Molecular views of redox regulation: three-dimensional structures of redox regulatory proteins and protein complexes.
Identifieur interne : 001063 ( Main/Exploration ); précédent : 001062; suivant : 001064Molecular views of redox regulation: three-dimensional structures of redox regulatory proteins and protein complexes.
Auteurs : J. Qin [États-Unis] ; Y. Yang ; A. Velyvis ; A. GronenbornSource :
- Antioxidants & redox signaling [ 1523-0864 ] ; 2000.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Conformation des protéines (MeSH), Glutarédoxines (MeSH), Glutathion (métabolisme), Humains (MeSH), Modèles moléculaires (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protéines (composition chimique), Protéines (métabolisme), Structure moléculaire (MeSH), Séquence d'acides aminés (MeSH), Thiorédoxines (composition chimique), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Protéines, Thiorédoxines.
- métabolisme : Glutathion, Protéines, Thiorédoxines.
- Animaux, Conformation des protéines, Glutarédoxines, Humains, Modèles moléculaires, Oxidoreductases, Oxydoréduction, Structure moléculaire, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Glutaredoxins (MeSH), Glutathione (metabolism), Humans (MeSH), Models, Molecular (MeSH), Molecular Structure (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Protein Conformation (MeSH), Proteins (chemistry), Proteins (metabolism), Thioredoxins (chemistry), Thioredoxins (metabolism).
- MESH :
- chemical , chemistry : Proteins, Thioredoxins.
- chemical , metabolism : Glutathione, Proteins, Thioredoxins.
- chemical : Glutaredoxins, Oxidoreductases.
- Amino Acid Sequence, Animals, Humans, Models, Molecular, Molecular Structure, Oxidation-Reduction, Protein Conformation.
Abstract
The last decade has witnessed the explosion of research on redox-controlled cellular and biochemical processes. Whereas the vast majority of these studies have centered on clinical, genetic, and biochemical aspects of redox signaling and regulation inside and outside the cell, a significant number of nuclear magnetic resonance (NMR) and crystallographic studies have been undertaken to obtain an atomic-level understanding of the mechanisms of the redox regulation. This review highlights the recent progress of three-dimensional structure determination of key proteins and protein complexes involved in redox regulation. An increased list of such class of protein structures and their complexes with ligands will provide invaluable insight into the molecular basis of redox-regulatory processes and may be useful for the future development of therapeutic agents for redox-related diseases.
DOI: 10.1089/ars.2000.2.4-827
PubMed: 11213487
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Velyvis</name></author><author><name sortKey="Gronenborn, A" sort="Gronenborn, A" uniqKey="Gronenborn A" first="A" last="Gronenborn">A. 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Whereas the vast majority of these studies have centered on clinical, genetic, and biochemical aspects of redox signaling and regulation inside and outside the cell, a significant number of nuclear magnetic resonance (NMR) and crystallographic studies have been undertaken to obtain an atomic-level understanding of the mechanisms of the redox regulation. This review highlights the recent progress of three-dimensional structure determination of key proteins and protein complexes involved in redox regulation. An increased list of such class of protein structures and their complexes with ligands will provide invaluable insight into the molecular basis of redox-regulatory processes and may be useful for the future development of therapeutic agents for redox-related diseases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11213487</PMID><DateCompleted><Year>2001</Year><Month>03</Month><Day>08</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1523-0864</ISSN><JournalIssue CitedMedium="Print"><Volume>2</Volume><Issue>4</Issue><PubDate><Year>2000</Year><Season>Winter</Season></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Molecular views of redox regulation: three-dimensional structures of redox regulatory proteins and protein complexes.</ArticleTitle><Pagination><MedlinePgn>827-40</MedlinePgn></Pagination><Abstract><AbstractText>The last decade has witnessed the explosion of research on redox-controlled cellular and biochemical processes. Whereas the vast majority of these studies have centered on clinical, genetic, and biochemical aspects of redox signaling and regulation inside and outside the cell, a significant number of nuclear magnetic resonance (NMR) and crystallographic studies have been undertaken to obtain an atomic-level understanding of the mechanisms of the redox regulation. This review highlights the recent progress of three-dimensional structure determination of key proteins and protein complexes involved in redox regulation. An increased list of such class of protein structures and their complexes with ligands will provide invaluable insight into the molecular basis of redox-regulatory processes and may be useful for the future development of therapeutic agents for redox-related diseases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Qin</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Structural Biology Program, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA. qinj@ccf.org</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Velyvis</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Gronenborn</LastName><ForeName>A</ForeName><Initials>A</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="D013487">Research Support, U.S. Gov't, P.H.S.</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 UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">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><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></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>80</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>2</Month><Day>24</Day><Hour>12</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>3</Month><Day>10</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>2</Month><Day>24</Day><Hour>12</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11213487</ArticleId><ArticleId IdType="doi">10.1089/ars.2000.2.4-827</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Ohio</li></region></list><tree><noCountry><name sortKey="Gronenborn, A" sort="Gronenborn, A" uniqKey="Gronenborn A" first="A" last="Gronenborn">A. Gronenborn</name><name sortKey="Velyvis, A" sort="Velyvis, A" uniqKey="Velyvis A" first="A" last="Velyvis">A. Velyvis</name><name sortKey="Yang, Y" sort="Yang, Y" uniqKey="Yang Y" first="Y" last="Yang">Y. Yang</name></noCountry><country name="États-Unis"><region name="Ohio"><name sortKey="Qin, J" sort="Qin, J" uniqKey="Qin J" first="J" last="Qin">J. Qin</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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