rhénanie-Palatinat</li>
<li>Rhénanie-du-Nord-Westphalie</li>
<li>Sarre (Land)</li>
</region>
<settlement><li>Düsseldorf</li>
<li>Juliers</li>
<li>Kaiserslautern</li>
<li>Sarrebruck</li>
</settlement>
<orgName><li>Université technique de Kaiserslautern</li>
</orgName>
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<tree><country name="Allemagne"><region name="Rhénanie-Palatinat"><name sortKey="Liedgens, Linda" sort="Liedgens, Linda" uniqKey="Liedgens L" first="Linda" last="Liedgens">Linda Liedgens</name>
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<name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name>
<name sortKey="Geissel, Fabian" sort="Geissel, Fabian" uniqKey="Geissel F" first="Fabian" last="Geissel">Fabian Geissel</name>
<name sortKey="Gohlke, Holger" sort="Gohlke, Holger" uniqKey="Gohlke H" first="Holger" last="Gohlke">Holger Gohlke</name>
<name sortKey="Gohlke, Holger" sort="Gohlke, Holger" uniqKey="Gohlke H" first="Holger" last="Gohlke">Holger Gohlke</name>
<name sortKey="Laporte, Hugo" sort="Laporte, Hugo" uniqKey="Laporte H" first="Hugo" last="Laporte">Hugo Laporte</name>
<name sortKey="Morgan, Bruce" sort="Morgan, Bruce" uniqKey="Morgan B" first="Bruce" last="Morgan">Bruce Morgan</name>
<name sortKey="W Schenbach, Lucas" sort="W Schenbach, Lucas" uniqKey="W Schenbach L" first="Lucas" last="W Schenbach">Lucas W Schenbach</name>
<name sortKey="Zimmermann, Jannik" sort="Zimmermann, Jannik" uniqKey="Zimmermann J" first="Jannik" last="Zimmermann">Jannik Zimmermann</name>
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   |texte=   Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins.
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	Serveur d'exploration sur la glutarédoxine
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Serveur d'exploration sur la glutarédoxine

Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins.

Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins.

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