GlutaredoxinV1, Main, Exploration, bibRecord, 000B10

Lights on iron-sulfur clusters.

Identifieur interne : 000B10 ( Main/Exploration ); précédent : 000B09; suivant : 000B11

Lights on iron-sulfur clusters.

Auteurs : Christopher Horst Lillig [Allemagne] ; Roland Lill

Source :

Chemistry & biology [ 1879-1301 ] ; 2009.

RBID : pubmed:20064428

Descripteurs français

KwdFr :
- Dimérisation (MeSH), Fer (composition chimique), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Humains (MeSH), Lignée cellulaire (MeSH), Microscopie de fluorescence (MeSH), Mutation (MeSH), Protéines de fusion recombinantes (composition chimique), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines luminescentes (composition chimique), Protéines luminescentes (métabolisme), Soufre (composition chimique).
MESH :
- composition chimique : Fer, Glutarédoxines, Protéines de fusion recombinantes, Protéines luminescentes, Soufre.
- génétique : Glutarédoxines, Protéines de fusion recombinantes.
- métabolisme : Glutarédoxines, Protéines de fusion recombinantes, Protéines luminescentes.
- Dimérisation, Humains, Lignée cellulaire, Microscopie de fluorescence, Mutation.

English descriptors

KwdEn :
- Cell Line (MeSH), Dimerization (MeSH), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Humans (MeSH), Iron (chemistry), Luminescent Proteins (chemistry), Luminescent Proteins (metabolism), Microscopy, Fluorescence (MeSH), Mutation (MeSH), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Sulfur (chemistry).
MESH :
- chemical , chemistry : Glutaredoxins, Iron, Luminescent Proteins, Recombinant Fusion Proteins, Sulfur.
- chemical , genetics : Glutaredoxins, Recombinant Fusion Proteins.
- chemical , metabolism : Glutaredoxins, Luminescent Proteins, Recombinant Fusion Proteins.
- Cell Line, Dimerization, Humans, Microscopy, Fluorescence, Mutation.

Abstract

The biogenesis of iron-sulfur proteins within a living cell is traditionally investigated by enzyme activity measurements and radiolabeling techniques. In this issue of Chemistry and Biology, Hoff et al. introduce a non-invasive fluorescence-based method to trace the formation of iron-sulfur clusters at high sensitivity.

DOI: 10.1016/j.chembiol.2009.12.005
PubMed: 20064428

Affiliations:

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

to stream Main, to step Corpus: 000A41
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Le document en format XML

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<author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name>
<affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg</wicri:regionArea>
<placeName><region type="land" nuts="1">Hesse (Land)</region>
<region type="district" nuts="2">District de Giessen</region>
<settlement type="city">Marbourg</settlement>
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<author><name sortKey="Lill, Roland" sort="Lill, Roland" uniqKey="Lill R" first="Roland" last="Lill">Roland Lill</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Lights on iron-sulfur clusters.</title>
<author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name>
<affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany.</nlm:affiliation>
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<wicri:regionArea>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg</wicri:regionArea>
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<series><title level="j">Chemistry & biology</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line (MeSH)</term>
<term>Dimerization (MeSH)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Iron (chemistry)</term>
<term>Luminescent Proteins (chemistry)</term>
<term>Luminescent Proteins (metabolism)</term>
<term>Microscopy, Fluorescence (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Recombinant Fusion Proteins (chemistry)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Sulfur (chemistry)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Dimérisation (MeSH)</term>
<term>Fer (composition chimique)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Lignée cellulaire (MeSH)</term>
<term>Microscopie de fluorescence (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Protéines de fusion recombinantes (composition chimique)</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines luminescentes (composition chimique)</term>
<term>Protéines luminescentes (métabolisme)</term>
<term>Soufre (composition chimique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term>
<term>Iron</term>
<term>Luminescent Proteins</term>
<term>Recombinant Fusion Proteins</term>
<term>Sulfur</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Luminescent Proteins</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Fer</term>
<term>Glutarédoxines</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines luminescentes</term>
<term>Soufre</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term>
<term>Protéines de fusion recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines luminescentes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Cell Line</term>
<term>Dimerization</term>
<term>Humans</term>
<term>Microscopy, Fluorescence</term>
<term>Mutation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Dimérisation</term>
<term>Humains</term>
<term>Lignée cellulaire</term>
<term>Microscopie de fluorescence</term>
<term>Mutation</term>
</keywords>
</textClass>
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</teiHeader>
<front><div type="abstract" xml:lang="en">The biogenesis of iron-sulfur proteins within a living cell is traditionally investigated by enzyme activity measurements and radiolabeling techniques. In this issue of Chemistry and Biology, Hoff et al. introduce a non-invasive fluorescence-based method to trace the formation of iron-sulfur clusters at high sensitivity.</div>
</front>
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<DateCompleted><Year>2010</Year>
<Month>03</Month>
<Day>11</Day>
</DateCompleted>
<DateRevised><Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1879-1301</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>16</Volume>
<Issue>12</Issue>
<PubDate><Year>2009</Year>
<Month>Dec</Month>
<Day>24</Day>
</PubDate>
</JournalIssue>
<Title>Chemistry & biology</Title>
<ISOAbbreviation>Chem Biol</ISOAbbreviation>
</Journal>
<ArticleTitle>Lights on iron-sulfur clusters.</ArticleTitle>
<Pagination><MedlinePgn>1213-4</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.chembiol.2009.12.005</ELocationID>
<Abstract><AbstractText>The biogenesis of iron-sulfur proteins within a living cell is traditionally investigated by enzyme activity measurements and radiolabeling techniques. In this issue of Chemistry and Biology, Hoff et al. introduce a non-invasive fluorescence-based method to trace the formation of iron-sulfur clusters at high sensitivity.</AbstractText>
<CopyrightInformation>Copyright  2009 Elsevier Ltd. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lillig</LastName>
<ForeName>Christopher Horst</ForeName>
<Initials>CH</Initials>
<AffiliationInfo><Affiliation>Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lill</LastName>
<ForeName>Roland</ForeName>
<Initials>R</Initials>
</Author>
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<Language>eng</Language>
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<MedlineJournalInfo><Country>United States</Country>
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<NlmUniqueID>9500160</NlmUniqueID>
<ISSNLinking>1074-5521</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C516008">GLRX2 protein, human</NameOfSubstance>
</Chemical>
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<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
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<CommentsCorrectionsList><CommentsCorrections RefType="CommentOn"><RefSource>Chem Biol. 2009 Dec 24;16(12):1299-308</RefSource>
<PMID Version="1">20064440</PMID>
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</CommentsCorrectionsList>
<MeshHeadingList><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName>
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<MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName>
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<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
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<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008164" MajorTopicYN="N">Luminescent Proteins</DescriptorName>
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<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008856" MajorTopicYN="N">Microscopy, Fluorescence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
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<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013455" MajorTopicYN="N">Sulfur</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
</MeshHeadingList>
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<Day>13</Day>
<Hour>6</Hour>
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<country name="Allemagne"><region name="Hesse (Land)"><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name>
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Lights on iron-sulfur clusters.

Lights on iron-sulfur clusters.

Source :

Descripteurs français

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki