Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism.
Identifieur interne : 000F22 ( Main/Exploration ); précédent : 000F21; suivant : 000F23Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism.
Auteurs : Stefan Rahlfs [Allemagne] ; Christine Nickel ; Marcel Deponte ; R Heiner Schirmer ; Katja BeckerSource :
- Redox report : communications in free radical research [ 1351-0002 ] ; 2003.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Humains (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Plasmodium falciparum (physiologie), Protéines (métabolisme), Protéines de protozoaire (physiologie), Prévision (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Thiorédoxines (métabolisme).
- MESH :
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Forecasting (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Plasmodium falciparum (physiology), Proteins (metabolism), Protozoan Proteins (physiology), Sequence Homology, Amino Acid (MeSH), Thioredoxins (metabolism).
- MESH :
- chemical , metabolism : Proteins, Thioredoxins.
- chemical , physiology : Protozoan Proteins.
- chemical : Glutaredoxins, Oxidoreductases.
- physiology : Plasmodium falciparum.
- Amino Acid Sequence, Animals, Forecasting, Humans, Molecular Sequence Data, Oxidation-Reduction, Sequence Homology, Amino Acid.
Abstract
Over the last few years, an increasing number of different functions have been ascribed to small redox-active proteins like thioredoxins (Trx) and glutaredoxins (Grx). These functions include redox regulation of transcription and translation, antioxidant defence, involvement in protein folding and cellular signalling, and reduction of ribonucleotide reductase. In the malarial parasite Plasmodium falciparum, a classical Trx and a typical Grx have been described as well as a number of Trx- and Grx-like proteins including monothiol glutaredoxins. Furthermore, plasmoredoxin, a redox-active protein related to Trx, has been characterized; plasmoredoxin is unique for malarial parasites, therefore having great potential as diagnostic tool. In this minireview, we summarize the current knowledge on members of the thioredoxin superfamily and their function in the malarial parasite P. falciparum.
DOI: 10.1179/135100003225002844
PubMed: 14962358
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism.</title><author><name sortKey="Rahlfs, Stefan" sort="Rahlfs, Stefan" uniqKey="Rahlfs S" first="Stefan" last="Rahlfs">Stefan Rahlfs</name><affiliation wicri:level="1"><nlm:affiliation>Interdisciplinary Research Center, Justus Liebig University, Giessen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Interdisciplinary Research Center, Justus Liebig University, Giessen</wicri:regionArea><wicri:noRegion>Giessen</wicri:noRegion><wicri:noRegion>Giessen</wicri:noRegion><wicri:noRegion>Giessen</wicri:noRegion></affiliation></author><author><name sortKey="Nickel, Christine" sort="Nickel, Christine" uniqKey="Nickel C" first="Christine" last="Nickel">Christine Nickel</name></author><author><name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name></author><author><name sortKey="Schirmer, R Heiner" sort="Schirmer, R Heiner" uniqKey="Schirmer R" first="R Heiner" last="Schirmer">R Heiner Schirmer</name></author><author><name sortKey="Becker, Katja" sort="Becker, Katja" uniqKey="Becker K" first="Katja" last="Becker">Katja Becker</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2003">2003</date><idno type="RBID">pubmed:14962358</idno><idno type="pmid">14962358</idno><idno type="doi">10.1179/135100003225002844</idno><idno type="wicri:Area/Main/Corpus">000E86</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000E86</idno><idno type="wicri:Area/Main/Curation">000E86</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000E86</idno><idno type="wicri:Area/Main/Exploration">000E86</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism.</title><author><name sortKey="Rahlfs, Stefan" sort="Rahlfs, Stefan" uniqKey="Rahlfs S" first="Stefan" last="Rahlfs">Stefan Rahlfs</name><affiliation wicri:level="1"><nlm:affiliation>Interdisciplinary Research Center, Justus Liebig University, Giessen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Interdisciplinary Research Center, Justus Liebig University, Giessen</wicri:regionArea><wicri:noRegion>Giessen</wicri:noRegion><wicri:noRegion>Giessen</wicri:noRegion><wicri:noRegion>Giessen</wicri:noRegion></affiliation></author><author><name sortKey="Nickel, Christine" sort="Nickel, Christine" uniqKey="Nickel C" first="Christine" last="Nickel">Christine Nickel</name></author><author><name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name></author><author><name sortKey="Schirmer, R Heiner" sort="Schirmer, R Heiner" uniqKey="Schirmer R" first="R Heiner" last="Schirmer">R Heiner Schirmer</name></author><author><name sortKey="Becker, Katja" sort="Becker, Katja" uniqKey="Becker K" first="Katja" last="Becker">Katja Becker</name></author></analytic><series><title level="j">Redox report : communications in free radical research</title><idno type="ISSN">1351-0002</idno><imprint><date when="2003" type="published">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Forecasting (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Humans (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Plasmodium falciparum (physiology)</term><term>Proteins (metabolism)</term><term>Protozoan Proteins (physiology)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Plasmodium falciparum (physiologie)</term><term>Protéines (métabolisme)</term><term>Protéines de protozoaire (physiologie)</term><term>Prévision (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Protozoan Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Plasmodium falciparum</term><term>Protéines de protozoaire</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Forecasting</term><term>Humans</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Humains</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Prévision</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Over the last few years, an increasing number of different functions have been ascribed to small redox-active proteins like thioredoxins (Trx) and glutaredoxins (Grx). These functions include redox regulation of transcription and translation, antioxidant defence, involvement in protein folding and cellular signalling, and reduction of ribonucleotide reductase. In the malarial parasite Plasmodium falciparum, a classical Trx and a typical Grx have been described as well as a number of Trx- and Grx-like proteins including monothiol glutaredoxins. Furthermore, plasmoredoxin, a redox-active protein related to Trx, has been characterized; plasmoredoxin is unique for malarial parasites, therefore having great potential as diagnostic tool. In this minireview, we summarize the current knowledge on members of the thioredoxin superfamily and their function in the malarial parasite P. falciparum.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14962358</PMID><DateCompleted><Year>2004</Year><Month>05</Month><Day>27</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1351-0002</ISSN><JournalIssue CitedMedium="Print"><Volume>8</Volume><Issue>5</Issue><PubDate><Year>2003</Year></PubDate></JournalIssue><Title>Redox report : communications in free radical research</Title><ISOAbbreviation>Redox Rep</ISOAbbreviation></Journal><ArticleTitle>Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism.</ArticleTitle><Pagination><MedlinePgn>246-50</MedlinePgn></Pagination><Abstract><AbstractText>Over the last few years, an increasing number of different functions have been ascribed to small redox-active proteins like thioredoxins (Trx) and glutaredoxins (Grx). These functions include redox regulation of transcription and translation, antioxidant defence, involvement in protein folding and cellular signalling, and reduction of ribonucleotide reductase. In the malarial parasite Plasmodium falciparum, a classical Trx and a typical Grx have been described as well as a number of Trx- and Grx-like proteins including monothiol glutaredoxins. Furthermore, plasmoredoxin, a redox-active protein related to Trx, has been characterized; plasmoredoxin is unique for malarial parasites, therefore having great potential as diagnostic tool. In this minireview, we summarize the current knowledge on members of the thioredoxin superfamily and their function in the malarial parasite P. falciparum.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rahlfs</LastName><ForeName>Stefan</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Interdisciplinary Research Center, Justus Liebig University, Giessen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nickel</LastName><ForeName>Christine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Deponte</LastName><ForeName>Marcel</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Schirmer</LastName><ForeName>R Heiner</ForeName><Initials>RH</Initials></Author><Author ValidYN="Y"><LastName>Becker</LastName><ForeName>Katja</ForeName><Initials>K</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Redox Rep</MedlineTA><NlmUniqueID>9511366</NlmUniqueID><ISSNLinking>1351-0002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516005">GLRX protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015800">Protozoan Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005544" MajorTopicYN="N">Forecasting</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010963" MajorTopicYN="N">Plasmodium falciparum</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015800" MajorTopicYN="N">Protozoan Proteins</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>31</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>2</Month><Day>14</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>5</Month><Day>28</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>2</Month><Day>14</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">14962358</ArticleId><ArticleId IdType="doi">10.1179/135100003225002844</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Becker, Katja" sort="Becker, Katja" uniqKey="Becker K" first="Katja" last="Becker">Katja Becker</name><name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name><name sortKey="Nickel, Christine" sort="Nickel, Christine" uniqKey="Nickel C" first="Christine" last="Nickel">Christine Nickel</name><name sortKey="Schirmer, R Heiner" sort="Schirmer, R Heiner" uniqKey="Schirmer R" first="R Heiner" last="Schirmer">R Heiner Schirmer</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Rahlfs, Stefan" sort="Rahlfs, Stefan" uniqKey="Rahlfs S" first="Stefan" last="Rahlfs">Stefan Rahlfs</name></noRegion></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 000F22 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000F22 | 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:14962358
|texte= Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:14962358" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |