[Characterization of some thiol oxidoreductase family members].
Identifieur interne : 000689 ( Main/Exploration ); précédent : 000688; suivant : 000690[Characterization of some thiol oxidoreductase family members].
Auteurs : E G Varlamova ; M V Gol'Tiaev ; S V Novoselov ; V I Novoselov ; E E FecenkoSource :
- Molekuliarnaia biologiia [ 0026-8984 ]
Descripteurs français
- KwdFr :
- Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Glutathione peroxidase (composition chimique), Glutathione peroxidase (métabolisme), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Peroxirédoxines (composition chimique), Peroxirédoxines (métabolisme), Peroxyde d'hydrogène (métabolisme), Thiols (métabolisme), Thiorédoxines (composition chimique), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Glutarédoxines, Glutathione peroxidase, Oxidoreductases, Peroxirédoxines, Thiorédoxines.
- métabolisme : Glutarédoxines, Glutathione peroxidase, Oxidoreductases, Peroxirédoxines, Peroxyde d'hydrogène, Thiols, Thiorédoxines.
English descriptors
- KwdEn :
- Glutaredoxins (chemistry), Glutaredoxins (metabolism), Glutathione Peroxidase (chemistry), Glutathione Peroxidase (metabolism), Hydrogen Peroxide (metabolism), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Peroxiredoxins (chemistry), Peroxiredoxins (metabolism), Sulfhydryl Compounds (metabolism), Thioredoxins (chemistry), Thioredoxins (metabolism).
- MESH :
- chemical , chemistry : Glutaredoxins, Glutathione Peroxidase, Oxidoreductases, Peroxiredoxins, Thioredoxins.
- chemical , metabolism : Glutaredoxins, Glutathione Peroxidase, Hydrogen Peroxide, Oxidoreductases, Peroxiredoxins, Sulfhydryl Compounds, Thioredoxins.
Abstract
There are no doubt about the important role of free radicals and reactive oxygen species in the processes of cell activity. The disturbances of intracellular redox processes are often accompanied with the development of such common pathologies as diabetes, myocardial infarction, neurodegeneration, broncho-pulmonary diseases, cancer, etc. To date, there are a large number of antioxidant enzymes related to different redox biology systems, the key role among them is played by enzymes belong to the thiol oxidoreductases superfamily, which consists of thioredoxin, glutaredoxin, peroxiredoxin, protein disulfidizomeraz, glutathione peroxidase families, and a number of other proteins. In addition to the antioxidant function, thiol oxidoreductases display the ability to recycle of hydroperoxide to form specific disulfide bonds within and between proteins that significantly extends the range of their functionality. Therefore, biochemical characterization and elucidation of functional mechanisms of the superfamily proteins is a highly actual problem of redox biology.
DOI: 10.7868/s0026898413040149
PubMed: 24466746
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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The disturbances of intracellular redox processes are often accompanied with the development of such common pathologies as diabetes, myocardial infarction, neurodegeneration, broncho-pulmonary diseases, cancer, etc. To date, there are a large number of antioxidant enzymes related to different redox biology systems, the key role among them is played by enzymes belong to the thiol oxidoreductases superfamily, which consists of thioredoxin, glutaredoxin, peroxiredoxin, protein disulfidizomeraz, glutathione peroxidase families, and a number of other proteins. In addition to the antioxidant function, thiol oxidoreductases display the ability to recycle of hydroperoxide to form specific disulfide bonds within and between proteins that significantly extends the range of their functionality. Therefore, biochemical characterization and elucidation of functional mechanisms of the superfamily proteins is a highly actual problem of redox biology.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24466746</PMID><DateCompleted><Year>2014</Year><Month>03</Month><Day>11</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>12</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0026-8984</ISSN><JournalIssue CitedMedium="Print"><Volume>47</Volume><Issue>4</Issue><PubDate><MedlineDate>2013 Jul-Aug</MedlineDate></PubDate></JournalIssue><Title>Molekuliarnaia biologiia</Title><ISOAbbreviation>Mol Biol (Mosk)</ISOAbbreviation></Journal><ArticleTitle>[Characterization of some thiol oxidoreductase family members].</ArticleTitle><Pagination><MedlinePgn>568-82</MedlinePgn></Pagination><Abstract><AbstractText>There are no doubt about the important role of free radicals and reactive oxygen species in the processes of cell activity. The disturbances of intracellular redox processes are often accompanied with the development of such common pathologies as diabetes, myocardial infarction, neurodegeneration, broncho-pulmonary diseases, cancer, etc. To date, there are a large number of antioxidant enzymes related to different redox biology systems, the key role among them is played by enzymes belong to the thiol oxidoreductases superfamily, which consists of thioredoxin, glutaredoxin, peroxiredoxin, protein disulfidizomeraz, glutathione peroxidase families, and a number of other proteins. In addition to the antioxidant function, thiol oxidoreductases display the ability to recycle of hydroperoxide to form specific disulfide bonds within and between proteins that significantly extends the range of their functionality. Therefore, biochemical characterization and elucidation of functional mechanisms of the superfamily proteins is a highly actual problem of redox biology.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Varlamova</LastName><ForeName>E G</ForeName><Initials>EG</Initials></Author><Author ValidYN="Y"><LastName>Gol'tiaev</LastName><ForeName>M V</ForeName><Initials>MV</Initials></Author><Author ValidYN="Y"><LastName>Novoselov</LastName><ForeName>S V</ForeName><Initials>SV</Initials></Author><Author ValidYN="Y"><LastName>Novoselov</LastName><ForeName>V I</ForeName><Initials>VI</Initials></Author><Author ValidYN="Y"><LastName>Fecenko</LastName><ForeName>E E</ForeName><Initials>EE</Initials></Author></AuthorList><Language>rus</Language><PublicationTypeList><PublicationType UI="D004740">English Abstract</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType 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MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>1</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>1</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>3</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24466746</ArticleId><ArticleId IdType="doi">10.7868/s0026898413040149</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Fecenko, E E" sort="Fecenko, E E" uniqKey="Fecenko E" first="E E" last="Fecenko">E E Fecenko</name><name sortKey="Gol Tiaev, M V" sort="Gol Tiaev, M V" uniqKey="Gol Tiaev M" first="M V" last="Gol'Tiaev">M V Gol'Tiaev</name><name sortKey="Novoselov, S V" sort="Novoselov, S V" uniqKey="Novoselov S" first="S V" last="Novoselov">S V Novoselov</name><name sortKey="Novoselov, V I" sort="Novoselov, V I" uniqKey="Novoselov V" first="V I" last="Novoselov">V I Novoselov</name><name sortKey="Varlamova, E G" sort="Varlamova, E G" uniqKey="Varlamova E" first="E G" last="Varlamova">E G Varlamova</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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