Nucleoredoxin, a novel thioredoxin family member involved in cell growth and differentiation.
Identifieur interne : 000C71 ( Main/Exploration ); précédent : 000C70; suivant : 000C72Nucleoredoxin, a novel thioredoxin family member involved in cell growth and differentiation.
Auteurs : Yosuke Funato [Japon] ; Hiroaki MikiSource :
- Antioxidants & redox signaling [ 1523-0864 ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Différenciation cellulaire (MeSH), Domaine catalytique (MeSH), Facteur de transcription NF-kappa B (métabolisme), Glutarédoxines (MeSH), Humains (MeSH), Modèles biologiques (MeSH), Motifs d'acides aminés (MeSH), Oxidoreductases (métabolisme), Oxidoreductases (physiologie), Oxydoréduction (MeSH), Phylogenèse (MeSH), Prolifération cellulaire (MeSH), Protéines nucléaires (métabolisme), Protéines nucléaires (physiologie), Spécificité d'espèce (MeSH), Structure tertiaire des protéines (MeSH), Thiorédoxines (métabolisme).
- MESH :
- métabolisme : Facteur de transcription NF-kappa B, Oxidoreductases, Protéines nucléaires, Thiorédoxines.
- physiologie : Oxidoreductases, Protéines nucléaires.
- Animaux, Différenciation cellulaire, Domaine catalytique, Glutarédoxines, Humains, Modèles biologiques, Motifs d'acides aminés, Oxydoréduction, Phylogenèse, Prolifération cellulaire, Spécificité d'espèce, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Animals (MeSH), Catalytic Domain (MeSH), Cell Differentiation (MeSH), Cell Proliferation (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Models, Biological (MeSH), NF-kappa B (metabolism), Nuclear Proteins (metabolism), Nuclear Proteins (physiology), Oxidation-Reduction (MeSH), Oxidoreductases (metabolism), Oxidoreductases (physiology), Phylogeny (MeSH), Protein Structure, Tertiary (MeSH), Species Specificity (MeSH), Thioredoxins (metabolism).
- MESH :
- chemical , metabolism : NF-kappa B, Nuclear Proteins, Oxidoreductases, Thioredoxins.
- chemical , physiology : Nuclear Proteins, Oxidoreductases.
- chemical : Glutaredoxins.
- Amino Acid Motifs, Animals, Catalytic Domain, Cell Differentiation, Cell Proliferation, Humans, Models, Biological, Oxidation-Reduction, Phylogeny, Protein Structure, Tertiary, Species Specificity.
Abstract
Thioredoxin (TRX) family proteins are involved in various biologic processes by regulating the response to oxidative stress. Nucleoredoxin (NRX), a relatively uncharacterized member of the TRX family protein, has recently been reported to regulate the Wnt/beta-catenin pathway, which itself regulates cell fate and early development, in a redox-dependent manner. In this review, we describe the TRX family proteins and discuss in detail the similarities and differences between NRX and other TRX family proteins. Although NRX possesses a conserved TRX domain and a catalytic motif for oxidoreductase activity, its sequence homology to TRX is not as high as that of the close relatives of TRX. The sequence of NRX is more similar to that of tryparedoxin (TryX), a TRX family member originally identified in parasite trypanosomes. We also discuss the reported properties and potential physiologic roles of NRX.
DOI: 10.1089/ars.2007.1550
PubMed: 17567240
Affiliations:
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Le document en format XML
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(metabolism)</term><term>Nuclear Proteins (metabolism)</term><term>Nuclear Proteins (physiology)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (metabolism)</term><term>Oxidoreductases (physiology)</term><term>Phylogeny (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Species Specificity (MeSH)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Différenciation cellulaire (MeSH)</term><term>Domaine catalytique (MeSH)</term><term>Facteur de transcription NF-kappa B (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Modèles biologiques (MeSH)</term><term>Motifs d'acides aminés (MeSH)</term><term>Oxidoreductases (métabolisme)</term><term>Oxidoreductases (physiologie)</term><term>Oxydoréduction (MeSH)</term><term>Phylogenèse (MeSH)</term><term>Prolifération cellulaire (MeSH)</term><term>Protéines nucléaires (métabolisme)</term><term>Protéines 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Nucleoredoxin (NRX), a relatively uncharacterized member of the TRX family protein, has recently been reported to regulate the Wnt/beta-catenin pathway, which itself regulates cell fate and early development, in a redox-dependent manner. In this review, we describe the TRX family proteins and discuss in detail the similarities and differences between NRX and other TRX family proteins. Although NRX possesses a conserved TRX domain and a catalytic motif for oxidoreductase activity, its sequence homology to TRX is not as high as that of the close relatives of TRX. The sequence of NRX is more similar to that of tryparedoxin (TryX), a TRX family member originally identified in parasite trypanosomes. We also discuss the reported properties and potential physiologic roles of NRX.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17567240</PMID><DateCompleted><Year>2007</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1523-0864</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>8</Issue><PubDate><Year>2007</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Nucleoredoxin, a novel thioredoxin family member involved in cell growth and differentiation.</ArticleTitle><Pagination><MedlinePgn>1035-57</MedlinePgn></Pagination><Abstract><AbstractText>Thioredoxin (TRX) family proteins are involved in various biologic processes by regulating the response to oxidative stress. Nucleoredoxin (NRX), a relatively uncharacterized member of the TRX family protein, has recently been reported to regulate the Wnt/beta-catenin pathway, which itself regulates cell fate and early development, in a redox-dependent manner. In this review, we describe the TRX family proteins and discuss in detail the similarities and differences between NRX and other TRX family proteins. Although NRX possesses a conserved TRX domain and a catalytic motif for oxidoreductase activity, its sequence homology to TRX is not as high as that of the close relatives of TRX. The sequence of NRX is more similar to that of tryparedoxin (TryX), a TRX family member originally identified in parasite trypanosomes. We also discuss the reported properties and potential physiologic roles of NRX.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Funato</LastName><ForeName>Yosuke</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Division of Cancer Genomics, Institute of Medical Science, University of Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Miki</LastName><ForeName>Hiroaki</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013045" MajorTopicYN="N">Species Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>209</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>6</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>9</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>6</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17567240</ArticleId><ArticleId IdType="doi">10.1089/ars.2007.1550</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><noCountry><name sortKey="Miki, Hiroaki" sort="Miki, Hiroaki" uniqKey="Miki H" first="Hiroaki" last="Miki">Hiroaki Miki</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Funato, Yosuke" sort="Funato, Yosuke" uniqKey="Funato Y" first="Yosuke" last="Funato">Yosuke Funato</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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